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Conserved domains on  [gi|1034562449|ref|XP_016857995|]
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SH3-containing GRB2-like protein 3-interacting protein 1 isoform X1 [Homo sapiens]

Protein Classification

SGIP1_MHD domain-containing protein( domain architecture ID 10174180)

SGIP1_MHD domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SGIP1_MHD cd09266
mu-homology domain (MHD) of Scr homology 3 (SH3)-domain growth factor receptor-bound 2 (GRB2) ...
 583-849 0e+00

mu-homology domain (MHD) of Scr homology 3 (SH3)-domain growth factor receptor-bound 2 (GRB2)-like (endophilin) interacting protein 1 (also known as endophilin-3-interacting protein, SGIP1) and similar proteins; This family corresponds to the MHD found in mammalian neuronal-specific transcript SGIP1 and similar proteins. Unlike other members in this family, SGIP1 does not contain EFC/F-BAR domain, but does have a proline-rich domain (PRD) and a C-terminal MHD. It is an endophilin-interacting protein that plays an obligatory role in the regulation of energy homeostasis, and is also involved in clathrin-mediated endocytosis by interacting with phospholipids and eps15.


:

Pssm-ID: 271172  Cd Length: 267  Bit Score: 580.47  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562449 583 PVAAAFTETVNAYFKGADPSKCIVKITGEMVLSFPAGITRHFANNPSPAALTFRVINFSRLEHVLPNPQLLCCDNTQNDA 662
Cdd:cd09266     1 PVAAAFTETVNAYFKGADPSKCIVKITGEMVLSFPAGITRHFANNPSPAALTFRITNYSRLEHVLPNPQLLCCDNTQAKG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562449 663 NTKEFWVNMPNLMTHLKKVSEQKPQATYYNVDMLKYQVSAQGIQSTPLNLAVNWRCEPSSTDLRIDYKYNTDAMTTAVAL 742
Cdd:cd09266    81 NAKEFWVNMPNLMTHLKKVSEQKPQATYYNVDMLKYQVSAQGPQSTPLNLAVSWRCEPSSTDLRIDYKYNGDAMTTPVAL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562449 743 NNVQFLVPIDGGVTKLQAVLPPAVWNAEQQRILWKIPDISQKSENGGVGSLLARFQLSEGPSKPSPLVVQFTSEGSTLSG 822
Cdd:cd09266   161 NNVQFLVPIDGGVTKLQAVLPPAVWNAEQQRILWKIPDISQKSENGGVGSLLARFQLSEGPSKPAPLAVQFTSEGSTLSG 240

                         250       260
                  ....*....|....*....|....*..
gi 1034562449 823 CDIELVGAGYRFSLIKKRFAAGKYLAD 849
Cdd:cd09266   241 CDIELVGPGYRFSLIKKRFAAGKYLAD 267
 
Name Accession Description Interval E-value
SGIP1_MHD cd09266
mu-homology domain (MHD) of Scr homology 3 (SH3)-domain growth factor receptor-bound 2 (GRB2) ...
 583-849 0e+00

mu-homology domain (MHD) of Scr homology 3 (SH3)-domain growth factor receptor-bound 2 (GRB2)-like (endophilin) interacting protein 1 (also known as endophilin-3-interacting protein, SGIP1) and similar proteins; This family corresponds to the MHD found in mammalian neuronal-specific transcript SGIP1 and similar proteins. Unlike other members in this family, SGIP1 does not contain EFC/F-BAR domain, but does have a proline-rich domain (PRD) and a C-terminal MHD. It is an endophilin-interacting protein that plays an obligatory role in the regulation of energy homeostasis, and is also involved in clathrin-mediated endocytosis by interacting with phospholipids and eps15.


