NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|194294540|ref|NP_057060|]
View 

sorting nexin-7 isoform a [Homo sapiens]

Protein Classification

PX and BAR domain-containing protein( domain architecture ID 10163608)

PX (Phox homology) and BAR (Bin/Amphiphysin/Rvs) domain-containing protein, similar to sorting nexins that are involved in regulating membrane traffic and protein sorting in the endosomal system

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
BAR_SNX7 cd07666
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 7; BAR domains are dimerization, lipid ...
 195-437 2.18e-174

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 7; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. The specific function of SNX7 is still unknown. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


:

Pssm-ID: 153350  Cd Length: 243  Bit Score: 487.87  E-value: 2.18e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540 195 HPTLTFNEDFKIFLTAQAWELSSHKKQGPGLLSRMGQTVRAVASSMRGVKNRPEEFMEMNNFIELFSQKINLIDKISQRI 274
Cdd:cd07666    1 HPTLTFNEDFKIFLTAQAWELSSHKKQGPGLLSRMGQTVKAVASSVRGVKNRPEEFTEMNEYVEAFSQKINVLDKISQRI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540 275 YKEEREYFDEMKEYGPIHILWSASEEDLVDTLKDVASCIDRCCKATEKRMSGLSEALLPVVHEYVLYSEMLMGVMKRRDQ 354
Cdd:cd07666   81 YKEQREYFEELKEYGPIYTLWSASEEELADSLKGMASCIDRCCKATDKRMKGLSEQLLPVIHEYVLYSETLMGVIKRRDQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540 355 IQAELDSKVEVLTYKKADTDLLPEEIGKLEDKVECANNALKADWERWKQNMQNDIKLAFTDMAEENIHYYEQCLATWESF 434
Cdd:cd07666  161 IQAELDSKVEALANKKADRDLLKEEIEKLEDKVECANNALKADWERWKQNMQTDLRSAFTDMAENNISYYEECLATWESF 240


                 ...
gi 194294540 435 LTS 437
Cdd:cd07666  241 LHS 243
PX_SNX7 cd07284
The phosphoinositide binding Phox Homology domain of Sorting Nexin 7; The PX domain is a ...
 96-211 3.99e-83

The phosphoinositide binding Phox Homology domain of Sorting Nexin 7; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Some SNXs are localized in early endosome structures such as clathrin-coated pits, while others are located in late structures of the endocytic pathway. SNX7 harbors a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain, similar to the sorting nexins SNX1-2, SNX4-6, SNX8, SNX30, and SNX32. Both domains have been shown to determine the specific membrane-targeting of SNX1. The specific function of SNX7 has yet to be elucidated.


:

Pssm-ID: 132817  Cd Length: 116  Bit Score: 251.05  E-value: 3.99e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540  96 LFITVDEPESHVTTIETFITYRIITKTSRGEFDSSEFEVRRRYQDFLWLKGKLEEAHPTLIIPPLPEKFIVKGMVERFND 175
Cdd:cd07284    1 IFITVDEPESHVTAIETFITYRVMTKTSRSEFDSSEFEVRRRYQDFLWLKGRLEEAHPTLIIPPLPEKFVMKGMVERFNE 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 194294540 176 DFIETRRKALHKFLNRIADHPTLTFNEDFKIFLTAQ 211
Cdd:cd07284   81 DFIETRRKALHKFLNRIADHPTLTFNEDFKIFLTAQ 116
 
Name Accession Description Interval E-value
BAR_SNX7 cd07666
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 7; BAR domains are dimerization, lipid ...
 195-437 2.18e-174

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 7; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. The specific function of SNX7 is still unknown. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153350  Cd Length: 243  Bit Score: 487.87  E-value: 2.18e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540 195 HPTLTFNEDFKIFLTAQAWELSSHKKQGPGLLSRMGQTVRAVASSMRGVKNRPEEFMEMNNFIELFSQKINLIDKISQRI 274
Cdd:cd07666    1 HPTLTFNEDFKIFLTAQAWELSSHKKQGPGLLSRMGQTVKAVASSVRGVKNRPEEFTEMNEYVEAFSQKINVLDKISQRI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540 275 YKEEREYFDEMKEYGPIHILWSASEEDLVDTLKDVASCIDRCCKATEKRMSGLSEALLPVVHEYVLYSEMLMGVMKRRDQ 354
Cdd:cd07666   81 YKEQREYFEELKEYGPIYTLWSASEEELADSLKGMASCIDRCCKATDKRMKGLSEQLLPVIHEYVLYSETLMGVIKRRDQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540 355 IQAELDSKVEVLTYKKADTDLLPEEIGKLEDKVECANNALKADWERWKQNMQNDIKLAFTDMAEENIHYYEQCLATWESF 434
Cdd:cd07666  161 IQAELDSKVEALANKKADRDLLKEEIEKLEDKVECANNALKADWERWKQNMQTDLRSAFTDMAENNISYYEECLATWESF 240


                 ...
gi 194294540 435 LTS 437
Cdd:cd07666  241 LHS 243
PX_SNX7 cd07284
The phosphoinositide binding Phox Homology domain of Sorting Nexin 7; The PX domain is a ...
 96-211 3.99e-83

The phosphoinositide binding Phox Homology domain of Sorting Nexin 7; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Some SNXs are localized in early endosome structures such as clathrin-coated pits, while others are located in late structures of the endocytic pathway. SNX7 harbors a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain, similar to the sorting nexins SNX1-2, SNX4-6, SNX8, SNX30, and SNX32. Both domains have been shown to determine the specific membrane-targeting of SNX1. The specific function of SNX7 has yet to be elucidated.


Pssm-ID: 132817  Cd Length: 116  Bit Score: 251.05  E-value: 3.99e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540  96 LFITVDEPESHVTTIETFITYRIITKTSRGEFDSSEFEVRRRYQDFLWLKGKLEEAHPTLIIPPLPEKFIVKGMVERFND 175
Cdd:cd07284    1 IFITVDEPESHVTAIETFITYRVMTKTSRSEFDSSEFEVRRRYQDFLWLKGRLEEAHPTLIIPPLPEKFVMKGMVERFNE 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 194294540 176 DFIETRRKALHKFLNRIADHPTLTFNEDFKIFLTAQ 211
Cdd:cd07284   81 DFIETRRKALHKFLNRIADHPTLTFNEDFKIFLTAQ 116
PX pfam00787
PX domain; PX domains bind to phosphoinositides.
 127-209 6.45e-26

PX domain; PX domains bind to phosphoinositides.


Pssm-ID: 459940  Cd Length: 84  Bit Score: 100.39  E-value: 6.45e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540  127 FDSSEFEVRRRYQDFLWLKGKLEEAHPTLIIPPLPEKFIVKgmveRFNDDFIETRRKALHKFLNRIADHPTLTFNEDFKI 206
Cdd:pfam00787   4 FSLEEWSVRRRYSDFVELHKKLLRKFPSVIIPPLPPKRWLG----RYNEEFIEKRRKGLEQYLQRLLQHPELRNSEVLLE 79


                  ...
gi 194294540  207 FLT 209
Cdd:pfam00787  80 FLE 82
PX smart00312
PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function ...
 102-209 7.38e-23

PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function present in phox proteins, PLD isoforms, a PI3K isoform.


Pssm-ID: 214610  Cd Length: 105  Bit Score: 92.79  E-value: 7.38e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540   102 EPESHVTTIETFITYRIITKTSrgefdSSEFEVRRRYQDFLWLKGKLEEAHPTLIIPPLPEKfIVKGMVERFNDDFIETR 181
Cdd:smart00312   3 EPEKIGDGKHYYYVIEIETKTG-----LEEWTVSRRYSDFLELHSKLKKHFPRSILPPLPGK-KLFGRLNNFSEEFIEKR 76

                           90       100
                   ....*....|....*....|....*....
gi 194294540   182 RKALHKFLNRIADHPTL-TFNEDFKIFLT 209
Cdd:smart00312  77 RRGLEKYLQSLLNHPELiNHSEVVLEFLE 105
COG5391 COG5391
Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function ...
 68-384 3.33e-16

Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function prediction only];


Pssm-ID: 227680 [Multi-domain]  Cd Length: 524  Bit Score: 80.61  E-value: 3.33e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540  68 NSFSPMMPTSPLSMINQIKFEDEPDLKDLFI--TVDEPESH---VTTIETFITYRIITKTSRGEFDSSEFE---VRRRYQ 139
Cdd:COG5391  101 FRSLRDMLSLLLPTSLQPPLSTSHTILDYFIssTVSNPQSLtllVDSRDKHTSYEIITVTNLPSFQLRESRplvVRRRYS 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540 140 DFLWLKGKLEEAHPTLIIPPLPEK-FIVKGMVERFNDDFIETRRKALHKFLNRIADHPTLT---FNEDFKIFLTaQAWEL 215
Cdd:COG5391  181 DFESLHSILIKLLPLCAIPPLPSKkSNSEYYGDRFSDEFIEERRQSLQNFLRRVSTHPLLSnykNSKSWESHST-LLSSF 259

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540 216 SSHKKQGPGLLSrmgqtvravASSMRGVKNRPEEFMEMNNFIelfSQKINLIDKIsqriykeereyfdeMKEYGPIHILw 295
Cdd:COG5391  260 IENRKSVPTPLS---------LDLTSTTQELDMERKELNEST---SKAIHNILSI--------------FSLFEKILIQ- 312

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540 296 SASEEDLVDTLKDVASCIDRcckatekRMSGLSEALLPVVHeYVLYSEMLMGVMkrrdQIQAELDSKVEVLTYKKADTDL 375
Cdd:COG5391  313 LESEEESLTRLLESLNNLLL-------LVLNFSGVFAKRLE-QNQNSILNEGVV----QAETLRSSLKELLTQLQDEIKS 380


                 ....*....
gi 194294540 376 LPEEIGKLE 384
Cdd:COG5391  381 RESLILTDS 389
 
Name Accession Description Interval E-value
BAR_SNX7 cd07666
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 7; BAR domains are dimerization, lipid ...
 195-437 2.18e-174

