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Conserved domains on  [gi|568938658|ref|XP_006504736|]
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sorting nexin-8 isoform X2 [Mus musculus]

Protein Classification

sorting nexin-8 family protein( domain architecture ID 10160679)

sorting nexin-8 family protein, similar to Neurospora crassa sorting nexin mvp-1 which is required for vacuolar protein sorting.

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
BAR_SNX8 cd07597
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 8; BAR domains are dimerization, lipid ...
177-408 7.15e-97

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 8; 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. SNX8 and the yeast counterpart Mvp1p are involved in sorting and delivery of late-Golgi proteins, such as carboxypeptidase Y, to vacuoles. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


:

Pssm-ID: 153281 [Multi-domain]  Cd Length: 246  Bit Score: 290.36  E-value: 7.15e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938658 177 DFLPADIQTQFAMSRELIRNVYNSFYKLRDRAERIASRAIDNAADLLIFGKELSALGSDTTPLPSWAAlHLSTWGSLKQA 256
Cdd:cd07597   14 VLLPPDFQEQWANSRERIRRLLESWTKLRVLAERYEKRSQQQAADRAEFARLLNSLGELTARLYPWAG-DSDTWGDINEG 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938658 257 LKGLSVEFALLADRAAQQGKKEENDVVEKLNLFLDLLQSYKDLCERHEKGVLHKHQRALHKYGLMKRQMMS--AAHGREP 334
Cdd:cd07597   93 LSSLSKHFQLLSDLSEDEARAEEDGVLEKLKLQLDLLVSLRDLFERHEKLSLNNIQRLLKRIELNKKKLESlrAKPDVKG 172
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568938658 335 ESVEQLESRIVEQENVIQTMELRNYFSLYCLHQETQLVHVYLPLTSHILGAFVNSQIQGHKEMSKVWNDLKPKL 408
Cdd:cd07597  173 AEVDKLEASIIKDKESIANQLNRSWFIRECILEETQLFQETQFLLTSILQEFVKDEIQYHSELANVWERLVPKL 246
PX_SNX8_Mvp1p_like cd06866
The phosphoinositide binding Phox Homology domain of Sorting Nexin 8 and yeast Mvp1p; The PX ...
71-174 3.79e-60

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: 190.90  E-value: 3.79e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938658  71 DTVQVELIPEKKGLFLKHVEYEVSSQRFKSSVYRRYNDFVVFHEVLLHKFPYRMVPALPPKRVLG-ADREFIEGRRRALK 149
Cdd:cd06866    1 DTVTVELVPEKKGLFLKHVEYEVSSKRFKSTVYRRYSDFVWLHEYLLKRYPYRMVPALPPKRIGGsADREFLEARRRGLS 80
                         90       100
                 ....*....|....*....|....*
gi 568938658 150 RFINLVARHPPFSEDVLLKLFLSFS 174
Cdd:cd06866   81 RFLNLVARHPVLSEDELVRTFLTEP 105
 
Name Accession Description Interval E-value
BAR_SNX8 cd07597
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 8; BAR domains are dimerization, lipid ...
177-408 7.15e-97

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 8; 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. SNX8 and the yeast counterpart Mvp1p are involved in sorting and delivery of late-Golgi proteins, such as carboxypeptidase Y, to vacuoles. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153281 [Multi-domain]  Cd Length: 246  Bit Score: 290.36  E-value: 7.15e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938658 177 DFLPADIQTQFAMSRELIRNVYNSFYKLRDRAERIASRAIDNAADLLIFGKELSALGSDTTPLPSWAAlHLSTWGSLKQA 256
Cdd:cd07597   14 VLLPPDFQEQWANSRERIRRLLESWTKLRVLAERYEKRSQQQAADRAEFARLLNSLGELTARLYPWAG-DSDTWGDINEG 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938658 257 LKGLSVEFALLADRAAQQGKKEENDVVEKLNLFLDLLQSYKDLCERHEKGVLHKHQRALHKYGLMKRQMMS--AAHGREP 334
Cdd:cd07597   93 LSSLSKHFQLLSDLSEDEARAEEDGVLEKLKLQLDLLVSLRDLFERHEKLSLNNIQRLLKRIELNKKKLESlrAKPDVKG 172
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568938658 335 ESVEQLESRIVEQENVIQTMELRNYFSLYCLHQETQLVHVYLPLTSHILGAFVNSQIQGHKEMSKVWNDLKPKL 408
Cdd:cd07597  173 AEVDKLEASIIKDKESIANQLNRSWFIRECILEETQLFQETQFLLTSILQEFVKDEIQYHSELANVWERLVPKL 246
PX_SNX8_Mvp1p_like cd06866
The phosphoinositide binding Phox Homology domain of Sorting Nexin 8 and yeast Mvp1p; The PX ...
71-174 3.79e-60

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: 190.90  E-value: 3.79e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938658  71 DTVQVELIPEKKGLFLKHVEYEVSSQRFKSSVYRRYNDFVVFHEVLLHKFPYRMVPALPPKRVLG-ADREFIEGRRRALK 149
Cdd:cd06866    1 DTVTVELVPEKKGLFLKHVEYEVSSKRFKSTVYRRYSDFVWLHEYLLKRYPYRMVPALPPKRIGGsADREFLEARRRGLS 80
                         90       100
                 ....*....|....*....|....*
gi 568938658 150 RFINLVARHPPFSEDVLLKLFLSFS 174
Cdd:cd06866   81 RFLNLVARHPVLSEDELVRTFLTEP 105
PX pfam00787
PX domain; PX domains bind to phosphoinositides.
92-174 2.52e-22

PX domain; PX domains bind to phosphoinositides.


Pssm-ID: 459940  Cd Length: 84  Bit Score: 90.38  E-value: 2.52e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938658   92 EVSSQRFKSSVYRRYNDFVVFHEVLLHKFPYRMVPALPPKRVLGA-DREFIEGRRRALKRFINLVARHPPFSEDVLLKLF 170
Cdd:pfam00787   1 LPTFSLEEWSVRRRYSDFVELHKKLLRKFPSVIIPPLPPKRWLGRyNEEFIEKRRKGLEQYLQRLLQHPELRNSEVLLEF 80

                  ....
gi 568938658  171 LSFS 174
Cdd:pfam00787  81 LESD 84
COG5391 COG5391
Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function ...
78-312 3.44e-17