Pssm-ID: 271172  Cd Length: 267  Bit Score: 580.47  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562449 583 PVAAAFTETVNAYFKGADPSKCIVKITGEMVLSFPAGITRHFANNPSPAALTFRVINFSRLEHVLPNPQLLCCDNTQNDA 662
Cdd:cd09266     1 PVAAAFTETVNAYFKGADPSKCIVKITGEMVLSFPAGITRHFANNPSPAALTFRITNYSRLEHVLPNPQLLCCDNTQAKG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562449 663 NTKEFWVNMPNLMTHLKKVSEQKPQATYYNVDMLKYQVSAQGIQSTPLNLAVNWRCEPSSTDLRIDYKYNTDAMTTAVAL 742
Cdd:cd09266    81 NAKEFWVNMPNLMTHLKKVSEQKPQATYYNVDMLKYQVSAQGPQSTPLNLAVSWRCEPSSTDLRIDYKYNGDAMTTPVAL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562449 743 NNVQFLVPIDGGVTKLQAVLPPAVWNAEQQRILWKIPDISQKSENGGVGSLLARFQLSEGPSKPSPLVVQFTSEGSTLSG 822
Cdd:cd09266   161 NNVQFLVPIDGGVTKLQAVLPPAVWNAEQQRILWKIPDISQKSENGGVGSLLARFQLSEGPSKPAPLAVQFTSEGSTLSG 240

                         250       260
                  ....*....|....*....|....*..
gi 1034562449 823 CDIELVGAGYRFSLIKKRFAAGKYLAD 849
Cdd:cd09266   241 CDIELVGPGYRFSLIKKRFAAGKYLAD 267
muHD pfam10291
Muniscin C-terminal mu homology domain; The muniscins are a family of endocytic adaptors that ...
 582-847 9.52e-93

Muniscin C-terminal mu homology domain; The muniscins are a family of endocytic adaptors that is conserved from yeast to humans.This C-terminal domain is structurally similar to mu homology domains, and is the region of the muniscin proteins involved in the interactions with the endocytic adaptor-scaffold proteins Ede1-eps15. This interaction influences muniscin localization. The muniscins provide a combined adaptor-membrane-tubulation activity that is important for regulating endocytosis.


Pssm-ID: 463046  Cd Length: 255  Bit Score: 292.30  E-value: 9.52e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562449 582 LPVAAAFTETVNAYFKGADPSKciVKITGEMVLSFPAGITRHFannPSPAALTFRVINFSRLEHVLPNPQLLCcDNTQND 661
Cdd:pfam10291   1 PGLNASIAETVNAWFKDGDVTK--SKVTGEVALSYPAGIAASF---TPPAVLNFRLNNFSRLEKVAPNPAFVT-DESQSD 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562449 662 AntkEFWVNMPNLMTHLKKVSeqkpqatyynvdmLKYQVSAQG-IQSTPLNLAVNWRCEPSSTDLRIDYKYN-TDAMTTA 739
Cdd:pfam10291  75 G---EFKVNPQFLASRTPLGA-------------LKYQVHIDPlSASCPLILHPVWKCEPHQASLILTYSLNpSLAIASA 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562449 740 VALNNVQFLVPIDGG-VTKLQAvLPPAVWNAEQQRILWKIPDISQKSENGGvGSLLARFQLSEGPSKPSPLVVQFTSE-G 817
Cdd:pfam10291 139 VVLENLQVVVNLDGShATSAQS-KPQGTFNKEKSRITWKLPELSLTSDGDG-GKLIARFMTEGGASKPGGVAVKFEIEtG 216

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1034562449 818 STLSGCDIELV---------GAGYRFSLIKKRFAAGKYL 847
Cdd:pfam10291 217 DTLSGLGISLVdqvdeedpfGGGWKLVPTKRRLAAGKYL 255
 
Name Accession Description Interval E-value
SGIP1_MHD cd09266
mu-homology domain (MHD) of Scr homology 3 (SH3)-domain growth factor receptor-bound 2 (GRB2) ...
 583-849 0e+00

mu-homology domain (MHD) of Scr homology 3 (SH3)-domain growth factor receptor-bound 2 (GRB2)-like (endophilin) interacting protein 1 (also known as endophilin-3-interacting protein, SGIP1) and similar proteins; This family corresponds to the MHD found in mammalian neuronal-specific transcript SGIP1 and similar proteins. Unlike other members in this family, SGIP1 does not contain EFC/F-BAR domain, but does have a proline-rich domain (PRD) and a C-terminal MHD. It is an endophilin-interacting protein that plays an obligatory role in the regulation of energy homeostasis, and is also involved in clathrin-mediated endocytosis by interacting with phospholipids and eps15.