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 7; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. The specific function of SNX7 is still unknown. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153350  Cd Length: 243  Bit Score: 487.87  E-value: 2.18e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540 195 HPTLTFNEDFKIFLTAQAWELSSHKKQGPGLLSRMGQTVRAVASSMRGVKNRPEEFMEMNNFIELFSQKINLIDKISQRI 274
Cdd:cd07666    1 HPTLTFNEDFKIFLTAQAWELSSHKKQGPGLLSRMGQTVKAVASSVRGVKNRPEEFTEMNEYVEAFSQKINVLDKISQRI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540 275 YKEEREYFDEMKEYGPIHILWSASEEDLVDTLKDVASCIDRCCKATEKRMSGLSEALLPVVHEYVLYSEMLMGVMKRRDQ 354
Cdd:cd07666   81 YKEQREYFEELKEYGPIYTLWSASEEELADSLKGMASCIDRCCKATDKRMKGLSEQLLPVIHEYVLYSETLMGVIKRRDQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540 355 IQAELDSKVEVLTYKKADTDLLPEEIGKLEDKVECANNALKADWERWKQNMQNDIKLAFTDMAEENIHYYEQCLATWESF 434
Cdd:cd07666  161 IQAELDSKVEALANKKADRDLLKEEIEKLEDKVECANNALKADWERWKQNMQTDLRSAFTDMAENNISYYEECLATWESF 240


                 ...
gi 194294540 435 LTS 437
Cdd:cd07666  241 LHS 243
BAR_SNX7_30 cd07624
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins 7 and 30; BAR domains are dimerization, ...
 235-437 1.52e-107

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins 7 and 30; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. This subfamily consists of SNX7, SNX30, and similar proteins. The specific functions of SNX7 and SNX30 have not been elucidated. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153308  Cd Length: 200  Bit Score: 316.63  E-value: 1.52e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540 235 AVASSMRGVKNRPEEFMEMNNFIELFSQKINLIDKISQRIYKEEREYFDEMKEYGPIHILWSASEEDLVDTLKDVASCID 314
Cdd:cd07624    1 RNTSTMYLLKNRSPEFDKMNEYLTLFGEKLGTIERISQRIHKERIEYFDELKEYSPIFQLWSASETELAPLLEGVSSAVE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540 315 RCCKATEKRMSGLSEALLPVVHEYVLYSEMLMGVMKRRDQIQAELDSKVEVLTYKKADtdlLPEEIGKLEDKVECANNAL 394
Cdd:cd07624   81 RCTAALEVLLSDHEFVFLPPLREYLLYSDAVKDVLKRRDQFQIEYELSVEELNKKRLE---LLKEVEKLQDKLECANADL 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 194294540 395 KADWERWKQNMQNDIKLAFTDMAEENIHYYEQCLATWESFLTS 437
Cdd:cd07624  158 KADLERWKQNKRQDLKKILLDMAEKQIQYYEQCLAAWEEVLPA 200
BAR_SNX30 cd07667
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 30; BAR domains are dimerization, lipid ...
 195-435 4.89e-87

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 30; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. The specific function of SNX30 is still unknown. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153351  Cd Length: 240  Bit Score: 265.71  E-value: 4.89e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540 195 HPTLTFNEDFKIFLTAQawELSSHKKQGPGLLSRMGQTVRAVASSMRgVKNRPEEFMEMNNFIELFSQKINLIDKISQRI 274
Cdd:cd07667    1 HPVLSFNEHFNVFLTAK--DLNAYKKQGIALLSKMGESVKYVTGGYK-LRSRPLEFAAIGDYLDTFALKLGTIDRIAQRI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540 275 YKEEREYFDEMKEYGPIHILWSASEEDLVDTLKDVASCIDRCCKATEKRMSGLSEALLPVVHEYVLYSEMLMGVMKRRDQ 354
Cdd:cd07667   78 IKEEIEYLVELREYGPVYSTWSGLEGELAEPLEGVSACIGNCSTALEELTEDMTEDFLPVLREYILYSESMKNVLKKRDQ 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540 355 IQAELDSKVEVLTYKKADTDLLPEEIGKLEDKVECANNALKADWERWKQNMQNDIKLAFTDMAEENIHYYEQCLATWESF 434
Cdd:cd07667  158 VQAEYEAKLEAVALRKEERPKVPTDVEKCQDRVECFNADLKADMERWQNNKRQDFRQLLMGMADKNIQYYEKCLTAWESI 237


                 .
gi 194294540 435 L 435
Cdd:cd07667  238 I 238
PX_SNX7 cd07284
The phosphoinositide binding Phox Homology domain of Sorting Nexin 7; The PX domain is a ...
 96-211 3.99e-83

The phosphoinositide binding Phox Homology domain of Sorting Nexin 7; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Some SNXs are localized in early endosome structures such as clathrin-coated pits, while others are located in late structures of the endocytic pathway. SNX7 harbors a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain, similar to the sorting nexins SNX1-2, SNX4-6, SNX8, SNX30, and SNX32. Both domains have been shown to determine the specific membrane-targeting of SNX1. The specific function of SNX7 has yet to be elucidated.


Pssm-ID: 132817  Cd Length: 116  Bit Score: 251.05  E-value: 3.99e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540  96 LFITVDEPESHVTTIETFITYRIITKTSRGEFDSSEFEVRRRYQDFLWLKGKLEEAHPTLIIPPLPEKFIVKGMVERFND 175
Cdd:cd07284    1 IFITVDEPESHVTAIETFITYRVMTKTSRSEFDSSEFEVRRRYQDFLWLKGRLEEAHPTLIIPPLPEKFVMKGMVERFNE 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 194294540 176 DFIETRRKALHKFLNRIADHPTLTFNEDFKIFLTAQ 211
Cdd:cd07284   81 DFIETRRKALHKFLNRIADHPTLTFNEDFKIFLTAQ 116
PX_SNX7_30_like cd06860
The phosphoinositide binding Phox Homology domain of Sorting Nexins 7 and 30; The PX domain is ...
 96-211 1.50e-77

The phosphoinositide binding Phox Homology domain of Sorting Nexins 7 and 30; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Some SNXs are localized in early endosome structures such as clathrin-coated pits, while others are located in late structures of the endocytic pathway. This subfamily consists of SNX7, SNX30, and similar proteins. They harbor a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain, similar to the sorting nexins SNX1-2, SNX4-6, SNX8, and SNX32. Both domains have been shown to determine the specific membrane-targeting of SNX1. The specific function of the sorting nexins in this subfamily has yet to be elucidated.


Pssm-ID: 132770  Cd Length: 116  Bit Score: 236.85  E-value: 1.50e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540  96 LFITVDEPESHVTTIETFITYRIITKTSRGEFDSSEFEVRRRYQDFLWLKGKLEEAHPTLIIPPLPEKFIVKGMVERFND 175
Cdd:cd06860    1 LFITVDNPEKHVTTLETYITYRVTTKTTRSEFDSSEYSVRRRYQDFLWLRQKLEESHPTHIIPPLPEKHSVKGLLDRFSP 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 194294540 176 DFIETRRKALHKFLNRIADHPTLTFNEDFKIFLTAQ 211
Cdd:cd06860   81 EFVATRMRALHKFLNRIVEHPVLSFNEHLKVFLTAK 116
PX_SNX30 cd07283
The phosphoinositide binding Phox Homology domain of Sorting Nexin 30; The PX domain is a ...
 96-211 1.99e-53

The phosphoinositide binding Phox Homology domain of Sorting Nexin 30; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Some SNXs are localized in early endosome structures such as clathrin-coated pits, while others are located in late structures of the endocytic pathway. SNX30 harbors a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain, similar to the sorting nexins SNX1-2, SNX4-8, and SNX32. Both domains have been shown to determine the specific membrane-targeting of SNX1. The specific function of SNX30 has yet to be elucidated.


Pssm-ID: 132816  Cd Length: 116  Bit Score: 174.50  E-value: 1.99e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540  96 LFITVDEPESHVTTIETFITYRIITKTSRGEFDSSEFEVRRRYQDFLWLKGKLEEAHPTLIIPPLPEKFIVKGMVERFND 175
Cdd:cd07283    1 LFVTVDDPKKHVCTMETYITYRVTTKTTRTEFDLPEYSVRRRYQDFDWLRNKLEESQPTHLIPPLPEKFVVKGVVDRFSE 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 194294540 176 DFIETRRKALHKFLNRIADHPTLTFNEDFKIFLTAQ 211
Cdd:cd07283   81 EFVETRRKALDKFLKRIADHPVLSFNEHFNVFLTAK 116
PX_SNX1_2_like cd06859
The phosphoinositide binding Phox Homology domain of Sorting Nexins 1 and 2; The PX domain is ...
 96-211 2.96e-38

The phosphoinositide binding Phox Homology domain of Sorting Nexins 1 and 2; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. This subfamily consists of SNX1, SNX2, and similar proteins. They harbor a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain. Both domains have been shown to determine the specific membrane-targeting of SNX1. SNX1 and SNX2 are components of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi. The retromer consists of a cargo-recognition subcomplex and a subcomplex formed by a dimer of sorting nexins (SNX1 and/or SNX2), which ensures effcient cargo sorting by facilitating proper membrane localization of the cargo-recognition subcomplex.