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


Pssm-ID: 227680 [Multi-domain]  Cd Length: 524  Bit Score: 83.69  E-value: 3.44e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938658  78 IPEKKGLF----LKHVEYEV-------SSQRFKS---SVYRRYNDFVVFHEVLLHKFPYRMVPALPPKRVLG------AD 137
Cdd:COG5391  137 NPQSLTLLvdsrDKHTSYEIitvtnlpSFQLRESrplVVRRRYSDFESLHSILIKLLPLCAIPPLPSKKSNSeyygdrFS 216
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938658 138 REFIEGRRRALKRFINLVARHPPFSEDVLLKLFLSFS--GSDFLP---ADIQTQFAMSRELIRNVYNSFYKLRDRAERIA 212
Cdd:COG5391  217 DEFIEERRQSLQNFLRRVSTHPLLSNYKNSKSWESHStlLSSFIEnrkSVPTPLSLDLTSTTQELDMERKELNESTSKAI 296
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938658 213 SrAIDNaaDLLIFGKELSALGSD----TTPLPSWAALHLstwgslkQALKGLSVEFALLadraAQQGKKEENDVVEKLNL 288
Cdd:COG5391  297 H-NILS--IFSLFEKILIQLESEeeslTRLLESLNNLLL-------LVLNFSGVFAKRL----EQNQNSILNEGVVQAET 362
                        250       260
                 ....*....|....*....|....*..
gi 568938658 289 FLDLL---QSYKDLCERHEKGVLHKHQ 312
Cdd:COG5391  363 LRSSLkelLTQLQDEIKSRESLILTDS 389
PX smart00312
PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function ...
89-172 2.67e-16

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: 74.30  E-value: 2.67e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938658    89 VEYEVSSQRFKSSVYRRYNDFVVFHEVLLHKFPYRMVPALPPKRVLG----ADREFIEGRRRALKRFINLVARHPPFS-E 163
Cdd:smart00312  17 IEIETKTGLEEWTVSRRYSDFLELHSKLKKHFPRSILPPLPGKKLFGrlnnFSEEFIEKRRRGLEKYLQSLLNHPELInH 96

                   ....*....
gi 568938658   164 DVLLKLFLS 172
Cdd:smart00312  97 SEVVLEFLE 105
 
Name Accession Description Interval E-value
BAR_SNX8 cd07597
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 8; BAR domains are dimerization, lipid ...
177-408 7.15e-97

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexin 8; 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. SNX8 and the yeast counterpart Mvp1p are involved in sorting and delivery of late-Golgi proteins, such as carboxypeptidase Y, to vacuoles. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153281 [Multi-domain]  Cd Length: 246  Bit Score: 290.36  E-value: 7.15e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938658 177 DFLPADIQTQFAMSRELIRNVYNSFYKLRDRAERIASRAIDNAADLLIFGKELSALGSDTTPLPSWAAlHLSTWGSLKQA 256
Cdd:cd07597   14 VLLPPDFQEQWANSRERIRRLLESWTKLRVLAERYEKRSQQQAADRAEFARLLNSLGELTARLYPWAG-DSDTWGDINEG 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938658 257 LKGLSVEFALLADRAAQQGKKEENDVVEKLNLFLDLLQSYKDLCERHEKGVLHKHQRALHKYGLMKRQMMS--AAHGREP 334
Cdd:cd07597   93 LSSLSKHFQLLSDLSEDEARAEEDGVLEKLKLQLDLLVSLRDLFERHEKLSLNNIQRLLKRIELNKKKLESlrAKPDVKG 172
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568938658 335 ESVEQLESRIVEQENVIQTMELRNYFSLYCLHQETQLVHVYLPLTSHILGAFVNSQIQGHKEMSKVWNDLKPKL 408
Cdd:cd07597  173 AEVDKLEASIIKDKESIANQLNRSWFIRECILEETQLFQETQFLLTSILQEFVKDEIQYHSELANVWERLVPKL 246
PX_SNX8_Mvp1p_like cd06866
The phosphoinositide binding Phox Homology domain of Sorting Nexin 8 and yeast Mvp1p; The PX ...
71-174 3.79e-60

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: 190.90  E-value: 3.79e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938658  71 DTVQVELIPEKKGLFLKHVEYEVSSQRFKSSVYRRYNDFVVFHEVLLHKFPYRMVPALPPKRVLG-ADREFIEGRRRALK 149
Cdd:cd06866    1 DTVTVELVPEKKGLFLKHVEYEVSSKRFKSTVYRRYSDFVWLHEYLLKRYPYRMVPALPPKRIGGsADREFLEARRRGLS 80
                         90       100
                 ....*....|....*....|....*
gi 568938658 150 RFINLVARHPPFSEDVLLKLFLSFS 174
Cdd:cd06866   81 RFLNLVARHPVLSEDELVRTFLTEP 105
PX pfam00787
PX domain; PX domains bind to phosphoinositides.
92-174 2.52e-22

PX domain; PX domains bind to phosphoinositides.


Pssm-ID: 459940  Cd Length: 84  Bit Score: 90.38  E-value: 2.52e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938658   92 EVSSQRFKSSVYRRYNDFVVFHEVLLHKFPYRMVPALPPKRVLGA-DREFIEGRRRALKRFINLVARHPPFSEDVLLKLF 170
Cdd:pfam00787   1 LPTFSLEEWSVRRRYSDFVELHKKLLRKFPSVIIPPLPPKRWLGRyNEEFIEKRRKGLEQYLQRLLQHPELRNSEVLLEF 80

                  ....
gi 568938658  171 LSFS 174
Cdd:pfam00787  81 LESD 84
PX_domain cd06093
The Phox Homology domain, a phosphoinositide binding module; The PX domain is a ...
72-172 1.97e-20

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: 85.87  E-value: 1.97e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938658  72 TVQVELIPEKKGLFLKHVEYEVSSQRF---KSSVYRRYNDFVVFHEVLLHKFPYRMVPALPPKRVLGA-DREFIEGRRRA 147
Cdd:cd06093    1 SVSIPDYEKVKDGGKKYVVYIIEVTTQggeEWTVYRRYSDFEELHEKLKKKFPGVILPPLPPKKLFGNlDPEFIEERRKQ 80
                         90       100
                 ....*....|....*....|....*
gi 568938658 148 LKRFINLVARHPPFSEDVLLKLFLS 172
Cdd:cd06093   81 LEQYLQSLLNHPELRNSEELKEFLE 105
PX_SNX1_2_like cd06859
The phosphoinositide binding Phox Homology domain of Sorting Nexins 1 and 2; The PX domain is ...
79-171 5.20e-20

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: 84.94  E-value: 5.20e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938658  79 PEKKG-LFLKHVEYEVSSQ----RFK---SSVYRRYNDFVVFHEVLLHKFPYRMVPALPPKRVLGADR---EFIEGRRRA 147
Cdd:cd06859    8 PVKVGdGMSAYVVYRVTTKtnlpDFKkseFSVLRRYSDFLWLYERLVEKYPGRIVPPPPEKQAVGRFKvkfEFIEKRRAA 87
                         90       100
                 ....*....|....*....|....
gi 568938658 148 LKRFINLVARHPPFSEDVLLKLFL 171
Cdd:cd06859   88 LERFLRRIAAHPVLRKDPDFRLFL 111
COG5391 COG5391
Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function ...
78-312 3.44e-17