Pssm-ID: 271172  Cd Length: 267  Bit Score: 580.47  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562449 583 PVAAAFTETVNAYFKGADPSKCIVKITGEMVLSFPAGITRHFANNPSPAALTFRVINFSRLEHVLPNPQLLCCDNTQNDA 662
Cdd:cd09266     1 PVAAAFTETVNAYFKGADPSKCIVKITGEMVLSFPAGITRHFANNPSPAALTFRITNYSRLEHVLPNPQLLCCDNTQAKG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562449 663 NTKEFWVNMPNLMTHLKKVSEQKPQATYYNVDMLKYQVSAQGIQSTPLNLAVNWRCEPSSTDLRIDYKYNTDAMTTAVAL 742
Cdd:cd09266    81 NAKEFWVNMPNLMTHLKKVSEQKPQATYYNVDMLKYQVSAQGPQSTPLNLAVSWRCEPSSTDLRIDYKYNGDAMTTPVAL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562449 743 NNVQFLVPIDGGVTKLQAVLPPAVWNAEQQRILWKIPDISQKSENGGVGSLLARFQLSEGPSKPSPLVVQFTSEGSTLSG 822
Cdd:cd09266   161 NNVQFLVPIDGGVTKLQAVLPPAVWNAEQQRILWKIPDISQKSENGGVGSLLARFQLSEGPSKPAPLAVQFTSEGSTLSG 240

                         250       260
                  ....*....|....*....|....*..
gi 1034562449 823 CDIELVGAGYRFSLIKKRFAAGKYLAD 849
Cdd:cd09266   241 CDIELVGPGYRFSLIKKRFAAGKYLAD 267
AP_Syp1_like_MHD cd09265
Mu-homology domain (MHD) of endocytic adaptor protein (AP), Syp1; This family corresponds to ...
 583-849 5.15e-173

Mu-homology domain (MHD) of endocytic adaptor protein (AP), Syp1; This family corresponds to the MHD found in the metazoan counterparts of yeast Syp1, which includes two ubiquitously expressed membrane-sculpting F-BAR domain-containing Fer/Cip4 homology domain-only proteins 1 and 2 (FCH domain only 1 and 2, or FCHo1/FCHo2), neuronal-specific SH3-containing GRB2-like protein 3-interacting protein 1 (SGIP1), and related uncharacterized proteins. FCHo1/FCHo2 represent key initial proteins ultimately controlling cellular nutrient uptake, receptor regulation, and synaptic vesicle retrieval. They are required for plasma membrane clathrin-coated vesicle (CCV) budding and marked sites of CCV formation. They bind specifically to the plasma membrane and recruit the scaffold proteins eps15 and intersectin, which subsequently engage the adaptor complex AP2 and clathrin, leading to coated vesicle formation. Both FCHo1/FCHo2 contain an N-terminal EFC/F-BAR domain that induces membrane tabulation, a proline-rich domain (PRD) in the middle region, and a C-terminal MHD responsible for the binding of eps15 and intersectin. Another mammalian neuronal-specific protein, neuronal-specific transcript Scr homology 3 (SH3)-domain growth factor receptor-bound 2 (GRB2)-like (endophilin) interacting protein 1 [SGIP1] does not contain EFC/F-BAR domain, but does have a PRD and a C-terminal MHD and has been classified into this family as well. SGIP1 is an endophilin-interacting protein that plays an obligatory role in the regulation of energy homeostasis. It is also involved in clathrin-mediated endocytosis by interacting with phospholipids and eps15.


Pssm-ID: 271171  Cd Length: 266  Bit Score: 500.10  E-value: 5.15e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562449 583 PVAAAFTETVNAYFKGADPSKCIVKITGEMVLSFPAGITRHFANNPSPAALTFRVINFSRLEHVLPNPQLLCCDNTQNDA 662
Cdd:cd09265     1 PVAAAFTETVHAYFKGADPSKCIVKITGDMMMSFPAGIIRLLTSNPTPAPLTFRLKNASRLEHVLPNKQLIFSDPSQSDS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562449 663 NTKEFWVNMPNLMTHLKKVSEQKPQATYYNVDMLKYQVSAQGIQSTPLNLAVNWRCEPSSTDLRIDYKYNTDAMTTAVAL 742
Cdd:cd09265    81 ETKDFWFNMPALTTYLKRQAEQNPTASYYNVDVLKYQVSPTGPQSTPLQLASYWKCEPSSTDLRVDYKYNPEAMAIATPL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562449 743 NNVQFLVPIDGGVTKLQAVlPPAVWNAEQQRILWKIPDISQKSENGGVGSLLARFQLSEGPSKPSPLVVQFTSEGSTLSG 822
Cdd:cd09265   161 LNVQFSVPVDGGVTNVQSE-PPATWNAEQKRLLWKLPDISQNSEGGGVGSLRARFELSEGPSKPAPLAVQFNSEGTTLSG 239