Pssm-ID: 132769 [Multi-domain]  Cd Length: 114  Bit Score: 134.63  E-value: 2.96e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540  96 LFITVDEPESHVTTIETFITYRIITKTSRGEFDSSEFEVRRRYQDFLWLKGKLEEAHPTLIIPPLPEKFIVkGMVeRFND 175
Cdd:cd06859    1 FEISVTDPVKVGDGMSAYVVYRVTTKTNLPDFKKSEFSVLRRYSDFLWLYERLVEKYPGRIVPPPPEKQAV-GRF-KVKF 78

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 194294540 176 DFIETRRKALHKFLNRIADHPTLTFNEDFKIFLTAQ 211
Cdd:cd06859   79 EFIEKRRAALERFLRRIAAHPVLRKDPDFRLFLESD 114
BAR_SNX cd07596
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ...
 245-435 2.74e-33

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153280 [Multi-domain]  Cd Length: 218  Bit Score: 124.78  E-value: 2.74e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540 245 NRPEEFMEMNNFIELFSQKINLIDKISQRIYKEEREYFDEMKEYGPIHILWSASEED----LVDTLKDVASCIDRCCKAT 320
Cdd:cd07596    1 EEDQEFEEAKDYILKLEEQLKKLSKQAQRLVKRRRELGSALGEFGKALIKLAKCEEEvggeLGEALSKLGKAAEELSSLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540 321 EKRMSGLSEALLPVVHEYVLYSEMLMGVMKRRDQIQAELDSKVEVLTYKKA---------------------DTDLLPEE 379
Cdd:cd07596   81 EAQANQELVKLLEPLKEYLRYCQAVKETLDDRADALLTLQSLKKDLASKKAqleklkaapgikpakveeleeELEEAESA 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 194294540 380 IGKLEDKVECANNALKADWERWKQNMQNDIKLAFTDMAEENIHYYEQCLATWESFL 435
Cdd:cd07596  161 LEEARKRYEEISERLKEELKRFHEERARDLKAALKEFARLQVQYAEKIAEAWESLL 216
PX_Vps5p cd06861
The phosphoinositide binding Phox Homology domain of yeast sorting nexin Vps5p; The PX domain ...
 98-211 1.14e-31

The phosphoinositide binding Phox Homology domain of yeast sorting nexin Vps5p; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Vsp5p is the yeast counterpart of human SNX1 and is part of the retromer complex, which functions in the endosome-to-Golgi retrieval of vacuolar protein sorting receptor Vps10p, the Golgi-resident membrane protein A-ALP, and endopeptidase Kex2. The PX domain of Vps5p binds phosphatidylinositol-3-phosphate (PI3P). Similar to SNX1, Vps5p contains a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain. Both domains have been shown to determine the specific membrane-targeting of SNX1.


Pssm-ID: 132771  Cd Length: 112  Bit Score: 117.07  E-value: 1.14e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540  98 ITVDEPESHVTTIETFITYRIITKTSRGEFDSSEFEVRRRYQDFLWLKGKLEEAHPTLIIPPLPEKFIVKgmveRFNDDF 177
Cdd:cd06861    3 ITVGDPHKVGDLTSAHTVYTVRTRTTSPNFEVSSFSVLRRYRDFRWLYRQLQNNHPGVIVPPPPEKQSVG----RFDDNF 78

                         90       100       110
                 ....*....|....*....|....*....|....
gi 194294540 178 IETRRKALHKFLNRIADHPTLTFNEDFKIFLTAQ 211
Cdd:cd06861   79 VEQRRAALEKMLRKIANHPVLQKDPDFRLFLESE 112
PX_domain cd06093
The Phox Homology domain, a phosphoinositide binding module; The PX domain is a ...
 98-209 5.25e-27

The Phox Homology domain, a phosphoinositide binding module; The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to membranes. Proteins containing PX domains interact with PIs and have been implicated in highly diverse functions such as cell signaling, vesicular trafficking, protein sorting, lipid modification, cell polarity and division, activation of T and B cells, and cell survival. Many members of this superfamily bind phosphatidylinositol-3-phosphate (PI3P) but in some cases, other PIs such as PI4P or PI(3,4)P2, among others, are the preferred substrates. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction, as in the cases of p40phox, p47phox, and some sorting nexins (SNXs). The PX domain is conserved from yeast to humans and is found in more than 100 proteins. The majority of PX domain-containing proteins are SNXs, which play important roles in endosomal sorting.


Pssm-ID: 132768 [Multi-domain]  Cd Length: 106  Bit Score: 103.98  E-value: 5.25e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540  98 ITVDEPESHVTTIETFITYRIITKTSrgefDSSEFEVRRRYQDFLWLKGKLEEAHPTLIIPPLPEKFIVKgmveRFNDDF 177
Cdd:cd06093    2 VSIPDYEKVKDGGKKYVVYIIEVTTQ----GGEEWTVYRRYSDFEELHEKLKKKFPGVILPPLPPKKLFG----NLDPEF 73

                         90       100       110
                 ....*....|....*....|....*....|..
gi 194294540 178 IETRRKALHKFLNRIADHPTLTFNEDFKIFLT 209
Cdd:cd06093   74 IEERRKQLEQYLQSLLNHPELRNSEELKEFLE 105
PX_SNX_like cd06865
The phosphoinositide binding Phox Homology domain of SNX-like proteins; The PX domain is a ...
 98-211 3.72e-26

The phosphoinositide binding Phox Homology domain of SNX-like proteins; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Some SNXs are localized in early endosome structures such as clathrin-coated pits, while others are located in late structures of the endocytic pathway. This subfamily is composed of uncharacterized proteins, predominantly from plants, with similarity to sorting nexins. A few members show a similar domain architecture as a subfamily of sorting nexins, containing a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain. The PX-BAR structural unit is known to determine specific membrane localization.


Pssm-ID: 132775  Cd Length: 120  Bit Score: 102.50  E-value: 3.72e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540  98 ITVDEPESHVTTIE------TFITYRIITKTSRGEFDSSEFEVRRRYQDFLWLKGKLEEAHPTLIIPPLPEKFIVKGMVe 171
Cdd:cd06865    2 ITVSDPKKEQEPSRvplggpPYISYKVTTRTNIPSYTHGEFTVRRRFRDVVALADRLAEAYRGAFVPPRPDKSVVESQV- 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 194294540 172 RFNDDFIETRRKALHKFLNRIADHPTLTFNEDFKIFLTAQ 211
Cdd:cd06865   81 MQSAEFIEQRRVALEKYLNRLAAHPVIGLSDELRVFLTLQ 120
PX pfam00787
PX domain; PX domains bind to phosphoinositides.
 127-209 6.45e-26

PX domain; PX domains bind to phosphoinositides.


Pssm-ID: 459940  Cd Length: 84  Bit Score: 100.39  E-value: 6.45e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540  127 FDSSEFEVRRRYQDFLWLKGKLEEAHPTLIIPPLPEKFIVKgmveRFNDDFIETRRKALHKFLNRIADHPTLTFNEDFKI 206
Cdd:pfam00787   4 FSLEEWSVRRRYSDFVELHKKLLRKFPSVIIPPLPPKRWLG----RYNEEFIEKRRKGLEQYLQRLLQHPELRNSEVLLE 79


                  ...
gi 194294540  207 FLT 209
Cdd:pfam00787  80 FLE 82
PX_Atg24p cd06863
The phosphoinositide binding Phox Homology domain of yeast Atg24p, an autophagic degradation ...
 96-209 2.91e-25

The phosphoinositide binding Phox Homology domain of yeast Atg24p, an autophagic degradation protein; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. The yeast Atg24p is a sorting nexin (SNX) which is involved in membrane fusion events at the vacuolar surface during pexophagy. This is facilitated via binding of Atg24p to phosphatidylinositol 3-phosphate (PI3P) through its PX domain. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway.


Pssm-ID: 132773  Cd Length: 118  Bit Score: 99.67  E-value: 2.91e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540  96 LFITVDEP--ESHvTTIETFITYRIITKTSRGEFDSSEFEVRRRYQDFLWLKGKLEEAHPTLIIPPLPEKFIVKGMV-ER 172
Cdd:cd06863    1 LECLVSDPqkELD-GSSDTYISYLITTKTNLPSFSRKEFKVRRRYSDFVFLHECLSNDFPACVVPPLPDKHRLEYITgDR 79

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 194294540 173 FNDDFIETRRKALHKFLNRIADHPTLTFNEDFKIFLT 209
Cdd:cd06863   80 FSPEFITRRAQSLQRFLRRISLHPVLSQSKILHQFLE 116
PX_SNX2 cd07282
The phosphoinositide binding Phox Homology domain of Sorting Nexin 2; The PX domain is a ...
 98-208 8.60e-24

The phosphoinositide binding Phox Homology domain of Sorting Nexin 2; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX2 is a component of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi. The retromer consists of a cargo-recognition subcomplex and a subcomplex formed by a dimer of sorting nexins (SNX1 and/or SNX2), which ensures efficient cargo sorting by facilitating proper membrane localization of the cargo-recognition subcomplex. Similar to SNX1, SNX2 contains a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain. The PX domain of SNX2 preferentially binds phosphatidylinositol-3-phosphate (PI3P), but not PI(3,4,5)P3. Studies on mice deficient with SNX1 and/or SNX2 suggest that they provide an essential function in embryogenesis and are functionally redundant.


Pssm-ID: 132815  Cd Length: 124  Bit Score: 95.89  E-value: 8.60e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540  98 ITVDEPESHVTTIETFITYRIITKTSRGEFDSSEFEVRRRYQDFLWLKGKLEEA--HPTLIIPPLPEKFIVkGMV----- 170
Cdd:cd07282    3 IGVSDPEKVGDGMNAYMAYRVTTKTSLSMFSRSEFSVRRRFSDFLGLHSKLASKylHVGYIVPPAPEKSIV-GMTkvkvg 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 194294540 171 --ERFNDDFIETRRKALHKFLNRIADHPTLTFNEDFKIFL 208
Cdd:cd07282   82 keDSSSTEFVEKRRAALERYLQRTVKHPTLLQDPDLRQFL 121
PX smart00312
PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function ...
 102-209 7.38e-23

PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function present in phox proteins, PLD isoforms, a PI3K isoform.