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


Pssm-ID: 227680 [Multi-domain]  Cd Length: 524  Bit Score: 83.69  E-value: 3.44e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938658  78 IPEKKGLF----LKHVEYEV-------SSQRFKS---SVYRRYNDFVVFHEVLLHKFPYRMVPALPPKRVLG------AD 137
Cdd:COG5391  137 NPQSLTLLvdsrDKHTSYEIitvtnlpSFQLRESrplVVRRRYSDFESLHSILIKLLPLCAIPPLPSKKSNSeyygdrFS 216
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938658 138 REFIEGRRRALKRFINLVARHPPFSEDVLLKLFLSFS--GSDFLP---ADIQTQFAMSRELIRNVYNSFYKLRDRAERIA 212
Cdd:COG5391  217 DEFIEERRQSLQNFLRRVSTHPLLSNYKNSKSWESHStlLSSFIEnrkSVPTPLSLDLTSTTQELDMERKELNESTSKAI 296
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938658 213 SrAIDNaaDLLIFGKELSALGSD----TTPLPSWAALHLstwgslkQALKGLSVEFALLadraAQQGKKEENDVVEKLNL 288
Cdd:COG5391  297 H-NILS--IFSLFEKILIQLESEeeslTRLLESLNNLLL-------LVLNFSGVFAKRL----EQNQNSILNEGVVQAET 362
                        250       260
                 ....*....|....*....|....*..
gi 568938658 289 FLDLL---QSYKDLCERHEKGVLHKHQ 312
Cdd:COG5391  363 LRSSLkelLTQLQDEIKSRESLILTDS 389
PX smart00312
PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function ...
89-172 2.67e-16

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: 74.30  E-value: 2.67e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938658    89 VEYEVSSQRFKSSVYRRYNDFVVFHEVLLHKFPYRMVPALPPKRVLG----ADREFIEGRRRALKRFINLVARHPPFS-E 163
Cdd:smart00312  17 IEIETKTGLEEWTVSRRYSDFLELHSKLKKHFPRSILPPLPGKKLFGrlnnFSEEFIEKRRRGLEKYLQSLLNHPELInH 96

                   ....*....
gi 568938658   164 DVLLKLFLS 172
Cdd:smart00312  97 SEVVLEFLE 105
PX_Vps5p cd06861
The phosphoinositide binding Phox Homology domain of yeast sorting nexin Vps5p; The PX domain ...
88-172 2.84e-16

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: 74.31  E-value: 2.84e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938658  88 HVEYEVSS-------QRFKSSVYRRYNDFVVFHEVLLHKFPYRMVPALPPKRVLGA-DREFIEGRRRALKRFINLVARHP 159
Cdd:cd06861   18 HTVYTVRTrttspnfEVSSFSVLRRYRDFRWLYRQLQNNHPGVIVPPPPEKQSVGRfDDNFVEQRRAALEKMLRKIANHP 97
                         90
                 ....*....|...
gi 568938658 160 PFSEDVLLKLFLS 172
Cdd:cd06861   98 VLQKDPDFRLFLE 110
PX_Atg24p cd06863
The phosphoinositide binding Phox Homology domain of yeast Atg24p, an autophagic degradation ...
88-172 6.13e-16

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: 73.48  E-value: 6.13e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938658  88 HVEYEVSS-------QRFKSSVYRRYNDFVVFHEVLLHKFPYRMVPALPPKRVLG---ADR---EFIEGRRRALKRFINL 154
Cdd:cd06863   19 YISYLITTktnlpsfSRKEFKVRRRYSDFVFLHECLSNDFPACVVPPLPDKHRLEyitGDRfspEFITRRAQSLQRFLRR 98
                         90
                 ....*....|....*...
gi 568938658 155 VARHPPFSEDVLLKLFLS 172
Cdd:cd06863   99 ISLHPVLSQSKILHQFLE 116
PX_SNX7_30_like cd06860
The phosphoinositide binding Phox Homology domain of Sorting Nexins 7 and 30; The PX domain is ...
101-171 2.59e-15

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: 71.98  E-value: 2.59e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568938658 101 SVYRRYNDFVVFHEVLLHKFPYRMVPALPPKRVLGA--DR---EFIEGRRRALKRFINLVARHPPFSEDVLLKLFL 171
Cdd:cd06860   38 SVRRRYQDFLWLRQKLEESHPTHIIPPLPEKHSVKGllDRfspEFVATRMRALHKFLNRIVEHPVLSFNEHLKVFL 113
PX_SNX4 cd06864
The phosphoinositide binding Phox Homology domain of Sorting Nexin 4; The PX domain is a ...
100-171 7.27e-15

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: 70.86  E-value: 7.27e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938658 100 SSVYRRYNDFVVFHEVLLHKFPYRMVPALPPKRV------LGADR---EFIEGRRRALKRFINLVARHPPFSEDVLLKLF 170
Cdd:cd06864   46 SSLWRRYSEFELLRNYLVVTYPYVIVPPLPEKRAmfmwqkLSSDTfdpDFVERRRAGLENFLLRVAGHPELCQDKIFLEF 125

                 .
gi 568938658 171 L 171
Cdd:cd06864  126 L 126
BAR cd07307
The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects ...
194-406 1.73e-13

The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects membrane curvature; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions including organelle biogenesis, membrane trafficking or remodeling, and cell division and migration. Mutations in BAR containing proteins have been linked to diseases and their inactivation in cells leads to altered membrane dynamics. A BAR domain with an additional N-terminal amphipathic helix (an N-BAR) can drive membrane curvature. These N-BAR domains are found in amphiphysins and endophilins, among others. BAR domains are also frequently found alongside domains that determine lipid specificity, such as the Pleckstrin Homology (PH) and Phox Homology (PX) domains which are present in beta centaurins (ACAPs and ASAPs) and sorting nexins, respectively. A FES-CIP4 Homology (FCH) domain together with a coiled coil region is called the F-BAR domain and is present in Pombe/Cdc15 homology (PCH) family proteins, which include Fes/Fes tyrosine kinases, PACSIN or syndapin, CIP4-like proteins, and srGAPs, among others. The Inverse (I)-BAR or IRSp53/MIM homology Domain (IMD) is found in multi-domain proteins, such as IRSp53 and MIM, that act as scaffolding proteins and transducers of a variety of signaling pathways that link membrane dynamics and the underlying actin cytoskeleton. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. The I-BAR domain induces membrane protrusions in the opposite direction compared to classical BAR and F-BAR domains, which produce membrane invaginations. BAR domains that also serve as protein interaction domains include those of arfaptin and OPHN1-like proteins, among others, which bind to Rac and Rho GAP domains, respectively.