                         250       260
                  ....*....|....*....|....*..
gi 1034562449 823 CDIELVGAGYRFSLIKKRFAAGKYLAD 849
Cdd:cd09265   240 VDIELVGSGYRLSLIKKRFAAGKYLCD 266
FCHo2_MHD cd09267
mu-homology domain (MHD) of F-BAR domain-containing Fer/Cip4 homology domain-only protein 2 ...
 583-849 5.30e-147

mu-homology domain (MHD) of F-BAR domain-containing Fer/Cip4 homology domain-only protein 2 (FCH domain only 2 or FCHo2) and similar proteins; This family corresponds to the MHD found in the ubiquitously expressed mammalian membrane-sculpting FCHo2 and similar proteins. FCHo2 represents a key initial protein that ultimately controls cellular nutrient uptake, receptor regulation, and synaptic vesicle retrieval. It is required for plasma membrane clathrin-coated vesicle (CCV) budding and marks sites of CCV formation. It binds specifically to the plasma membrane and recruits the scaffold proteins eps15 and intersectin, which subsequently engages the adaptor complex AP2 and clathrin, leading to coated vesicle formation. FCHo2 contains an N-terminal EFC/F-BAR domain, a proline-rich domain (PRD) in the middle region, and a C-terminal MHD. The crescent-shaped EFC/F-BAR domain can form an antiparallel dimer structure that binds PtdIns(4,5)P2-enriched membranes and can polymerize into rings to generate membrane tubules. The MHD is structurally related to the cargo-binding mu2 subunit of adaptor complex 2 (AP-2) and is responsible for the binding of eps15 and intersectin.


Pssm-ID: 211378  Cd Length: 267  Bit Score: 433.68  E-value: 5.30e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562449 583 PVAAAFTETVNAYFKGADPSKCIVKITGEMVLSFPAGITRHFANNPSPAALTFRVINFSRLEHVLPNPQLLCCDNTQNDA 662
Cdd:cd09267     1 PVAVALTESVNAYFKGADPTKCIVKITGDMTVSFPSGIIKVFTSNPSPAVLCFRLKNTSRLEQILPNAQLLYSDPSQSDS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562449 663 NTKEFWVNMPNLMTHLKKVSEQKPQATYYNVDMLKYQVSAQGIQSTPLNLAVNWRCEPSSTDLRIDYKYNTDAMTTAVAL 742
Cdd:cd09267    81 NTKDFWMNMQAVTVYLKKSSEQNPAASYYNVDILKYQVSSNGIQSTPLNLATYWKCSASTTDLRVDYKYNPEAMQPPSPL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562449 743 NNVQFLVPIDGGVTKLQAvLPPAVWNAEQQRILWKIPDISQKSENGGVGSLLARFQLSEGPSKPSPLVVQFTSEGSTLSG 822
Cdd:cd09267   161 SNVQVLVPVDGGVTNMQS-LPPAIWNAEQMKALWKLSSISEKSENGGSGSLRAKFELSEGPSKPATLAVQFFSEGSTLSG 239

                         250       260
                  ....*....|....*....|....*..
gi 1034562449 823 CDIELVGAGYRFSLIKKRFAAGKYLAD 849
Cdd:cd09267   240 VDMELVGTGYRLSLNKKRFATGRYMAD 266
FCHo1_MHD cd09268
mu-homology domain (MHD) of F-BAR domain-containing Fer/Cip4 homology domain-only protein 1 ...
 583-848 5.20e-110