Pssm-ID: 214610  Cd Length: 105  Bit Score: 92.79  E-value: 7.38e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540   102 EPESHVTTIETFITYRIITKTSrgefdSSEFEVRRRYQDFLWLKGKLEEAHPTLIIPPLPEKfIVKGMVERFNDDFIETR 181
Cdd:smart00312   3 EPEKIGDGKHYYYVIEIETKTG-----LEEWTVSRRYSDFLELHSKLKKHFPRSILPPLPGK-KLFGRLNNFSEEFIEKR 76

                           90       100
                   ....*....|....*....|....*....
gi 194294540   182 RKALHKFLNRIADHPTL-TFNEDFKIFLT 209
Cdd:smart00312  77 RRGLEKYLQSLLNHPELiNHSEVVLEFLE 105
PX_SNX9_18_like cd06862
The phosphoinositide binding Phox Homology domain of Sorting Nexins 9 and 18; The PX domain is ...
 98-213 9.94e-22

The phosphoinositide binding Phox Homology domain of Sorting Nexins 9 and 18; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. This subfamily consists of SNX9, SNX18, and similar proteins. They contain an N-terminal Src Homology 3 (SH3) domain, a PX domain, and a C-terminal Bin/Amphiphysin/Rvs (BAR) domain. SNX9 is localized to plasma membrane endocytic sites and acts primarily in clathrin-mediated endocytosis, while SNX18 is localized to peripheral endosomal structures, and acts in a trafficking pathway that is clathrin-independent but relies on AP-1 and PACS1.


Pssm-ID: 132772  Cd Length: 125  Bit Score: 90.07  E-value: 9.94e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540  98 ITVDEP--ESHVTTIETFITYRII-TKTSRgefdssefEVRRRYQDFLWLKGKLEEAHPTLIIPPLPEKFIVKgmveRFN 174
Cdd:cd06862    3 CTVTNPkkESKFKGLKSFIAYQITpTHTNV--------TVSRRYKHFDWLYERLVEKYSCIAIPPLPEKQVTG----RFE 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 194294540 175 DDFIETRRKALHKFLNRIADHPTLTFNEDFKIFLTAQ---AW 213
Cdd:cd06862   71 EDFIEKRRERLELWMNRLARHPVLSQSEVFRHFLTCTdekDW 112
PX_SNX1 cd07281
The phosphoinositide binding Phox Homology domain of Sorting Nexin 1; The PX domain is a ...
 96-208 1.73e-20

The phosphoinositide binding Phox Homology domain of Sorting Nexin 1; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX1 is both membrane associated and a cytosolic protein that exists as a tetramer in protein complexes. It can associate reversibly with membranes of the endosomal compartment, thereby coating these vesicles. SNX1 is a component of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi. The retromer consists of a cargo-recognition subcomplex and a subcomplex formed by a dimer of sorting nexins (SNX1 and/or SNX2), which ensures efficient cargo sorting by facilitating proper membrane localization of the cargo-recognition subcomplex. SNX1 contains a Bin/Amphiphysin/Rvs (BAR) domain C-terminal to the PX domain. The PX domain of SNX1 specifically binds phosphatidylinositol-3-phosphate (PI3P) and PI(3,5)P2, while the BAR domain detects membrane curvature. Both domains help determine the specific membrane-targeting of SNX1, which is localized to a microdomain in early endosomes where it regulates cation-independent mannose-6-phosphate receptor retrieval to the trans Golgi network.


Pssm-ID: 132814  Cd Length: 124  Bit Score: 86.65  E-value: 1.73e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540  96 LFITVDEPESHVTTIETFITYRIITKTSRGEFDSSEFEVRRRYQDFLWLKGKLEEAHPT--LIIPPLPEKFIVkGMV--- 170
Cdd:cd07281    1 LKVSITDPEKIGDGMNAYVVYKVTTQTSLLMFRSKHFTVKRRFSDFLGLYEKLSEKHSQngFIVPPPPEKSLI-GMTkvk 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 194294540 171 ----ERFNDDFIETRRKALHKFLNRIADHPTLTFNEDFKIFL 208
Cdd:cd07281   80 vgkeDSSSAEFLERRRAALERYLQRIVSHPSLLQDPDVREFL 121
PX_SNX4 cd06864
The phosphoinositide binding Phox Homology domain of Sorting Nexin 4; The PX domain is a ...
 98-209 3.31e-20

The phosphoinositide binding Phox Homology domain of Sorting Nexin 4; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX4 is involved in recycling traffic from the sorting endosome (post-Golgi endosome) back to the late Golgi. It shows a similar domain architecture as SNX1-2, among others, containing a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain. SNX4 is implicated in the regulation of plasma membrane receptor trafficking and interacts with receptors for EGF, insulin, platelet-derived growth factor and the long form of the leptin receptor.


Pssm-ID: 132774  Cd Length: 129  Bit Score: 86.27  E-value: 3.31e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540  98 ITVDEPE-----SHVTTIETFITYRIITKTSRGEFDSSEFE----VRRRYQDFLWLKGKLEEAHPTLIIPPLPEK----F 164
Cdd:cd06864    3 ITVTEAEkrtggSAMNLKETYTVYLIETKIVEHESEEGLSKklssLWRRYSEFELLRNYLVVTYPYVIVPPLPEKramfM 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 194294540 165 IVKGMVERFNDDFIETRRKALHKFLNRIADHPTLTFNEDFKIFLT 209
Cdd:cd06864   83 WQKLSSDTFDPDFVERRRAGLENFLLRVAGHPELCQDKIFLEFLT 127
PX_SNX3_like cd06894
The phosphoinositide binding Phox Homology domain of Sorting Nexin 3 and related proteins; The ...
 96-212 4.24e-19

The phosphoinositide binding Phox Homology domain of Sorting Nexin 3 and related proteins; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. This subfamily is composed of SNX3, SNX12, and fungal Grd19. Grd19 is involved in the localization of late Golgi membrane proteins in yeast. SNX3/Grp19 associates with the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi, and functions as a cargo-specific adaptor for the retromer.


Pssm-ID: 132804  Cd Length: 123  Bit Score: 82.89  E-value: 4.24e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540  96 LFITVDEPESHVTTIETFITYRIITKTSRGEFDSSEFEVRRRYQDFLWLKGKLEEaHPTLIIPPLPEKFIVKGMVER--- 172
Cdd:cd06894    2 LEIDVVNPQTHGVGKKRFTDYEVRMRTNLPVFKKKESSVRRRYSDFEWLRSELER-DSKIVVPPLPGKALKRQLPFRgdd 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 194294540 173 --FNDDFIETRRKALHKFLNRIADHPTLTFNEDFKIFLTAQA 212
Cdd:cd06894   81 giFEEEFIEERRKGLETFINKVAGHPLAQNEKCLHMFLQEET 122
PX_SNX3 cd07293
The phosphoinositide binding Phox Homology domain of Sorting Nexin 3; The PX domain is a ...
 96-202 1.33e-18

The phosphoinositide binding Phox Homology domain of Sorting Nexin 3; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX3 associates with early endosomes through a PX domain-mediated interaction with phosphatidylinositol-3-phosphate (PI3P). It associates with the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi, and functions as a cargo-specific adaptor for the retromer. SNX3 is required for the formation of multivesicular bodies, which function as transport intermediates to late endosomes. It also promotes cell surface expression of the amiloride-sensitive epithelial Na+ channel (ENaC), which is critical in sodium homeostasis and maintenance of extracellular fluid volume.


Pssm-ID: 132826  Cd Length: 123  Bit Score: 81.58  E-value: 1.33e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540  96 LFITVDEPESHVTTIETFITYRIITKTSRGEFDSSEFEVRRRYQDFLWLKGKLEEaHPTLIIPPLPEKFIVKGMVER--- 172
Cdd:cd07293    2 LEIDVTNPQTVGVGRGRFTTYEIRLKTNLPIFKLKESTVRRRYSDFEWLRSELER-ESKVVVPPLPGKALFRQLPFRgdd 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 194294540 173 --FNDDFIETRRKALHKFLNRIADHPtLTFNE 202
Cdd:cd07293   81 giFDDSFIEERKQGLEQFLNKVAGHP-LAQNE 111
PX_Grd19 cd07295
The phosphoinositide binding Phox Homology domain of fungal Grd19; The PX domain is a ...
 96-213 5.66e-17

The phosphoinositide binding Phox Homology domain of fungal Grd19; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Grd19 is involved in the localization of late Golgi membrane proteins in yeast. Grp19 associates with the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi, and functions as a cargo-specific adaptor for the retromer.


Pssm-ID: 132828  Cd Length: 116  Bit Score: 76.77  E-value: 5.66e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540  96 LFITVDEPESHVTTIETFITYRIITKTSRGEFDSSEFEVRRRYQDFLWLKGKLEEAHPTLIIPPLPEKFivkgMVERFND 175
Cdd:cd07295    2 LEIEVRNPKTHGIGRGMFTDYEIVCRTNIPAFKLRVSSVRRRYSDFEYFRDILERESPRVMIPPLPGKI----FTNRFSD 77

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 194294540 176 DFIETRRKALHKFLNRIADHPTL-TFNEDFKIFLTAQAW 213
Cdd:cd07295   78 EVIEERRQGLETFLQSVAGHPLLqTGSKVLAAFLQDPKF 116
PX_SNX8_Mvp1p_like cd06866
The phosphoinositide binding Phox Homology domain of Sorting Nexin 8 and yeast Mvp1p; The PX ...
 133-210 6.56e-17

The phosphoinositide binding Phox Homology domain of Sorting Nexin 8 and yeast Mvp1p; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Some SNXs are localized in early endosome structures such as clathrin-coated pits, while others are located in late structures of the endocytic pathway. SNX8 and the yeast counterpart Mvp1p are involved in sorting and delivery of late-Golgi proteins, such as carboxypeptidase Y, to vacuoles.


Pssm-ID: 132776  Cd Length: 105  Bit Score: 76.11  E-value: 6.56e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 194294540 133 EVRRRYQDFLWLKGKLEEAHPTLIIPPLPEKFIVKGMverfNDDFIETRRKALHKFLNRIADHPTLTFNEDFKIFLTA 210
Cdd:cd06866   31 TVYRRYSDFVWLHEYLLKRYPYRMVPALPPKRIGGSA----DREFLEARRRGLSRFLNLVARHPVLSEDELVRTFLTE 104
PX_SNX41_42 cd06867
The phosphoinositide binding Phox Homology domain of fungal Sorting Nexins 41 and 42; The PX ...
 105-208 8.94e-17

The phosphoinositide binding Phox Homology domain of fungal Sorting Nexins 41 and 42; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Some SNXs are localized in early endosome structures such as clathrin-coated pits, while others are located in late structures of the endocytic pathway. SNX41 and SNX42 (also called Atg20p) form dimers with SNX4, and are required in protein recycling from the sorting endosome (post-Golgi endosome) back to the late Golgi in yeast.