Pssm-ID: 153271 [Multi-domain]  Cd Length: 194  Bit Score: 68.63  E-value: 1.73e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938658 194 IRNVYNSFYKLRDRAERIASRAIDNAADLLIFGKELSALGSDTTPLPSWAalhlstwgslkqaLKGLSVEFALLADRAAQ 273
Cdd:cd07307    2 LDELEKLLKKLIKDTKKLLDSLKELPAAAEKLSEALQELGKELPDLSNTD-------------LGEALEKFGKIQKELEE 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938658 274 QGKKEENDVVEKlnlFLDLLQSYKDlcerHEKGVLHKHQRALHKyglmKRQMMSAAHGRE---PESVEQLESRIVEQENV 350
Cdd:cd07307   69 FRDQLEQKLENK---VIEPLKEYLK----KDLKEIKKRRKKLDK----ARLDYDAAREKLkklRKKKKDSSKLAEAEEEL 137
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568938658 351 IQTMELRNYFSLYCLHQETQLVHVYLPLTSHILGAFVNSQIQGHKEMSKVWNDLKP 406
Cdd:cd07307  138 QEAKEKYEELREELIEDLNKLEEKRKELFLSLLLSFIEAQSEFFKEVLKILEQLLP 193
PX_YPT35 cd07280
The phosphoinositide binding Phox Homology domain of the fungal protein YPT35; The PX domain ...
102-171 8.19e-13

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: 64.66  E-value: 8.19e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568938658 102 VYRRYNDFVVFHEVLLHKFP---YRMVPALPPKRVLGADR-----EFIEGRRRALKRFINLVARHPPFSEDVLLKLFL 171
Cdd:cd07280   41 AYKRYSEFVQLREALLDEFPrhkRNEIPQLPPKVPWYDSRvnlnkAWLEKRRRGLQYFLNCVLLNPVFGGSPVVKEFL 118
PX_SNX9_18_like cd06862
The phosphoinositide binding Phox Homology domain of Sorting Nexins 9 and 18; The PX domain is ...
82-174 1.72e-12

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: 63.87  E-value: 1.72e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938658  82 KGLfLKHVEYEVSSQRFKSSVYRRYNDFVVFHEVLLHKFPYRMVPALPPKRVLGA-DREFIEGRRRALKRFINLVARHPP 160
Cdd:cd06862   15 KGL-KSFIAYQITPTHTNVTVSRRYKHFDWLYERLVEKYSCIAIPPLPEKQVTGRfEEDFIEKRRERLELWMNRLARHPV 93
                         90
                 ....*....|....
gi 568938658 161 FSEDVLLKLFLSFS 174
Cdd:cd06862   94 LSQSEVFRHFLTCT 107
PX_MONaKA cd06871
The phosphoinositide binding Phox Homology domain of Modulator of Na,K-ATPase; The PX domain ...
71-171 1.73e-12

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: 63.92  E-value: 1.73e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938658  71 DTVQVELIPEKKGLFLKHVEYEVSSQRFKSS-----VYRRYNDFVVFHEVLlhKFPYRMVPaLPPKRVLG-ADREFIEGR 144
Cdd:cd06871    4 DTVPLTCVIEASQNIQSHTEYIIRVQRGPSPenswqVIRRYNDFDLLNASL--QISGISLP-LPPKKLIGnMDREFIAER 80
                         90       100
                 ....*....|....*....|....*..
gi 568938658 145 RRALKRFINLVARHPPFSEDVLLKLFL 171
Cdd:cd06871   81 QQGLQNYLNVILMNPILASCLPVKKFL 107
PX_SNX7 cd07284
The phosphoinositide binding Phox Homology domain of Sorting Nexin 7; The PX domain is a ...
92-172 4.26e-11

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: 59.99  E-value: 4.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938658  92 EVSSQRFKSS---VYRRYNDFVVFHEVLLHKFPYRMVPALPPKRVLGA-----DREFIEGRRRALKRFINLVARHPPFSE 163
Cdd:cd07284   26 KTSRSEFDSSefeVRRRYQDFLWLKGRLEEAHPTLIIPPLPEKFVMKGmverfNEDFIETRRKALHKFLNRIADHPTLTF 105

                 ....*....
gi 568938658 164 DVLLKLFLS 172
Cdd:cd07284  106 NEDFKIFLT 114
PX_SNX41_42 cd06867
The phosphoinositide binding Phox Homology domain of fungal Sorting Nexins 41 and 42; The PX ...
88-172 4.83e-11

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: 59.57  E-value: 4.83e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938658  88 HVEYEVSSQrfKSSVYRRYNDFVVFHEVLLHKFPYRMVPALPPKRVLGA----------DREFIEGRRRALKRFINLVAR 157
Cdd:cd06867   18 YIVYVIRLG--GSEVKRRYSEFESLRKNLTRLYPTLIIPPIPEKHSLKDyakkpskaknDAKIIERRKRMLQRFLNRCLQ 95
                         90
                 ....*....|....*
gi 568938658 158 HPPFSEDVLLKLFLS 172
Cdd:cd06867   96 HPILRNDIVFQKFLD 110
PX_SNX9 cd07285
The phosphoinositide binding Phox Homology domain of Sorting Nexin 9; The PX domain is a ...
88-173 8.53e-10

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: 56.57  E-value: 8.53e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938658  88 HVEYEVSSQRFKSSVYRRYNDFVVFHEVLLHKFPYRM-VPALPPKRVLGA-DREFIEGRRRALKRFINLVARHPPFSEDV 165
Cdd:cd07285   20 YIEYQLTPTNTNRSVNHRYKHFDWLYERLLVKFGLAIpIPSLPDKQVTGRfEEEFIKMRMERLQAWMTRMCRHPVISESE 99

                 ....*...
gi 568938658 166 LLKLFLSF 173
Cdd:cd07285  100 VFQQFLNF 107
PX_SNX2 cd07282
The phosphoinositide binding Phox Homology domain of Sorting Nexin 2; The PX domain is a ...
79-174 1.33e-09

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: 55.83  E-value: 1.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938658  79 PEKKGLFLK-HVEYEVSSQ-------RFKSSVYRRYNDFVVFHEVLLHKFPY--RMVPALPPKRVLGADR---------- 138
Cdd:cd07282    8 PEKVGDGMNaYMAYRVTTKtslsmfsRSEFSVRRRFSDFLGLHSKLASKYLHvgYIVPPAPEKSIVGMTKvkvgkedsss 87
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 568938658 139 -EFIEGRRRALKRFINLVARHPPFSEDVLLKLFLSFS 174
Cdd:cd07282   88 tEFVEKRRAALERYLQRTVKHPTLLQDPDLRQFLESS 124
PX_SNX16 cd07276
The phosphoinositide binding Phox Homology domain of Sorting Nexin 16; The PX domain is a ...
91-171 2.06e-09

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: 54.72  E-value: 2.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938658  91 YEVSSQRFKSSVY---------------RRYNDFVVFHEVLLHKFPYrMVPALPPKRVLGA--DREFIEGRRRALKRFIN 153
Cdd:cd07276   11 YEVMEERARFTVYkirvenkvgdswfvfRRYTDFVRLNDKLKQMFPG-FRLSLPPKRWFKDnfDPDFLEERQLGLQAFVN 89
                         90
                 ....*....|....*...
gi 568938658 154 LVARHPPFSEDVLLKLFL 171
Cdd:cd07276   90 NIMAHKDIAKCKLVREFF 107
PX_Grd19 cd07295
The phosphoinositide binding Phox Homology domain of fungal Grd19; The PX domain is a ...
100-159 2.76e-09