mu-homology domain (MHD) of F-BAR domain-containing Fer/Cip4 homology domain-only protein 1 (FCH domain only 1 or FCHo1, also known as KIAA0290) and similar proteins; This family corresponds to the MHD found in ubiquitously expressed mammalian membrane-sculpting FCHo1 and similar proteins. FCHo1 represents a key initial protein that ultimately controls cellular nutrient uptake, receptor regulation, and synaptic vesicle retrieval. It is required for plasma membrane clathrin-coated vesicle (CCV) budding and marks sites of CCV formation. It binds specifically to the plasma membrane and recruits the scaffold proteins eps15 and intersectin, which subsequently engage the adaptor complex AP2 and clathrin, leading to coated vesicle formation. FCHo1 contains an N-terminal EFC/F-BAR domain, a proline-rich domain (PRD) in the middle region, and a C-terminal MHD. The crescent-shaped EFC/F-BAR domain can form an antiparallel dimer structure that binds PtdIns(4,5)P2-enriched membranes and can polymerize into rings to generate membrane tubules. The MHD is structurally related to the cargo-binding mu2 subunit of adaptor complex 2 (AP-2) and is responsible for the binding of eps15 and intersectin. Unlike other F-BAR domain containing proteins, FCHo1 has neither the Src homology 3 (SH3) domain nor any other known domain for interaction with dynamin and actin cytoskeleton. However, it can periodically accumulate at the budding site of clathrin. FCHo1 may utilize a unique action mode for vesicle formation as compared with other F-BAR proteins.


Pssm-ID: 271173  Cd Length: 265  Bit Score: 337.71  E-value: 5.20e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562449 583 PVAAAFTETVNAYFKGADPSKCIVKITGEMVLSFPAGITRHFANNPSPAALTFRVINFSRLEHVLPNPQLLCCDNTQNDA 662
Cdd:cd09268     1 PVAAAFTEYVHAYFRGGALEGCLLRITGELTMSFPAGILRVFASTPTPPVLSFRLVHTSHVEHFAPNSELLFSDPSQSDP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562449 663 NTKEFWVNMPNLMTHLKKVSEQKPQATYYNVDMLKYQVSAQGIQSTPLNLAVNWRCEPSSTDLRIDYKYNTdAMTTAVAL 742
Cdd:cd09268    81 NTKDFWLNMPALTSYLQRMAEQNPQASYYNVTLLKYQVSKSGPSAAPLYLSATWQCGPTSTDVSLDYRQNP-ATAPATFL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562449 743 NNVQFLVPIDGGVTKLQAVlPPAVWNAEQQRILWKIPDISQKSENGGVGSLLARFQLSEGPSKPSPLVVQFTSEGSTLSG 822
Cdd:cd09268   160 TDVQILLPLDEPFTNLQSQ-PPAAWNAEERRLHWQLPHESAGNEHDGSGRLCASWQPLHAPSRPTSAAAQFTSEGSTLSG 238

                         250       260
                  ....*....|....*....|....*.
gi 1034562449 823 CDIELVGAGYRFSLIKKRFAAGKYLA 848
Cdd:cd09268   239 VDIELVGSGYRMSLVKKRFATGKYLV 264
muHD pfam10291
Muniscin C-terminal mu homology domain; The muniscins are a family of endocytic adaptors that ...
 582-847 9.52e-93

Muniscin C-terminal mu homology domain; The muniscins are a family of endocytic adaptors that is conserved from yeast to humans.This C-terminal domain is structurally similar to mu homology domains, and is the region of the muniscin proteins involved in the interactions with the endocytic adaptor-scaffold proteins Ede1-eps15. This interaction influences muniscin localization. The muniscins provide a combined adaptor-membrane-tubulation activity that is important for regulating endocytosis.


Pssm-ID: 463046  Cd Length: 255  Bit Score: 292.30  E-value: 9.52e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562449 582 LPVAAAFTETVNAYFKGADPSKciVKITGEMVLSFPAGITRHFannPSPAALTFRVINFSRLEHVLPNPQLLCcDNTQND 661
Cdd:pfam10291   1 PGLNASIAETVNAWFKDGDVTK--SKVTGEVALSYPAGIAASF---TPPAVLNFRLNNFSRLEKVAPNPAFVT-DESQSD 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562449 662 AntkEFWVNMPNLMTHLKKVSeqkpqatyynvdmLKYQVSAQG-IQSTPLNLAVNWRCEPSSTDLRIDYKYN-TDAMTTA 739
Cdd:pfam10291  75 G---EFKVNPQFLASRTPLGA-------------LKYQVHIDPlSASCPLILHPVWKCEPHQASLILTYSLNpSLAIASA 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562449 740 VALNNVQFLVPIDGG-VTKLQAvLPPAVWNAEQQRILWKIPDISQKSENGGvGSLLARFQLSEGPSKPSPLVVQFTSE-G 817
Cdd:pfam10291 139 VVLENLQVVVNLDGShATSAQS-KPQGTFNKEKSRITWKLPELSLTSDGDG-GKLIARFMTEGGASKPGGVAVKFEIEtG 216