Pssm-ID: 132777  Cd Length: 112  Bit Score: 75.75  E-value: 8.94e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540 105 SHVTTIETFITYRIITKTSrgefdssefEVRRRYQDFLWLKGKLEEAHPTLIIPPLPEK-----FIVKGMVERFNDDFIE 179
Cdd:cd06867   10 SSEGGSGSYIVYVIRLGGS---------EVKRRYSEFESLRKNLTRLYPTLIIPPIPEKhslkdYAKKPSKAKNDAKIIE 80

                         90       100
                 ....*....|....*....|....*....
gi 194294540 180 TRRKALHKFLNRIADHPTLTFNEDFKIFL 208
Cdd:cd06867   81 RRKRMLQRFLNRCLQHPILRNDIVFQKFL 109
COG5391 COG5391
Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function ...
 68-384 3.33e-16

Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function prediction only];


Pssm-ID: 227680 [Multi-domain]  Cd Length: 524  Bit Score: 80.61  E-value: 3.33e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540  68 NSFSPMMPTSPLSMINQIKFEDEPDLKDLFI--TVDEPESH---VTTIETFITYRIITKTSRGEFDSSEFE---VRRRYQ 139
Cdd:COG5391  101 FRSLRDMLSLLLPTSLQPPLSTSHTILDYFIssTVSNPQSLtllVDSRDKHTSYEIITVTNLPSFQLRESRplvVRRRYS 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540 140 DFLWLKGKLEEAHPTLIIPPLPEK-FIVKGMVERFNDDFIETRRKALHKFLNRIADHPTLT---FNEDFKIFLTaQAWEL 215
Cdd:COG5391  181 DFESLHSILIKLLPLCAIPPLPSKkSNSEYYGDRFSDEFIEERRQSLQNFLRRVSTHPLLSnykNSKSWESHST-LLSSF 259

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540 216 SSHKKQGPGLLSrmgqtvravASSMRGVKNRPEEFMEMNNFIelfSQKINLIDKIsqriykeereyfdeMKEYGPIHILw 295
Cdd:COG5391  260 IENRKSVPTPLS---------LDLTSTTQELDMERKELNEST---SKAIHNILSI--------------FSLFEKILIQ- 312

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540 296 SASEEDLVDTLKDVASCIDRcckatekRMSGLSEALLPVVHeYVLYSEMLMGVMkrrdQIQAELDSKVEVLTYKKADTDL 375
Cdd:COG5391  313 LESEEESLTRLLESLNNLLL-------LVLNFSGVFAKRLE-QNQNSILNEGVV----QAETLRSSLKELLTQLQDEIKS 380


                 ....*....
gi 194294540 376 LPEEIGKLE 384
Cdd:COG5391  381 RESLILTDS 389
PX_SNX18 cd07286
The phosphoinositide binding Phox Homology domain of Sorting Nexin 18; The PX domain is a ...
 99-221 5.19e-16

The phosphoinositide binding Phox Homology domain of Sorting Nexin 18; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX18, like SNX9, contains an N-terminal Src Homology 3 (SH3) domain, a PX domain, and a C-terminal Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature. The PX-BAR structural unit helps determine specific membrane localization. SNX18 is localized to peripheral endosomal structures, and acts in a trafficking pathway that is clathrin-independent but relies on AP-1 and PACS1.


Pssm-ID: 132819  Cd Length: 127  Bit Score: 74.32  E-value: 5.19e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540  99 TVDEP--ESHVTTIETFITYRIITKtsrgefdSSEFEVRRRYQDFLWLKGKLEEAHPTLIIPPLPEKfivkGMVERFNDD 176
Cdd:cd07286    4 TIDDPtkQTKFKGMKSYISYKLVPS-------HTGLQVHRRYKHFDWLYARLAEKFPVISVPHIPEK----QATGRFEED 72

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 194294540 177 FIETRRKALHKFLNRIADHPTLTFNEDFKIFLTA-----QAWELSSHKKQ 221
Cdd:cd07286   73 FISKRRKGLIWWMDHMCSHPVLARCDAFQHFLTCpstdeKAWKQGKRKAE 122
PX_SNX10 cd06898
The phosphoinositide binding Phox Homology domain of Sorting Nexin 10; The PX domain is a ...
 98-211 9.73e-16

The phosphoinositide binding Phox Homology domain of Sorting Nexin 10; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Some SNXs are localized in early endosome structures such as clathrin-coated pits, while others are located in late structures of the endocytic pathway. SNX10 may be involved in the regulation of endosome homeostasis. Its expression induces the formation of giant vacuoles in mammalian cells.


Pssm-ID: 132808  Cd Length: 113  Bit Score: 73.13  E-value: 9.73e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540  98 ITVDEPESHVTTIET-FITYRIITKTSRGEFDSSEFEVRRRYQDFLWLKGKLEEAHPTLIIPPLPEkfivKGMVERFND- 175
Cdd:cd06898    2 VEVRDPRTHKEDDWGsYTDYEIFLHTNSMCFTLKTSCVRRRYSEFVWLRNRLQKNALLIQLPSLPP----KNLFGRFNNe 77

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 194294540 176 DFIETRRKALHKFLNRIADHPTLTFNEDFKIFLTAQ 211
Cdd:cd06898   78 GFIEERQQGLQDFLEKVLQTPLLLSDSRLHLFLQTQ 113
PX_SNX12 cd07294
The phosphoinositide binding Phox Homology domain of Sorting Nexin 12; The PX domain is a ...
 96-212 3.97e-15

The phosphoinositide binding Phox Homology domain of Sorting Nexin 12; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Some SNXs are localized in early endosome structures such as clathrin-coated pits, while others are located in late structures of the endocytic pathway. The specific function of SNX12 has yet to be elucidated.


Pssm-ID: 132827  Cd Length: 132  Bit Score: 72.00  E-value: 3.97e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540  96 LFITVDEPESHVTTIETFITYRIITKTSRGEFDSSEFEVRRRYQDFLWLKGKLEEaHPTLIIPPLPEKFIVKGMVER--- 172
Cdd:cd07294    4 LEIDIFNPQTVGVGRNRFTTYEVRMRTNLPIFKLKESCVRRRYSDFEWLKNELER-DSKIVVPPLPGKALKRQLPFRgde 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 194294540 173 --FNDDFIETRRKALHKFLNRIADHPTLTFNEDFKIFLTAQA 212
Cdd:cd07294   83 giFEESFIEERRQGLEQFINKIAGHPLAQNERCLHMFLQDET 124
PX_SNX5 cd07291
The phosphoinositide binding Phox Homology domain of Sorting Nexin 5; The PX domain is a ...
 114-208 5.53e-11

The phosphoinositide binding Phox Homology domain of Sorting Nexin 5; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX5, abundantly expressed in macrophages, regulates macropinocytosis, a process that enables cells to internalize large amounts of external solutes. It may also be a component of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi, acting as a mammalian equivalent of yeast Vsp17p. It also binds the Fanconi anaemia complementation group A protein (FANCA). SNX5 harbors a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain, similar to other sorting nexins including SNX1-2. The PX-BAR structural unit helps determine the specific membrane-targeting of some SNXs. The PX domain of SNX5 binds phosphatidylinositol-3-phosphate (PI3P) and PI(3,4)P2. SNX5 is localized to a subdomain of early endosome and is recruited to the plasma membrane following EGF stimulation and elevation of PI(3,4)P2 levels.


Pssm-ID: 132824  Cd Length: 141  Bit Score: 60.46  E-value: 5.53e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540 114 ITYRIITKTSRGEFDSSEFEVRRRYQDFLWLKGKLEEA--HPTLIIPPLPEKFIVKGMVERFN-----------DDFIET 180
Cdd:cd07291   17 VKFTVHTKTTLPSFQSPDFSVTRQHEDFIWLHDALIETedYAGLIIPPAPPKPDFDGPREKMQklgegegsmtkEEFAKM 96

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 194294540 181 RRK-------------ALHK-FLNRIADHPTLTFNEDFKIFL 208
Cdd:cd07291   97 KQEleaeylavfkktvQVHEvFLQRLSSHPSLSKDRNFHIFL 138
PX_YPT35 cd07280
The phosphoinositide binding Phox Homology domain of the fungal protein YPT35; The PX domain ...
 113-196 1.49e-09

The phosphoinositide binding Phox Homology domain of the fungal protein YPT35; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. This subfamily is composed of YPT35 proteins from the fungal subkingdom Dikarya. The PX domain is involved in targeting of proteins to PI-enriched membranes, and may also be involved in protein-protein interaction. The PX domain of YPT35 binds to phosphatidylinositol 3-phosphate (PI3P). It also serves as a protein interaction domain, binding to members of the Yip1p protein family, which localize to the ER and Golgi. YPT35 is mainly associated with endosomes and together with Yip1p proteins, may be involved in a specific function in the endocytic pathway.


Pssm-ID: 132813  Cd Length: 120  Bit Score: 55.41  E-value: 1.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540 113 FITYRIITKTSrgEFDSSEFEVRRRYQDFLWLKGKLEEAHPT---LIIPPLPEKFIVKGMVERFNDDFIETRRKALHKFL 189
Cdd:cd07280   22 YVVWKITIETK--DLIGSSIVAYKRYSEFVQLREALLDEFPRhkrNEIPQLPPKVPWYDSRVNLNKAWLEKRRRGLQYFL 99


                 ....*..
gi 194294540 190 NRIADHP 196
Cdd:cd07280  100 NCVLLNP 106
PX_SNARE cd06897
The phosphoinositide binding Phox Homology domain of SNARE proteins from fungi; The PX domain ...
 112-208 6.39e-09

The phosphoinositide binding Phox Homology domain of SNARE proteins from fungi; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. This subfamily is composed of fungal proteins similar to Saccharomyces cerevisiae Vam7p. They contain an N-terminal PX domain and a C-terminal SNARE domain. The SNARE (Soluble NSF attachment protein receptor) family of proteins are integral membrane proteins that serve as key factors for vesicular trafficking. Vam7p is anchored at the vacuolar membrane through the specific interaction of its PX domain with phosphatidylinositol-3-phosphate (PI3P) present in bilayers. It plays an essential role in vacuole fusion. The PX domain is involved in targeting of proteins to PI-enriched membranes, and may also be involved in protein-protein interaction.