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: 54.81  E-value: 2.76e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568938658 100 SSVYRRYNDFVVFHEVLLHKFPYRMVPALPPKRVLGADR-EFIEGRRRALKRFINLVARHP 159
Cdd:cd07295   38 SSVRRRYSDFEYFRDILERESPRVMIPPLPGKIFTNRFSdEVIEERRQGLETFLQSVAGHP 98
PX_SNX1 cd07281
The phosphoinositide binding Phox Homology domain of Sorting Nexin 1; The PX domain is a ...
79-171 4.92e-09

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: 54.29  E-value: 4.92e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938658  79 PEKKGLFLK-HVEYEVSSQR----FKS---SVYRRYNDFVVFHEVLLHKFPYR--MVPALPPKRVLGADR---------- 138
Cdd:cd07281    8 PEKIGDGMNaYVVYKVTTQTsllmFRSkhfTVKRRFSDFLGLYEKLSEKHSQNgfIVPPPPEKSLIGMTKvkvgkedsss 87
                         90       100       110
                 ....*....|....*....|....*....|....
gi 568938658 139 -EFIEGRRRALKRFINLVARHPPFSEDVLLKLFL 171
Cdd:cd07281   88 aEFLERRRAALERYLQRIVSHPSLLQDPDVREFL 121
PX_SNX18 cd07286
The phosphoinositide binding Phox Homology domain of Sorting Nexin 18; The PX domain is a ...
88-177 6.16e-09

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: 53.90  E-value: 6.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938658  88 HVEYEVSSQRFKSSVYRRYNDFVVFHEVLLHKFPYRMVPALPPKRVLGA-DREFIEGRRRALKRFINLVARHPPFSEDVL 166
Cdd:cd07286   20 YISYKLVPSHTGLQVHRRYKHFDWLYARLAEKFPVISVPHIPEKQATGRfEEDFISKRRKGLIWWMDHMCSHPVLARCDA 99
                         90
                 ....*....|.
gi 568938658 167 LKLFLSFSGSD 177
Cdd:cd07286  100 FQHFLTCPSTD 110
BAR_SNX cd07596
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ...
182-406 2.00e-08

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: 54.28  E-value: 2.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938658 182 DIQTQFAMSRELIRNVYNSFYKLRDRAERIASRAIDNAADLLIFGKELSALG-SDTTPLpswaalhlstwGSLKQALKGL 260
Cdd:cd07596    1 EEDQEFEEAKDYILKLEEQLKKLSKQAQRLVKRRRELGSALGEFGKALIKLAkCEEEVG-----------GELGEALSKL 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938658 261 SVEFALLADRAAQQGKKEENDVVEKLNLFLDLLQSYKDLCERHEKgVLHKHQRALHKYGLMKRQM--MSAAHGREPESVE 338
Cdd:cd07596   70 GKAAEELSSLSEAQANQELVKLLEPLKEYLRYCQAVKETLDDRAD-ALLTLQSLKKDLASKKAQLekLKAAPGIKPAKVE 148
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568938658 339 QLESRIVEQEnvIQTMELRNYFSLYC---------LHQETQLVhvylpLTShILGAFVNSQIQGHKEMSKVWNDLKP 406
Cdd:cd07596  149 ELEEELEEAE--SALEEARKRYEEISerlkeelkrFHEERARD-----LKA-ALKEFARLQVQYAEKIAEAWESLLP 217
PX_SNX_like cd06865
The phosphoinositide binding Phox Homology domain of SNX-like proteins; The PX domain is a ...
100-172 7.30e-08

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: 50.88  E-value: 7.30e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568938658 100 SSVYRRYNDFVVFHEVLLHKFPYRMVPALPPKRVLGADR----EFIEGRRRALKRFINLVARHPPFSEDVLLKLFLS 172
Cdd:cd06865   42 FTVRRRFRDVVALADRLAEAYRGAFVPPRPDKSVVESQVmqsaEFIEQRRVALEKYLNRLAAHPVIGLSDELRVFLT 118
PX_SNARE cd06897
The phosphoinositide binding Phox Homology domain of SNARE proteins from fungi; The PX domain ...
78-172 7.95e-08

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: 50.35  E-value: 7.95e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938658  78 IPEKKGLFLKHVEYEVSSQ--RFKSSVYRRYNDFVVFHEVLLHKFPYRMVPALPPKRVLG---ADREFIEGRRRALKRFI 152
Cdd:cd06897    5 IPTTSVSPKPYTVYNIQVRlpLRSYTVSRRYSEFVALHKQLESEVGIEPPYPLPPKSWFLstsSNPKLVEERRVGLEAFL 84
                         90       100
                 ....*....|....*....|..
gi 568938658 153 N--LVARHPPFSEDVLLKLFLS 172
Cdd:cd06897   85 RalLNDEDSRWRNSPAVKEFLN 106
PX_SNX3_like cd06894
The phosphoinositide binding Phox Homology domain of Sorting Nexin 3 and related proteins; The ...
100-171 8.37e-08

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: 50.53  E-value: 8.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938658 100 SSVYRRYNDFVVFHEVLlHKFPYRMVPALPPKRVLGA----------DREFIEGRRRALKRFINLVARHPPFSEDVLLKL 169
Cdd:cd06894   38 SSVRRRYSDFEWLRSEL-ERDSKIVVPPLPGKALKRQlpfrgddgifEEEFIEERRKGLETFINKVAGHPLAQNEKCLHM 116

                 ..
gi 568938658 170 FL 171
Cdd:cd06894  117 FL 118
PX_CISK cd06870
The phosphoinositide binding Phox Homology Domain of Cytokine-Independent Survival Kinase; The ...
92-159 1.51e-07

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: 49.33  E-value: 1.51e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938658  92 EVSSQRFKSSVYRRYNDFVVFHEVLLHKFPyRMVPALPPKRVLGA--DREFIEGRRRALKRFINLVARHP 159
Cdd:cd06870   26 VVSVGRSSWFVFRRYAEFDKLYESLKKQFP-ASNLKIPGKRLFGNnfDPDFIKQRRAGLDEFIQRLVSDP 94
PX_SNX30 cd07283
The phosphoinositide binding Phox Homology domain of Sorting Nexin 30; The PX domain is a ...
101-172 2.51e-07

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: 48.93  E-value: 2.51e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568938658 101 SVYRRYNDFVVFHEVLLHKFPYRMVPALPPKRVLGA--DR---EFIEGRRRALKRFINLVARHPPFSEDVLLKLFLS 172
Cdd:cd07283   38 SVRRRYQDFDWLRNKLEESQPTHLIPPLPEKFVVKGvvDRfseEFVETRRKALDKFLKRIADHPVLSFNEHFNVFLT 114
PX_RUN cd07277
The phosphoinositide binding Phox Homology domain of uncharacterized proteins containing PX ...
101-155 3.34e-07

The phosphoinositide binding Phox Homology domain of uncharacterized proteins containing PX and RUN domains; The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to PI-enriched membranes. Members in this subfamily are uncharacterized proteins containing an N-terminal RUN domain and a C-terminal 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. The RUN domain is found in GTPases in the Rap and Rab families and may play a role in Ras-like signaling pathways.