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1034562449 818 STLSGCDIELV---------GAGYRFSLIKKRFAAGKYL 847
Cdd:pfam10291 217 DTLSGLGISLVdqvdeedpfGGGWKLVPTKRRLAAGKYL 255
AP_muniscins_like_MHD cd09257
Mu-homology domain (MHD) of muniscins adaptor proteins (AP) and similar proteins; This family ...
 583-849 1.27e-51

Mu-homology domain (MHD) of muniscins adaptor proteins (AP) and similar proteins; This family corresponds to the MHD found in muniscins, a novel family of endocytic adaptor proteins. The term, muniscins, has been assigned to name the MHD of proteins with both EFC/F-BAR domain and MHD. These two domains are responsible for the membrane-tubulation activity associated with transmembrane cargo proteins. Members in this family include an endocytic adaptor Syp1, the mammalian FCH domain only proteins (FCHo1/2), SH3-containing GRB2-like protein 3-interacting protein 1 (SGIP1), and related uncharacterized proteins. Syp1 is a poorly characterized yeast protein with multiple biological functions. Syp1 contains an N-terminal EFC/F-BAR domain that induces membrane tabulation, a proline-rich domain (PRD) in the middle region, and a C-terminal MHD that can directly binds to the endocytic adaptor/scaffold protein Ede1 or a transmembrane stress sensor cargo protein Mid2. Thus, Syp1 represents a novel type of endocytic adaptor protein that participates in endocytosis, promotes vesicle tabulation, and contributes to cell polarity and stress response. Syp1 shares the same domain architecture with its two ubiquitously expressed mammalian counterparts, the membrane-sculpting F-BAR domain-containing Fer/Cip4 homology domain-only proteins 1 and 2 (FCHo1/2). FCHo1/2 represent key initial proteins ultimately controlling cellular nutrient uptake, receptor regulation, and synaptic vesicle retrieval. They are required for plasma membrane clathrin-coated vesicle (CCV) budding and marked sites of CCV formation. They bind specifically to the plasma membrane and recruit the scaffold proteins eps15 and intersectin, which subsequently engage the adaptor complex AP2 and clathrin, leading to coated vesicle formation. Another mammalian neuronal-specific protein, neuronal-specific transcript Scr homology 3 (SH3)-domain growth factor receptor-bound 2 (GRB2)-like (endophilin) interacting protein 1 [SGIP1] does not contain EFC/F-BAR domain, but does have a PRD and a C-terminal MHD and has been classified into this family as well. SGIP1 is an endophilin-interacting protein that plays an obligatory role in the regulation of energy homeostasis. It is also involved in clathrin-mediated endocytosis by interacting with phospholipids and eps15.


Pssm-ID: 271165  Cd Length: 244  Bit Score: 180.64  E-value: 1.27e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562449 583 PVAAAFTETVNAYFKGadPSKCIVKITGEMVLSFPAGITRhfannPSPAALTFRVINFSRLEHVLPNPQLLCCDntQNDA 662
Cdd:cd09257     1 GVKAALTEELNAEFKG--SSLQSVGVEGEVQLAVPSSDAK-----PKPAPFNLRLNDASSLEKAAPNVAFLNSV--PSGS 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562449 663 NTKEFWVNMPNLmthlkkvseqkpQATYYNVDMLKYQVSAQGIqSTPLNLAVNWRCEPSSTDLRIDYKYNTDAMTtavAL 742
Cdd:cd09257    72 SPGEFLVNTKAI------------RASEVGSPILKYSCSSKLR-PVPLRVQTVWRCESHQTSVMLQYVSNPSLPG---PL 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562449 743 NNVQFLVPIDGGVTKLQAVLPPAVWNAEQQRILWKIPDISQkseNGGVGSLLARFQLSEGPS---KPSPLVVQFTSEGST 819
Cdd:cd09257   136 QDVTVIVNVPPGAGENLKSSPGAVWNEEKRRLTWKLPELGV---NGEGGELRARFQIDAGQTaekVPFPVLVRCLSEGST 212

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1034562449 820 LSGCDIELVGAGYR--FSLIKKRFAAGKYLAD 849
Cdd:cd09257   213 LSGLGLEVVALEEEwaFIEVKVTRRFGVYHAE 244
AP_Syp1_MHD cd09264
mu-homology domain (MHD) of adaptor protein (AP), Syp1, and related proteins; This family ...
 586-813 3.00e-17

mu-homology domain (MHD) of adaptor protein (AP), Syp1, and related proteins; This family corresponds to the MHD found in a novel endocytic adaptor Syp1 and related proteins. Syp1 is a poorly characterized yeast protein with multiple biological functions. It was originally identified as a suppressor of a yeast profiling deletion and later as a suppressor of arf3delta (Arf3 is the yeast homologue of Arf6, a mammalian regulator of endocytosis). Syp1 can bind to septins and physically link with cell polarity factors. It also directly binds to the endocytic adaptor/scaffold protein Ede1, and plays a role in endocytosis. Further studies show that Syp1 is itself an endocytic adaptor protein contributing to stress responses. Its mu-homology domain at the C-terminus binds to the cargo protein Mid2, a transmembrane stress sensor protein, and mediates Mid2 internalization. In addition, Syp1 contains an EFC/F-BAR domain which can induce membrane tabulation.


Pssm-ID: 271170  Cd Length: 257  Bit Score: 82.44  E-value: 3.00e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562449 586 AAFTETVNAYFKGADPSKciVKITGEMVLSFpagitRHFANNPSPAALTFRVINFSRLEHVLPNPQLLCCDNTQNdantk 665
Cdd:cd09264     4 ASIVETVNASFKDGQLTK--SSVIGEVALNY-----NSDPNVTPTSNINVRLNNFQVLEKVLLNPTFVEPVVSPN----- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562449 666 EFWVNMPNLMTHLKKVseqkpqatyynvdmLKYQVSAQGIQST-PLNLAVNWRCEPSSTDLRIDYKYNTD-AMTTAVALN 743
Cdd:cd09264    72 EFTVNPSLITSKTLGA--------------FKYQLHLDPSASQcPIIVTPVWKFEEHQASLIIFVKLNPSfRNSESLTLE 137

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034562449 744 NVQFLVPIDGGVTKLQAVLPPA-VWNAEQQRILWKIPDISQKSENGgvGSLLARFQlSEGPSKPSPLVVQF 813
Cdd:cd09264   138 NLVLSVALDGAVKATSAQSKPQgSFSREKSRITWRLPDPTVLDDSE--EKLIARFM-TEGLGSEAPGGVEA 205
Adap_comp_sub pfam00928
Adaptor complexes medium subunit family; This family also contains members which are coatomer ...
 692-846 3.29e-05

Adaptor complexes medium subunit family; This family also contains members which are coatomer subunits.


Pssm-ID: 395742  Cd Length: 259  Bit Score: 46.53  E-value: 3.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562449 692 NVDMLKYQVSaqgiqSTPLNLAVNWRCEP--SSTDLRIDYKYNTDA-MTTAVALNNVQFLVPIDGGVTK--LQAVLPPAV 766
Cdd:pfam00928  95 EFELMRYRLS-----TNEVKLPFTVKPIVsvSGDEGRVEIEVKLRSdFPKKLTAENVVISIPVPKEASSpvLRVSDGKAK 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034562449 767 WNAEQQRILWKIPDISQKSENGGVGSLLARFQLSEGPSKPS--PLVVQFTSEGSTLSGCDIE---LVGAGYR-FSLIKKR 840
Cdd:pfam00928 170 YDPEENALEWSIKKIPGGNESSLSGELELSVESSSDDEFPSdpPISVEFSIPMFTASGLKVRylkVEEENYKpYKWVRYV 249


                  ....*.
gi 1034562449 841 FAAGKY 846
Cdd:pfam00928 250 TQSGSY 255
 
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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