Pssm-ID: 132807  Cd Length: 108  Bit Score: 53.43  E-value: 6.39e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540 112 TFITYRIITKTSRGEFdssefEVRRRYQDFLWLKGKLEEAHPTLIIPPLPEKFIVKGMVErfNDDFIETRRKALHKFLNR 191
Cdd:cd06897   14 PYTVYNIQVRLPLRSY-----TVSRRYSEFVALHKQLESEVGIEPPYPLPPKSWFLSTSS--NPKLVEERRVGLEAFLRA 86

                         90
                 ....*....|....*....
gi 194294540 192 IADHPTLTFNED--FKIFL 208
Cdd:cd06897   87 LLNDEDSRWRNSpaVKEFL 105
BAR_SNX4 cd07622
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 4; BAR domains are dimerization, lipid ...
 234-437 1.46e-08

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 4; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. SNX4 is involved in recycling traffic from the sorting endosome (post-Golgi endosome) back to the late Golgi. It is also implicated in the regulation of plasma membrane receptor trafficking and interacts with receptors for EGF, insulin, platelet-derived growth factor and leptin. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153306  Cd Length: 201  Bit Score: 54.70  E-value: 1.46e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540 234 RAVASSMRGvKNRPEEFMEMNNFIELFSQKINLIDKISQRIykEEREYFDEM--KEYGPIHILWSASEEDLVDTLKDVAS 311
Cdd:cd07622    1 KALNASFRL-RNPDKRFEDLKNYSDELQTNLNNLLKVRARL--AERLYGVYKihANYGRVFSEWSAIEKEMGDGLQKAGH 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540 312 CIDRCCKATEkrmSGL--SEALLPVVHEYVLYSEMLMGVMKRRDQIQAELDSKVEVLTYKKADTdllpEEigKLEDKVEC 389
Cdd:cd07622   78 YMDSYAASID---NGLedEELIADQLKEYLFFADSLRAVCKKHELLQYDLEKAEDALANKKQQG----EE--AVKEAKDE 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 194294540 390 ANNALKA---DWERWKQNMQNDIKLAFTDMAEENIHYYEQCLATWESFLTS 437
Cdd:cd07622  149 LNEFVKKaleDVERFKKQKVRDLKEILISYAKLQIKLAKKGLQTWTNIKEC 199
PX_SNX5_like cd06892
The phosphoinositide binding Phox Homology domain of Sorting Nexins 5 and 6; The PX domain is ...
 120-208 2.52e-08

The phosphoinositide binding Phox Homology domain of Sorting Nexins 5 and 6; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Members of this subfamily include SNX5, SNX6, and similar proteins. They contain a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain, similar to other sorting nexins including SNX1-2. The PX-BAR structural unit helps determine the specific membrane-targeting of some SNXs. SNX5 and SNX6 may be components of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi, acting as a mammalian equivalent of yeast Vsp17p.


Pssm-ID: 132802  Cd Length: 141  Bit Score: 52.82  E-value: 2.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540 120 TKTSRGEFDSSEFEVRRRYQDFLWLKGKLEEA--HPTLIIPPLP---------EKFIVKG-------------MVERFND 175
Cdd:cd06892   23 TKTTLPTFQKPEFSVTRQHEEFVWLHDTLVENedYAGLIIPPAPpkpdfdasrEKLQKLGegegsmtkeefekMKQELEA 102

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 194294540 176 DFIETRRK--ALHK-FLNRIADHPTLTFNEDFKIFL 208
Cdd:cd06892  103 EYLAIFKKtvAMHEvFLRRLASHPVLRNDANFRVFL 138
PX_SNX20_21_like cd07279
The phosphoinositide binding Phox Homology domain of Sorting Nexins 20 and 21; The PX domain ...
 99-209 2.96e-08

The phosphoinositide binding Phox Homology domain of Sorting Nexins 20 and 21; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. This subfamily consists of SNX20, SNX21, and similar proteins. SNX20 interacts with P-Selectin glycoprotein ligand-1 (PSGL-1), a surface-expressed mucin that acts as a ligand for the selectin family of adhesion proteins. It may function in the sorting and cycling of PSGL-1 into endosomes. SNX21, also called SNX-L, is distinctly and highly-expressed in fetal liver and may be involved in protein sorting and degradation during embryonic liver development.


Pssm-ID: 132812  Cd Length: 112  Bit Score: 51.56  E-value: 2.96e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540  99 TVDEPESHvttietFITYRIITKTSrGEFDSSEFEVRRRYQDFLWLKGKLEEAHPTLIipplpEK--FIVKGMVERFNDD 176
Cdd:cd07279   10 TVKEGEKK------YVVYQLAVVQT-GDPDTQPAFIERRYSDFLKLYKALRKQHPQLM-----AKvsFPRKVLMGNFSSE 77

                         90       100       110
                 ....*....|....*....|....*....|...
gi 194294540 177 FIETRRKALHKFLNRIADHPTLTFNEDFKIFLT 209
Cdd:cd07279   78 LIAERSRAFEQFLGHILSIPNLRDSKAFLDFLQ 110
PX_CISK cd06870
The phosphoinositide binding Phox Homology Domain of Cytokine-Independent Survival Kinase; The ...
 128-210 5.79e-08

The phosphoinositide binding Phox Homology Domain of Cytokine-Independent Survival Kinase; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Cytokine-independent survival kinase (CISK), also called Serum- and Glucocorticoid-induced Kinase 3 (SGK3), plays a role in cell growth and survival. It is expressed in most tissues and is most abundant in the embryo and adult heart and spleen. It was originally discovered in a screen for antiapoptotic genes. It phosphorylates and inhibits the proapoptotic proteins, Bad and FKHRL1. CISK/SGK3 also regulates many transporters, ion channels, and receptors. It plays a critical role in hair follicle morphogenesis and hair cycling. N-terminal to a catalytic kinase domain, CISK contains a PX domain which binds highly phosphorylated PIs, directs membrane localization, and regulates the enzyme's activity.


Pssm-ID: 132780  Cd Length: 109  Bit Score: 50.87  E-value: 5.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540 128 DSSEFEVRRRYQDFLWLKGKLEEAHPTLIIPpLPEKfivKGMVERFNDDFIETRRKALHKFLNRIADHPTLTFNEDFKIF 207
Cdd:cd06870   30 GRSSWFVFRRYAEFDKLYESLKKQFPASNLK-IPGK---RLFGNNFDPDFIKQRRAGLDEFIQRLVSDPKLLNHPDVRAF 105


                 ...
gi 194294540 208 LTA 210
Cdd:cd06870  106 LQM 108
PX_SNX9 cd07285
The phosphoinositide binding Phox Homology domain of Sorting Nexin 9; The PX domain is a ...
 110-221 7.32e-08

The phosphoinositide binding Phox Homology domain of Sorting Nexin 9; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX9, also known as SH3PX1, is a cytosolic protein that interacts with proteins associated with clathrin-coated pits such as Cdc-42-associated tyrosine kinase 2 (ACK2). It contains an N-terminal Src Homology 3 (SH3) domain, a PX domain, and a C-terminal Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature. The PX-BAR structural unit helps determine specific membrane localization. Through its SH3 domain, SNX9 binds class I polyproline sequences found in dynamin 1/2 and the WASP/N-WASP actin regulators. SNX9 is localized to plasma membrane endocytic sites and acts primarily in clathrin-mediated endocytosis. Its array of interacting partners suggests that SNX9 functions at the interface between endocytosis and actin cytoskeletal organization.


Pssm-ID: 132818  Cd Length: 126  Bit Score: 50.79  E-value: 7.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540 110 IETFITYRII-TKTSRgefdssefEVRRRYQDFLWLKGKLEEAHPTLI-IPPLPEKFIVKgmveRFNDDFIETRRKALHK 187
Cdd:cd07285   17 LKSYIEYQLTpTNTNR--------SVNHRYKHFDWLYERLLVKFGLAIpIPSLPDKQVTG----RFEEEFIKMRMERLQA 84

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 194294540 188 FLNRIADHPTLTFNEDFKIFLT---AQAWELSSHKKQ 221
Cdd:cd07285   85 WMTRMCRHPVISESEVFQQFLNfrdEKEWKTGKRKAE 121
PX_MONaKA cd06871
The phosphoinositide binding Phox Homology domain of Modulator of Na,K-ATPase; The PX domain ...
 119-209 1.17e-07

The phosphoinositide binding Phox Homology domain of Modulator of Na,K-ATPase; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. MONaKA (Modulator of Na,K-ATPase) binds the plasma membrane ion transporter, Na,K-ATPase, and modulates its enzymatic and ion pump activities. It modulates brain Na,K-ATPase and may be involved in regulating electrical excitability and synaptic transmission. MONaKA contains an N-terminal PX domain and a C-terminal catalytic kinase domain. The PX domain interacts with PIs and plays a role in targeting proteins to PI-enriched membranes.


Pssm-ID: 132781  Cd Length: 120  Bit Score: 50.05  E-value: 1.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540 119 ITKTSRGEFDSSEFEVRRRYQDFLWLKGKLEEAHPTLIIPPlpEKFIvkGMVERfndDFIETRRKALHKFLNRIADHPTL 198
Cdd:cd06871   25 IIRVQRGPSPENSWQVIRRYNDFDLLNASLQISGISLPLPP--KKLI--GNMDR---EFIAERQQGLQNYLNVILMNPIL 97

                         90
                 ....*....|.
gi 194294540 199 TFNEDFKIFLT 209
Cdd:cd06871   98 ASCLPVKKFLD 108
PX_SNX16 cd07276
The phosphoinositide binding Phox Homology domain of Sorting Nexin 16; The PX domain is a ...
 113-198 1.90e-07

The phosphoinositide binding Phox Homology domain of Sorting Nexin 16; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX16 contains a central PX domain followed by a coiled-coil region. SNX16 is localized in early and recycling endosomes through the binding of its PX domain to phosphatidylinositol-3-phosphate (PI3P). It plays a role in epidermal growth factor (EGF) signaling by regulating EGF receptor membrane trafficking.