Pssm-ID: 132810  Cd Length: 118  Bit Score: 48.88  E-value: 3.34e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568938658 101 SVYRRYNDFVVFHEVLLHKFPYRMVPALPPKRVLG-ADREFIEGRRRALKRFINLV 155
Cdd:cd07277   33 NVYRRYSEFYELHKKLKKKFPVVRSFDFPPKKAIGnKDAKFVEERRKRLQVYLRRV 88
PX_SNX14 cd06877
The phosphoinositide binding Phox Homology domain of Sorting Nexin 14; The PX domain is a ...
101-172 3.51e-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: 3.51e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568938658 101 SVYRRYNDFVVFhEVLLHKFPYRMVPA-LPPKRVLGA-DREFIEGRRRALKRFINLVARHPPFSEDVLLKLFLS 172
Cdd:cd06877   45 SVLRRYNEFYVL-ESKLTEFHGEFPDApLPSRRIFGPkSYEFLESKREIFEEFLQKLLQKPELRGSELLYDFLS 117
PX_SNX10 cd06898
The phosphoinositide binding Phox Homology domain of Sorting Nexin 10; The PX domain is a ...
87-171 3.89e-07

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: 48.48  E-value: 3.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938658  87 KHVEYEVSSQ-------RFKSSVYRRYNDFVVFHEVLLHKFPYRMVPALPPKRVLGA--DREFIEGRRRALKRFINLVAR 157
Cdd:cd06898   17 SYTDYEIFLHtnsmcftLKTSCVRRRYSEFVWLRNRLQKNALLIQLPSLPPKNLFGRfnNEGFIEERQQGLQDFLEKVLQ 96
                         90
                 ....*....|....
gi 568938658 158 HPPFSEDVLLKLFL 171
Cdd:cd06898   97 TPLLLSDSRLHLFL 110
PX_p40phox cd06882
The phosphoinositide binding Phox Homology domain of the p40phox subunit of NADPH oxidase; The ...
80-177 9.02e-07

The phosphoinositide binding Phox Homology domain of the p40phox subunit of NADPH oxidase; The PX domain is a phosphoinositide binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. p40phox contains an N-terminal PX domain, a central SH3 domain that binds p47phox, and a C-terminal PB1 domain that interacts with p67phox. It is a cytosolic subunit of the phagocytic NADPH oxidase complex (also called Nox2 or gp91phox) which plays a crucial role in the cellular response to bacterial infection. NADPH oxidase catalyzes the transfer of electrons from NADPH to oxygen during phagocytosis forming superoxide and reactive oxygen species. p40phox positively regulates NADPH oxidase in both phosphatidylinositol-3-phosphate (PI3P)-dependent and PI3P-independent manner. The PX domain is a phospholipid-binding module involved in the membrane targeting of proteins. The p40phox PX domain binds to PI3P, an abundant lipid in phagosomal membranes, playing an important role in the localization of NADPH oxidase. The PX domain of p40phox is also involved in protein-protein interaction.


Pssm-ID: 132792  Cd Length: 123  Bit Score: 47.82  E-value: 9.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938658  80 EKKGLFLKHVEY--EV---SSQRFKssVYRRYNDFVVFHEVLLHKFPY--------RMVPALPPKRVLGADREFIEGRRR 146
Cdd:cd06882   12 EEKRGFTNYYVFviEVktkGGSKYL--IYRRYRQFFALQSKLEERFGPeagssaydCTLPTLPGKIYVGRKAEIAERRIP 89
                         90       100       110
                 ....*....|....*....|....*....|..
gi 568938658 147 ALKRFI-NLVARHPPFSEDVLLKLFLSFSGSD 177
Cdd:cd06882   90 LLNRYMkELLSLPVWVLMDEDVRLFFYQTESD 121
PX_SNX15_like cd06881
The phosphoinositide binding Phox Homology domain of Sorting Nexin 15-like proteins; The PX ...
88-170 7.40e-06

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: 45.00  E-value: 7.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938658  88 HVEYEVSSQRFK---------SSVYRRYNDFVVFHEVL--LHKFPYR--MVPALPPKRVLGA-DREFIEGRRRALKRFIN 153
Cdd:cd06881   17 YTEYKITSKVFSrsvpedvseVVVWKRYSDFKKLHRELsrLHKQLYLsgSFPPFPKGKYFGRfDAAVIEERRQAILELLD 96
                         90
                 ....*....|....*..
gi 568938658 154 LVARHPPFSEDVLLKLF 170
Cdd:cd06881   97 FVGNHPALYQSSAFQQF 113
PX_UP1_plant cd06879
The phosphoinositide binding Phox Homology domain of uncharacterized plant proteins; The PX ...
102-171 2.37e-05

The phosphoinositide binding Phox Homology domain of uncharacterized plant 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: 132789  Cd Length: 138  Bit Score: 43.86  E-value: 2.37e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568938658 102 VYRRYNDFVVFHEVLLHKFPYRMVPALPPKRVL-GADREFIEGRRRALKRFINLVARHPPFSEDVLLKLFL 171
Cdd:cd06879   65 VLRRFNDFLKLHTDLKKLFPKKKLPAAPPKGLLrMKNRALLEERRHSLEEWMGKLLSDIDLSRSVPVASFL 135
PX_KIF16B_SNX23 cd06874
The phosphoinositide binding Phox Homology domain of KIF16B kinesin or Sorting Nexin 23; The ...
88-159 2.90e-05

The phosphoinositide binding Phox Homology domain of KIF16B kinesin or Sorting Nexin 23; 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. KIF16B, also called sorting nexin 23 (SNX23), is a family-3 kinesin which harbors an N-terminal kinesin motor domain containing ATP and microtubule binding sites, a ForkHead Associated (FHA) domain, and a C-terminal PX domain. The PX domain of KIF16B binds to phosphatidylinositol-3-phosphate (PI3P) in early endosomes and plays a role in the transport of early endosomes to the plus end of microtubules. By regulating early endosome plus end motility, KIF16B modulates the balance between recycling and degradation of receptors. 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: 132784  Cd Length: 127  Bit Score: 43.52  E-value: 2.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938658  88 HVEYEVSSQRF--KSSVYRRYNDFVVFHEVLLHKFPyrMVPAL--PPKRVLGA-DREFIEGRRRA----LKRFINLVARH 158
Cdd:cd06874   18 HFEFEVKITVLdeTWTVFRRYSRFRELHKTMKLKYP--EVAALefPPKKLFGNkSERVAKERRRQletyLRNFFSVCLKL 95

                 .
gi 568938658 159 P 159
Cdd:cd06874   96 P 96
PX_UP2_fungi cd06869
The phosphoinositide binding Phox Homology domain of uncharacterized fungal proteins; The PX ...
102-172 4.02e-05