Pssm-ID: 132809  Cd Length: 110  Bit Score: 49.33  E-value: 1.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540 113 FITYRIITKTSRGEFdsseFEVRRRYQDFLWLKGKLEEAHPTLIIpPLPEKFIVKgmvERFNDDFIETRRKALHKFLNRI 192
Cdd:cd07276   20 FTVYKIRVENKVGDS----WFVFRRYTDFVRLNDKLKQMFPGFRL-SLPPKRWFK---DNFDPDFLEERQLGLQAFVNNI 91


                 ....*.
gi 194294540 193 ADHPTL 198
Cdd:cd07276   92 MAHKDI 97
PX_HS1BP3 cd06868
The phosphoinositide binding Phox Homology domain of HS1BP3; The PX domain is a ...
 104-208 2.42e-07

The phosphoinositide binding Phox Homology domain of HS1BP3; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Hematopoietic lineage cell-specific protein-1 (HS1) binding protein 3 (HS1BP3) associates with HS1 proteins through their SH3 domains, suggesting a role in mediating signaling. It has been reported that HS1BP3 might affect the IL-2 signaling pathway in hematopoietic lineage cells. Mutations in HS1BP3 may also be associated with familial Parkinson disease and essential tremor. HS1BP3 contains a PX domain, a leucine zipper, motifs similar to immunoreceptor tyrosine-based inhibitory motif and proline-rich regions. The PX domain interacts with PIs and plays a role in targeting proteins to PI-enriched membranes.


Pssm-ID: 132778  Cd Length: 120  Bit Score: 49.33  E-value: 2.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540 104 ESHVTTIETFITYRIITKTSRGEFDSS--------EFEVRRRYQDFLWLKGKLEEAHPTLIIPPLPEKFIVKGMVErfnd 175
Cdd:cd06868   11 EIRGKTSSGHVLYQIVVVTRLAAFKSAkhkeedvvQFMVSKKYSEFEELYKKLSEKYPGTILPPLPRKALFVSESD---- 86

                         90       100       110
                 ....*....|....*....|....*....|...
gi 194294540 176 dfIETRRKALHKFLNRIADHPTLTFNEDFKIFL 208
Cdd:cd06868   87 --IRERRAAFNDFMRFISKDEKLANCPELLEFL 117
PX_SNX14 cd06877
The phosphoinositide binding Phox Homology domain of Sorting Nexin 14; The PX domain is a ...
 132-210 4.09e-07

The phosphoinositide binding Phox Homology domain of Sorting Nexin 14; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX14 may be involved in recruiting other proteins to the membrane via protein-protein and protein-ligand interaction. It is expressed in the embryonic nervous system of mice, and is co-expressed in the motoneurons and the anterior pituary with Islet-1. SNX14 shows a similar domain architecture as SNX13, containing an N-terminal PXA domain, a regulator of G protein signaling (RGS) domain, a PX domain, and a C-terminal domain that is conserved in some SNXs.


Pssm-ID: 132787  Cd Length: 119  Bit Score: 48.53  E-value: 4.09e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 194294540 132 FEVRRRYQDFLWLKGKLEEAHPTLIIPPLPEKfivKGMVERfNDDFIETRRKALHKFLNRIADHPTLTFNEDFKIFLTA 210
Cdd:cd06877   44 WSVLRRYNEFYVLESKLTEFHGEFPDAPLPSR---RIFGPK-SYEFLESKREIFEEFLQKLLQKPELRGSELLYDFLSP 118
PX_SNX19 cd06893
The phosphoinositide binding Phox Homology domain of Sorting Nexin 19; The PX domain is a ...
 125-208 1.45e-06

The phosphoinositide binding Phox Homology domain of Sorting Nexin 19; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX19 contains an N-terminal PXA domain, a central PX domain, and a C-terminal domain that is conserved in some SNXs. These domains are also found in SNX13 and SNX14, which also contain a regulator of G protein signaling (RGS) domain in between the PXA and PX domains. SNX19 interacts with IA-2, a major autoantigen found in type-1 diabetes. It inhibits the conversion of phosphatidylinositol-4,5-bisphosphate [PI(4,5)P2] to PI(3,4,5)P3, which leads in the decrease of protein phosphorylation in the Akt signaling pathway, resulting in apoptosis. SNX19 may also be implicated in coronary heart disease and thyroid oncocytic tumors.


Pssm-ID: 132803 [Multi-domain]  Cd Length: 132  Bit Score: 47.54  E-value: 1.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540 125 GEFDSSEFEVRRRYQDFLWLKGKLEEaHPTLiipplpEKFI-VKGMVERFND--------DFIETRRKALHKFLNRIADH 195
Cdd:cd06893   44 SEQPLATHTVNRRFREFLTLQTRLEE-NPKF------RKIMnVKGPPKRLFDlpfgnmdkDKIEARRGLLETFLRQLCSI 116

                         90
                 ....*....|...
gi 194294540 196 PTLTFNEDFKIFL 208
Cdd:cd06893  117 PEISNSEEVQEFL 129
PX_MDM1p cd06876
The phosphoinositide binding Phox Homology domain of yeast MDM1p; The PX domain is a ...
 113-209 4.78e-06

The phosphoinositide binding Phox Homology domain of yeast MDM1p; The PX domain is a phosphoinositide binding (PI) module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Yeast MDM1p is a filament-like protein localized in punctate structures distributed throughout the cytoplasm. It plays an important role in nuclear and mitochondrial transmission to daughter buds. Members of this subfamily show similar domain architectures as some sorting nexins (SNXs). Some members are similar to SNX19 in that they contain an N-terminal PXA domain, a central PX domain, and a C-terminal domain that is conserved in some SNXs. Others are similar to SNX13 and SNX14, which also harbor these three domains as well as a regulator of G protein signaling (RGS) domain in between the PXA and PX domains. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway.


Pssm-ID: 132786  Cd Length: 133  Bit Score: 45.76  E-value: 4.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540 113 FITYRIITKTSRGEFDSSEFEVRRRYQDFLWLKGKLEEAHPTLIIPPLPEKFIVkgMVERFNDDFIETRRKALHKFLNRI 192
Cdd:cd06876   38 FVVYLIEVQRLNNDDQSSGWVVARRYSEFLELHKYLKKRYPGVLKLDFPQKRKI--SLKYSKTLLVEERRKALEKYLQEL 115

                         90
                 ....*....|....*..
gi 194294540 193 ADHPTLTFNEDFKIFLT 209
Cdd:cd06876  116 LKIPEVCEDEEFRKFLS 132
PX_RPK118_like cd07287
The phosphoinositide binding Phox Homology domain of RPK118-like proteins; The PX domain is a ...
 97-198 1.08e-05

The phosphoinositide binding Phox Homology domain of RPK118-like proteins; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Members of this subfamily bear similarity to human RPK118, which contains an N-terminal PX domain, a Microtubule Interacting and Trafficking (MIT) domain, and a kinase domain. RPK118 binds sphingosine kinase, a key enzyme in the synthesis of sphingosine 1-phosphate (SPP), a lipid messenger involved in many cellular events. RPK118 may be involved in transmitting SPP-mediated signaling. It also binds the antioxidant peroxiredoxin-3 (PRDX3) and may be involved in the transport of PRDX3 from the cytoplasm to its site of function in the mitochondria. Members of this subfamily also show similarity to sorting nexin 15 (SNX15), which contains PX and MIT domains but does not contain a kinase domain. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNX15 plays a role in protein trafficking processes in the endocytic pathway and the trans-Golgi network. The PX domain of SNX15 interacts with the PDGF receptor and is responsible for the membrane association of the protein.


Pssm-ID: 132820  Cd Length: 118  Bit Score: 44.57  E-value: 1.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540  97 FITVDEPESHVTTIETF-ITYRIITKtsRGEFDSSEFEVRRRYQDFLWLKGKLEEAHPTL-----IIPPLPeKFIVKGmv 170
Cdd:cd07287    4 FYTVTDPRRHPKGYTVYkVTARIVSR--KNPEDVQEIVVWKRYSDFKKLHKDLWQIHKNLcrqseLFPPFA-KAKVFG-- 78

                         90       100
                 ....*....|....*....|....*...
gi 194294540 171 eRFNDDFIETRRKALHKFLNRIADHPTL 198
Cdd:cd07287   79 -RFDESVIEERRQCAEDLLQFSANIPAL 105
PX_SNX13 cd06873
The phosphoinositide binding Phox Homology domain of Sorting Nexin 13; The PX domain is a ...
 112-192 1.47e-05

The phosphoinositide binding Phox Homology domain of Sorting Nexin 13; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX13, also called RGS-PX1, contains an N-terminal PXA domain, a regulator of G protein signaling (RGS) domain, a PX domain, and a C-terminal domain that is conserved in some SNXs. It specifically binds to the stimulatory subunit of the heterotrimeric G protein G(alpha)s, serving as its GTPase activating protein, through the RGS domain. It preferentially binds phosphatidylinositol-3-phosphate (PI3P) through the PX domain and is localized in early endosomes. SNX13 is involved in endosomal sorting of EGFR into multivesicular bodies (MVB) for delivery to the lysosome.