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: 42.65  E-value: 4.02e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568938658 102 VYRRYNDFVVFHEVLLHKFPYRMVPALPPKrvlgaDREFIEGRRRALKRFINLVARHPPFSEDVLLKLFLS 172
Cdd:cd06869   52 VARRYSDFKKLHHDLKKEFPGKKLPKLPHK-----DKLPREKLRLSLRQYLRSLLKDPEVAHSSILQEFLT 117
PX_SNX13 cd06873
The phosphoinositide binding Phox Homology domain of Sorting Nexin 13; The PX domain is a ...
102-155 4.79e-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: 42.64  E-value: 4.79e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568938658 102 VYRRYNDFVVFHEVLLHKFPYRMVPALPPKRVL-GADREFIEGRRRALKRFINLV 155
Cdd:cd06873   43 VYRRYSDFHDLHMRLKEKFPNLSKLSFPGKKTFnNLDRAFLEKRRKMLNQYLQSL 97
PX_SNX3 cd07293
The phosphoinositide binding Phox Homology domain of Sorting Nexin 3; The PX domain is a ...
99-171 4.99e-05

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: 42.67  E-value: 4.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938658  99 KSSVYRRYNDFVVFHEVLlHKFPYRMVPALPPKRVLGA----------DREFIEGRRRALKRFINLVARHPPFSEDVLLK 168
Cdd:cd07293   37 ESTVRRRYSDFEWLRSEL-ERESKVVVPPLPGKALFRQlpfrgddgifDDSFIEERKQGLEQFLNKVAGHPLAQNERCLH 115

                 ...
gi 568938658 169 LFL 171
Cdd:cd07293  116 MFL 118
PX_PI3K_C2_68D cd06884
The phosphoinositide binding Phox Homology Domain of Class II Phosphoinositide 3-Kinases ...
78-160 7.89e-05

The phosphoinositide binding Phox Homology Domain of Class II Phosphoinositide 3-Kinases similar to the Drosophila PI3K_68D protein; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. The Phosphoinositide 3-Kinase (PI3K) family of enzymes catalyzes the phosphorylation of the 3-hydroxyl group of the inositol ring of phosphatidylinositol. PI3Ks play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation and apoptosis. PI3Ks are divided into three main classes (I, II, and III) based on their substrate specificity, regulation, and domain structure. Class II PI3Ks preferentially use PI as a substrate to produce PI3P, but can also phosphorylate PI4P to produce PI(3,4)P2. They function as monomers and do not associate with any regulatory subunits. Class II enzymes contain an N-terminal Ras binding domain, a lipid binding C2 domain, a PI3K homology domain of unknown function, an ATP-binding cataytic domain, a PX domain, and a second C2 domain at the C-terminus. PI3K_68D is a novel PI3K which is widely expressed throughout the Drosophila life cycle. In vitro, it has been shown to phosphorylate PI and PI4P. It is involved in signaling pathways that affect pattern formation of Drosophila wings.


Pssm-ID: 132794  Cd Length: 111  Bit Score: 41.63  E-value: 7.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938658  78 IPEKKGLFLKHVEYEvsSQRFKSSVYRRYNDFVVFHEVLLHKFPYRMVPALPPKRVLGA--DREFIEGRRRALKRFINLV 155
Cdd:cd06884   14 DPEKYYVYVVEVTRE--NQASPQHVFRTYKEFLELYQKLCRKFPLAKLHPLSTGSHVGRsnIKSVAEKRKQDIQQFLNSL 91

                 ....*
gi 568938658 156 ARHPP 160
Cdd:cd06884   92 FKMAE 96
PX_HS1BP3 cd06868
The phosphoinositide binding Phox Homology domain of HS1BP3; The PX domain is a ...
88-171 1.03e-04

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: 41.63  E-value: 1.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938658  88 HVEYEV----SSQRFKSSVYR-----------RYNDFVVFHEVLLHKFPYRMVPALPPKRVLGADREfIEGRRRALKRFI 152
Cdd:cd06868   20 HVLYQIvvvtRLAAFKSAKHKeedvvqfmvskKYSEFEELYKKLSEKYPGTILPPLPRKALFVSESD-IRERRAAFNDFM 98
                         90
                 ....*....|....*....
gi 568938658 153 NLVARHPPFSEDVLLKLFL 171
Cdd:cd06868   99 RFISKDEKLANCPELLEFL 117
PX_MDM1p cd06876
The phosphoinositide binding Phox Homology domain of yeast MDM1p; The PX domain is a ...
102-172 1.16e-04

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: 41.91  E-value: 1.16e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568938658 102 VYRRYNDFVVFHEVLLHKFPYRMVPALPPKRVLG---ADREFIEGRRRALKRFINLVARHPPFSEDVLLKLFLS 172
Cdd:cd06876   59 VARRYSEFLELHKYLKKRYPGVLKLDFPQKRKISlkySKTLLVEERRKALEKYLQELLKIPEVCEDEEFRKFLS 132
PX_SNX17_31 cd06885
The phosphoinositide binding Phox Homology domain of Sorting Nexins 17 and 31; The PX domain ...
105-159 5.86e-04

The phosphoinositide binding Phox Homology domain of Sorting Nexins 17 and 31; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Members of this subfamily include sorting nexin 17 (SNX17), SNX31, and similar proteins. They contain an N-terminal PX domain followed by a truncated FERM (4.1, ezrin, radixin, and moesin) domain and a unique C-terminal region. 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. SNX17 is known to regulate the trafficking and processing of a number of proteins. It binds some members of the low-density lipoprotein receptor (LDLR) family such as LDLR, VLDLR, ApoER2, and others, regulating their endocytosis. It also binds P-selectin and may regulate its lysosomal degradation. SNX17 is highly expressed in neurons. It binds amyloid precursor protein (APP) and may be involved in its intracellular trafficking and processing to amyloid beta peptide, which plays a central role in the pathogenesis of Alzheimer's disease. The biological function of SNX31 is unknown.


Pssm-ID: 132795  Cd Length: 104  Bit Score: 39.24  E-value: 5.86e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568938658 105 RYNDFVVFHEVLLHKFPYRMVPALPPKRVLGADREFIEGRRRALKRFINLVARHP 159
Cdd:cd06885   34 RYSQLHGLNEQLKKEFGNRKLPPFPPKKLLPLTPAQLEERRLQLEKYLQAVVQDP 88
PX_IRAS cd06875
The phosphoinositide binding Phox Homology domain of the Imidazoline Receptor ...
92-155 1.24e-03

The phosphoinositide binding Phox Homology domain of the Imidazoline Receptor Antisera-Selected; 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. Imidazoline Receptor Antisera-Selected (IRAS), also called nischarin, contains an N-terminal PX domain, leucine rich repeats, and a predicted coiled coil domain. The PX domain of IRAS binds to phosphatidylinositol-3-phosphate in membranes. Together with the coiled coil domain, it is essential for the localization of IRAS to endosomes. IRAS has been shown to interact with integrin and inhibit cell migration. Its interaction with alpha5 integrin causes a redistribution of the receptor from the cell surface to endosomal structures, suggesting that IRAS may function as a sorting nexin (SNX) which regulates the endosomal trafficking of integrin. 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. 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: 132785  Cd Length: 116  Bit Score: 38.41  E-value: 1.24e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568938658  92 EVSSQRFKSSVYRRYNDFVVFHEVLL--HKFPYRMvpaLPPKRVLG-ADREFIEGRRRALKRFINLV 155
Cdd:cd06875   23 EVKVGSVEWTVKHRYSDFAELHDKLVaeHKVDKDL---LPPKKLIGnKSPSFVEKRRKELEIYLQTL 86
PX_SNX22 cd06880
The phosphoinositide binding Phox Homology domain of Sorting Nexin 22; The PX domain is a ...
99-183 1.28e-03

The phosphoinositide binding Phox Homology domain of Sorting Nexin 22; 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. SNX22 may be involved in recruiting other proteins to the membrane via protein-protein and protein-ligand interaction. The biological function of SNX22 is not yet known.


Pssm-ID: 132790  Cd Length: 110  Bit Score: 38.41  E-value: 1.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938658  99 KSSVYRRYNDFVVFHEVLLHKFPyrmVPALPPKRVLGADREFIEGRRRALKRFINLVARHppfseDVLLKLFLSFSGSDF 178
Cdd:cd06880   32 RHTVEKRYSEFHALHKKLKKSIK---TPDFPPKRVRNWNPKVLEQRRQGLEAYLQGLLKI-----NELPKQLLDFLGVRH 103

                 ....*
gi 568938658 179 LPADI 183
Cdd:cd06880  104 FPSLP 108
PX_SNX20 cd07300
The phosphoinositide binding Phox Homology domain of Sorting Nexin 20; The PX domain is a ...
87-155 1.62e-03

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: 38.26  E-value: 1.62e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568938658  87 KHVEYEV------SSQRFKSSVYRRYNDFVVFHEVLLHKFPYRMVPALPPKRVLGAD--REFIEGRRRALKRFINLV 155
Cdd:cd07300   17 KHVVYQIiviqtgSFDCNKVVIERRYSDFLKLHQELLSDFSEELEDVVFPKKKLTGNfsEEIIAERRVALRDYLTLL 93
PX_FISH cd06888
The phosphoinositide binding Phox Homology domain of Five SH protein; The PX domain is a ...
73-150 2.51e-03

The phosphoinositide binding Phox Homology domain of Five SH protein; 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. Five SH (FISH), also called Tks5, is a scaffolding protein and Src substrate that is localized in podosomes, which are electron-dense structures found in Src-transformed fibroblasts, osteoclasts, macrophages, and some invasive cancer cells. FISH contains an N-terminal PX domain and five Src homology 3 (SH3) domains. FISH binds and regulates some members of the ADAMs family of transmembrane metalloproteases, which function as sheddases and mediators of cell and matrix interactions. It is required for podosome formation, degradation of the extracellular matrix, and cancer cell invasion. This subfamily also includes proteins with a different number of SH3 domains than FISH, such as Tks4, which contains four SH3 domains instead of five. The Tks4 adaptor protein is required for the formation of functional podosomes. It has overlapping, but not identical, functions as FISH. The PX domain is involved in targeting of proteins to PI-enriched membranes, and may also be involved in protein-protein interaction.


Pssm-ID: 132798  Cd Length: 119  Bit Score: 37.79  E-value: 2.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938658  73 VQVELIPEKKGLFLKHVEYEVSSQrfkSSVYRRYNDFVVFHEVLLHKFP---------YRMVPALPPKRVLGadREFIeg 143
Cdd:cd06888    9 VEKRRAPSKHYVYIINVTWSDGSS---NVIYRRYSKFFDLQMQLLDKFPieggqkdpsQRIIPFLPGKILFR--RSHI-- 81

                 ....*..
gi 568938658 144 RRRALKR 150
Cdd:cd06888   82 RDVAVKR 88
PX_SNX12 cd07294
The phosphoinositide binding Phox Homology domain of Sorting Nexin 12; The PX domain is a ...
99-171 3.77e-03

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: 37.33  E-value: 3.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938658  99 KSSVYRRYNDFVVFHEVLlHKFPYRMVPALPPKRVLGA----------DREFIEGRRRALKRFINLVARHPPFSEDVLLK 168
Cdd:cd07294   39 ESCVRRRYSDFEWLKNEL-ERDSKIVVPPLPGKALKRQlpfrgdegifEESFIEERRQGLEQFINKIAGHPLAQNERCLH 117

                 ...
gi 568938658 169 LFL 171
Cdd:cd07294  118 MFL 120
PX_SNX20_21_like cd07279
The phosphoinositide binding Phox Homology domain of Sorting Nexins 20 and 21; The PX domain ...
87-171 4.34e-03

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: 36.92  E-value: 4.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938658  87 KHVEYEVSSQR------FKSSVYRRYNDFVVFHEVLLHKFPYRMVPALPPKRVLGA--DREFIEGRRRALKRFINLVARH 158
Cdd:cd07279   17 KYVVYQLAVVQtgdpdtQPAFIERRYSDFLKLYKALRKQHPQLMAKVSFPRKVLMGnfSSELIAERSRAFEQFLGHILSI 96
                         90
                 ....*....|...
gi 568938658 159 PPFSEDVLLKLFL 171
Cdd:cd07279   97 PNLRDSKAFLDFL 109
PX_p47phox cd06887
The phosphoinositide binding Phox Homology domain of the p47phox subunit of NADPH oxidase; The ...
78-160 7.52e-03

The phosphoinositide binding Phox Homology domain of the p47phox subunit of NADPH oxidase; 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. p47phox is a cytosolic subunit of the phagocytic NADPH oxidase complex (also called Nox2 or gp91phox), which plays a key role in the ability of phagocytes to defend against bacterial infections. NADPH oxidase catalyzes the transfer of electrons from NADPH to oxygen during phagocytosis forming superoxide and reactive oxygen species. p47phox is required for activation of NADH oxidase and plays a role in translocation. It contains an N-terminal PX domain, two Src Homology 3 (SH3) domains, and a C-terminal domain that contains PxxP motifs for binding SH3 domains. The PX domain of p47phox is unique in that it contains two distinct basic pockets on the membrane-binding surface: one preferentially binds phosphatidylinositol-3,4-bisphosphate [PI(3,4)P2] and is analogous to the PI3P-binding pocket of p40phox, while the other binds anionic phospholipids such as phosphatidic acid or phosphatidylserine. Simultaneous binding in the two pockets results in increased membrane affinity. The PX domain of p47phox is also involved in protein-protein interaction.


Pssm-ID: 132797  Cd Length: 118  Bit Score: 36.35  E-value: 7.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568938658  78 IPEKKGLFLKHVEYEVSSQRFkssVYRRYNDFVVFHEVLLHKFP---------YRMVPALPPKRVLGADREfIEGRRRAL 148
Cdd:cd06887   14 VPSQHYVYMFLVKWQDLSEKL---VYRRFTEIYEFHKTLKEMFPieagdinkeNRIIPHLPAPKWFDGQRA-AENRQGTL 89
                         90
                 ....*....|..
gi 568938658 149 KRFINLVARHPP 160
Cdd:cd06887   90 TEYCSTLLSLPP 101
 
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.
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