Pssm-ID: 132783  Cd Length: 120  Bit Score: 44.18  E-value: 1.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540 112 TFITYRI-ITKTSRGEFDSSeFEVRRRYQDFLWLKGKLEEAHPTLIIPPLPEKFIVKGMverfNDDFIETRRKALHKFLN 190
Cdd:cd06873   21 TYAVYAIsVTRIYPNGQEES-WHVYRRYSDFHDLHMRLKEKFPNLSKLSFPGKKTFNNL----DRAFLEKRRKMLNQYLQ 95


                 ..
gi 194294540 191 RI 192
Cdd:cd06873   96 SL 97
PX_SNX15 cd07288
The phosphoinositide binding Phox Homology domain of Sorting Nexin 15; The PX domain is a ...
 97-208 3.33e-05

The phosphoinositide binding Phox Homology domain of Sorting Nexin 15; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX15 contains an N-terminal PX domain and a C-terminal Microtubule Interacting and Trafficking (MIT) domain. It plays a role in protein trafficking processes in the endocytic pathway and the trans-Golgi network. The PX domain of SNX15 interacts with the PDGF receptor and is responsible for the membrane association of the protein.


Pssm-ID: 132821  Cd Length: 118  Bit Score: 43.03  E-value: 3.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540  97 FITVDEPESHVTT-IETFITYRIITKTSRGefDSSEFEVRRRYQDFLWLKGKLEEAHPTLI-----IPPLPEKFIVKgmv 170
Cdd:cd07288    4 FYSVTDPRTHPKGyTEYKVTAQFISKKQPE--DVKEVVVWKRYSDLKKLHGELAYTHRNLFrrqeeFPPFPRAQVFG--- 78

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 194294540 171 eRFNDDFIETRRKALHKFLNRIADHPTLTFNEDFKIFL 208
Cdd:cd07288   79 -RFEAAVIEERRNAAEAMLLFTVNIPALYNSPQLKEFF 115
PX_SNX15_like cd06881
The phosphoinositide binding Phox Homology domain of Sorting Nexin 15-like proteins; The PX ...
 99-198 4.26e-05

The phosphoinositide binding Phox Homology domain of Sorting Nexin 15-like proteins; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Members of this subfamily have similarity to sorting nexin 15 (SNX15), which contains an N-terminal PX domain and a C-terminal Microtubule Interacting and Trafficking (MIT) domain. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNX15 plays a role in protein trafficking processes in the endocytic pathway and the trans-Golgi network. The PX domain of SNX15 interacts with the PDGF receptor and is responsible for the membrane association of the protein. Other members of this subfamily contain an additional C-terminal kinase domain, similar to human RPK118, which binds sphingosine kinase and the antioxidant peroxiredoxin-3 (PRDX3). RPK118 may be involved in the transport of proteins such as PRDX3 from the cytoplasm to its site of function in the mitochondria.


Pssm-ID: 132791  Cd Length: 117  Bit Score: 42.69  E-value: 4.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540  99 TVDEPESHVT--TIETfITYRIITKTSrgEFDSSEFEVRRRYQDFLWLKGKLEEAHPTLII----PPLPEKFIVKgmveR 172
Cdd:cd06881    6 TVTDTRRHKKgyTEYK-ITSKVFSRSV--PEDVSEVVVWKRYSDFKKLHRELSRLHKQLYLsgsfPPFPKGKYFG----R 78

                         90       100
                 ....*....|....*....|....*.
gi 194294540 173 FNDDFIETRRKALHKFLNRIADHPTL 198
Cdd:cd06881   79 FDAAVIEERRQAILELLDFVGNHPAL 104
PX_Bem1p cd06890
The phosphoinositide binding Phox Homology domain of Bem1p; The PX domain is a ...
 116-209 7.53e-05

The phosphoinositide binding Phox Homology domain of Bem1p; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Members of this subfamily bear similarity to Saccharomyces cerevisiae Bem1p, containing two Src Homology 3 (SH3) domains at the N-terminus, a central PX domain, and a C-terminal PB1 domain. Bem1p is a scaffolding protein that is critical for proper Cdc42p activation during bud formation in yeast. During budding and mating, Bem1p migrates to the plasma membrane where it can serve as an adaptor for Cdc42p and some other proteins. Bem1p also functions as an effector of the G1 cyclin Cln3p and the cyclin-dependent kinase Cdc28p in promoting vacuolar fusion. The PX domain is involved in targeting of proteins to PI-enriched membranes, and may also be involved in protein-protein interaction. The PX domain of Bem1p specifically binds phosphatidylinositol-4-phosphate (PI4P).


Pssm-ID: 132800  Cd Length: 112  Bit Score: 41.89  E-value: 7.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540 116 YRIITKTSrgefDSSEFEVRRRYQDFLWLKGKL-----EEA---HPTLIIPPLPEKFIvkgmvERFNDDFIETRRKALHK 187
Cdd:cd06890   17 YRVRATLS----DGKTRYLCRYYQDFYKLHIALldlfpAEAgrnSSKRILPYLPGPVT-----DVVNDSISLKRLNDLNE 87

                         90       100
                 ....*....|....*....|...
gi 194294540 188 FLNRIADHPT-LTFNEDFKIFLT 209
Cdd:cd06890   88 YLNELINLPAyIQTSEVVRDFFA 110
PX_SNX6 cd07292
The phosphoinositide binding Phox Homology domain of Sorting Nexin 6; The PX domain is a ...
 114-208 7.60e-05

The phosphoinositide binding Phox Homology domain of Sorting Nexin 6; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX6 forms a stable complex with SNX1 and may be a component of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi, acting as a mammalian equivalent of yeast Vsp17p. It interacts with the receptor serine/threonine kinases from the transforming growth factor-beta family. It also plays roles in enhancing the degradation of EGFR and in regulating the activity of Na,K-ATPase through its interaction with Translationally Controlled Tumor Protein (TCTP). SNX6 harbors a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain, similar to other sorting nexins including SNX1-2. The PX-BAR structural unit helps determine the specific membrane-targeting of some SNXs.


Pssm-ID: 132825  Cd Length: 141  Bit Score: 42.78  E-value: 7.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540 114 ITYRIITKTSRGEFDSSEFEVRRRYQDFLWLKGKL--EEAHPTLIIPPLP---------EKFIVKG-------------M 169
Cdd:cd07292   17 VKFTVHTKSSLPNFKQNEFSVVRQHEEFIWLHDSFveNEDYAGYIIPPAPprpdfdasrEKLQKLGegegsmtkeeftkM 96

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 194294540 170 VERFNDDFIETRRK--ALHK-FLNRIADHPTLTFNEDFKIFL 208
Cdd:cd07292   97 KQELEAEYLAIFKKtvAMHEvFLCRVAAHPILRKDLNFHVFL 138
PX_UP2_fungi cd06869
The phosphoinositide binding Phox Homology domain of uncharacterized fungal proteins; The PX ...
 115-210 3.93e-04

The phosphoinositide binding Phox Homology domain of uncharacterized fungal proteins; The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to PI-enriched membranes. Members in this subfamily are uncharacterized fungal proteins containing a PX domain. PX domain harboring proteins have been implicated in highly diverse functions such as cell signaling, vesicular trafficking, protein sorting, lipid modification, cell polarity and division, activation of T and B cells, and cell survival. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction.


Pssm-ID: 132779  Cd Length: 119  Bit Score: 39.96  E-value: 3.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540 115 TYRIITKTSRGEFDSSEFEVRRRYQDFLWLKGKLEEAHPTLIIPPLPEKFivkgMVERfnddfiETRRKALHKFLNRIAD 194
Cdd:cd06869   33 HYEFIIRVRREGEEYRTIYVARRYSDFKKLHHDLKKEFPGKKLPKLPHKD----KLPR------EKLRLSLRQYLRSLLK 102

                         90
                 ....*....|....*.
gi 194294540 195 HPTLTFNEDFKIFLTA 210
Cdd:cd06869  103 DPEVAHSSILQEFLTS 118
PX_SNX20 cd07300
The phosphoinositide binding Phox Homology domain of Sorting Nexin 20; The PX domain is a ...
 109-211 8.94e-04

The phosphoinositide binding Phox Homology domain of Sorting Nexin 20; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Some SNXs are localized in early endosome structures such as clathrin-coated pits, while others are located in late structures of the endocytic pathway. SNX20 interacts with P-Selectin glycoprotein ligand-1 (PSGL-1), a surface-expressed mucin that acts as a ligand for the selectin family of adhesion proteins. The PX domain of SNX20 binds PIs and targets the SNX20/PSGL-1 complex to endosomes. SNX20 may function in the sorting and cycling of PSGL-1 into endosomes.


Pssm-ID: 132833  Cd Length: 114  Bit Score: 39.03  E-value: 8.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540 109 TIETFITYRIITKTSrGEFDSSEFEVRRRYQDFLWLKGKL-----EEAHPTliipplpeKFIVKGMVERFNDDFIETRRK 183
Cdd:cd07300   14 TISKHVVYQIIVIQT-GSFDCNKVVIERRYSDFLKLHQELlsdfsEELEDV--------VFPKKKLTGNFSEEIIAERRV 84

                         90       100
                 ....*....|....*....|....*...
gi 194294540 184 ALHKFLNRIADHPTLTFNEDFKIFLTAQ 211
Cdd:cd07300   85 ALRDYLTLLYSLRFVRRSQAFQDFLTHP 112
BAR_SNX1_2 cd07623
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins 1 and 2; BAR domains are dimerization, ...
 346-435 2.37e-03

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins 1 and 2; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. This subfamily consists of SNX1, SNX2, and similar proteins. SNX1 and SNX2 are components of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi. The retromer consists of a cargo-recognition subcomplex and a subcomplex formed by a dimer of sorting nexins (SNX1 and/or SNX2), which ensures efficient cargo sorting by facilitating proper membrane localization of the cargo-recognition subcomplex. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153307  Cd Length: 224  Bit Score: 39.18  E-value: 2.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194294540 346 MGVMKRRDQ-IQAELDSKVEVLTYKKADTDLLPEEIGKLEDKVECANNALKADWERWKQNMQNDIKLAFTDMAEENIHYY 424
Cdd:cd07623  130 QTLTKKREAkAKLELSGRTDKLDQAQQEIKEWEAKVDRGQKEFEEISKTIKKEIERFEKNRVKDFKDIIIKYLESLLNTQ 209

                         90
                 ....*....|.
gi 194294540 425 EQCLATWESFL 435
Cdd:cd07623  210 QQLIKYWEAFL 220
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH