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Conserved domains on  [gi|21536264|ref|NP_659155|]
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SH3-containing GRB2-like protein 3-interacting protein 1 isoform b [Mus musculus]

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) ...
 539-805 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: 575.85  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536264 539 PVAAAFTETVNAYFKGADPSKCIVKITGEMVLSFPAGITRHFANNPSPAALTFRVVNSSRLEHVLPNPQLLCCDNTQNDA 618
Cdd:cd09266   1 PVAAAFTETVNAYFKGADPSKCIVKITGEMVLSFPAGITRHFANNPSPAALTFRITNYSRLEHVLPNPQLLCCDNTQAKG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536264 619 NTKEFWVNMPNLMTHLKKVSEQKPQATYYNVDMLKYQVSAQGIQSTPLNLAVNWRCEPASTDLRIDYKYNTDAMSTAVAL 698
Cdd:cd09266  81 NAKEFWVNMPNLMTHLKKVSEQKPQATYYNVDMLKYQVSAQGPQSTPLNLAVSWRCEPSSTDLRIDYKYNGDAMTTPVAL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536264 699 NNVQFLVPIDGGVTKLQAVLPPAVWNAEQQRILWKIPDISQKSENGGVGSLLARFQLSEGPSKPSPLVVQFTSEGSTLSG 778
Cdd:cd09266 161 NNVQFLVPIDGGVTKLQAVLPPAVWNAEQQRILWKIPDISQKSENGGVGSLLARFQLSEGPSKPAPLAVQFTSEGSTLSG 240

                       250       260
                ....*....|....*....|....*..
gi 21536264 779 CDIELVGAGYRFSLIKKRFAAGKYLAD 805
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) ...
 539-805 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: 575.85  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536264 539 PVAAAFTETVNAYFKGADPSKCIVKITGEMVLSFPAGITRHFANNPSPAALTFRVVNSSRLEHVLPNPQLLCCDNTQNDA 618
Cdd:cd09266   1 PVAAAFTETVNAYFKGADPSKCIVKITGEMVLSFPAGITRHFANNPSPAALTFRITNYSRLEHVLPNPQLLCCDNTQAKG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536264 619 NTKEFWVNMPNLMTHLKKVSEQKPQATYYNVDMLKYQVSAQGIQSTPLNLAVNWRCEPASTDLRIDYKYNTDAMSTAVAL 698
Cdd:cd09266  81 NAKEFWVNMPNLMTHLKKVSEQKPQATYYNVDMLKYQVSAQGPQSTPLNLAVSWRCEPSSTDLRIDYKYNGDAMTTPVAL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536264 699 NNVQFLVPIDGGVTKLQAVLPPAVWNAEQQRILWKIPDISQKSENGGVGSLLARFQLSEGPSKPSPLVVQFTSEGSTLSG 778
Cdd:cd09266 161 NNVQFLVPIDGGVTKLQAVLPPAVWNAEQQRILWKIPDISQKSENGGVGSLLARFQLSEGPSKPAPLAVQFTSEGSTLSG 240

                       250       260
                ....*....|....*....|....*..
gi 21536264 779 CDIELVGAGYRFSLIKKRFAAGKYLAD 805
Cdd:cd09266 241 CDIELVGPGYRFSLIKKRFAAGKYLAD 267
muHD pfam10291
Muniscin C-terminal mu homology domain; The muniscins are a family of endocytic adaptors that ...
 538-803 2.55e-92

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: 289.99  E-value: 2.55e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536264   538 LPVAAAFTETVNAYFKGADPSKciVKITGEMVLSFPAGITRHFannPSPAALTFRVVNSSRLEHVLPNPQLLCcDNTQND 617
Cdd:pfam10291   1 PGLNASIAETVNAWFKDGDVTK--SKVTGEVALSYPAGIAASF---TPPAVLNFRLNNFSRLEKVAPNPAFVT-DESQSD 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536264   618 AntkEFWVNMPNLMTHLKKVSeqkpqatyynvdmLKYQVSAQG-IQSTPLNLAVNWRCEPASTDLRIDYKYN-TDAMSTA 695
Cdd:pfam10291  75 G---EFKVNPQFLASRTPLGA-------------LKYQVHIDPlSASCPLILHPVWKCEPHQASLILTYSLNpSLAIASA 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536264   696 VALNNVQFLVPIDGG-VTKLQAvLPPAVWNAEQQRILWKIPDISQKSENGGvGSLLARFQLSEGPSKPSPLVVQFTSE-G 773
Cdd:pfam10291 139 VVLENLQVVVNLDGShATSAQS-KPQGTFNKEKSRITWKLPELSLTSDGDG-GKLIARFMTEGGASKPGGVAVKFEIEtG 216

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 21536264   774 STLSGCDIELV---------GAGYRFSLIKKRFAAGKYL 803
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) ...
 539-805 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: 575.85  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536264 539 PVAAAFTETVNAYFKGADPSKCIVKITGEMVLSFPAGITRHFANNPSPAALTFRVVNSSRLEHVLPNPQLLCCDNTQNDA 618
Cdd:cd09266   1 PVAAAFTETVNAYFKGADPSKCIVKITGEMVLSFPAGITRHFANNPSPAALTFRITNYSRLEHVLPNPQLLCCDNTQAKG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536264 619 NTKEFWVNMPNLMTHLKKVSEQKPQATYYNVDMLKYQVSAQGIQSTPLNLAVNWRCEPASTDLRIDYKYNTDAMSTAVAL 698
Cdd:cd09266  81 NAKEFWVNMPNLMTHLKKVSEQKPQATYYNVDMLKYQVSAQGPQSTPLNLAVSWRCEPSSTDLRIDYKYNGDAMTTPVAL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536264 699 NNVQFLVPIDGGVTKLQAVLPPAVWNAEQQRILWKIPDISQKSENGGVGSLLARFQLSEGPSKPSPLVVQFTSEGSTLSG 778
Cdd:cd09266 161 NNVQFLVPIDGGVTKLQAVLPPAVWNAEQQRILWKIPDISQKSENGGVGSLLARFQLSEGPSKPAPLAVQFTSEGSTLSG 240

                       250       260
                ....*....|....*....|....*..
gi 21536264 779 CDIELVGAGYRFSLIKKRFAAGKYLAD 805
Cdd:cd09266 241 CDIELVGPGYRFSLIKKRFAAGKYLAD 267
AP_Syp1_like_MHD cd09265
Mu-homology domain (MHD) of endocytic adaptor protein (AP), Syp1; This family corresponds to ...
 539-805 1.77e-172

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: 497.40  E-value: 1.77e-172
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536264 539 PVAAAFTETVNAYFKGADPSKCIVKITGEMVLSFPAGITRHFANNPSPAALTFRVVNSSRLEHVLPNPQLLCCDNTQNDA 618
Cdd:cd09265   1 PVAAAFTETVHAYFKGADPSKCIVKITGDMMMSFPAGIIRLLTSNPTPAPLTFRLKNASRLEHVLPNKQLIFSDPSQSDS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536264 619 NTKEFWVNMPNLMTHLKKVSEQKPQATYYNVDMLKYQVSAQGIQSTPLNLAVNWRCEPASTDLRIDYKYNTDAMSTAVAL 698
Cdd:cd09265  81 ETKDFWFNMPALTTYLKRQAEQNPTASYYNVDVLKYQVSPTGPQSTPLQLASYWKCEPSSTDLRVDYKYNPEAMAIATPL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536264 699 NNVQFLVPIDGGVTKLQAVlPPAVWNAEQQRILWKIPDISQKSENGGVGSLLARFQLSEGPSKPSPLVVQFTSEGSTLSG 778
Cdd:cd09265 161 LNVQFSVPVDGGVTNVQSE-PPATWNAEQKRLLWKLPDISQNSEGGGVGSLRARFELSEGPSKPAPLAVQFNSEGTTLSG 239

                       250       260
                ....*....|....*....|....*..
gi 21536264 779 CDIELVGAGYRFSLIKKRFAAGKYLAD 805
Cdd:cd09265 240 VDIELVGSGYRLSLIKKRFAAGKYLCD 266
FCHo2_MHD cd09267
mu-homology domain (MHD) of F-BAR domain-containing Fer/Cip4 homology domain-only protein 2 ...
 539-805 1.12e-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: 1.12e-147
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536264 539 PVAAAFTETVNAYFKGADPSKCIVKITGEMVLSFPAGITRHFANNPSPAALTFRVVNSSRLEHVLPNPQLLCCDNTQNDA 618
Cdd:cd09267   1 PVAVALTESVNAYFKGADPTKCIVKITGDMTVSFPSGIIKVFTSNPSPAVLCFRLKNTSRLEQILPNAQLLYSDPSQSDS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536264 619 NTKEFWVNMPNLMTHLKKVSEQKPQATYYNVDMLKYQVSAQGIQSTPLNLAVNWRCEPASTDLRIDYKYNTDAMSTAVAL 698
Cdd:cd09267  81 NTKDFWMNMQAVTVYLKKSSEQNPAASYYNVDILKYQVSSNGIQSTPLNLATYWKCSASTTDLRVDYKYNPEAMQPPSPL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536264 699 NNVQFLVPIDGGVTKLQAvLPPAVWNAEQQRILWKIPDISQKSENGGVGSLLARFQLSEGPSKPSPLVVQFTSEGSTLSG 778
Cdd:cd09267 161 SNVQVLVPVDGGVTNMQS-LPPAIWNAEQMKALWKLSSISEKSENGGSGSLRAKFELSEGPSKPATLAVQFFSEGSTLSG 239

                       250       260
                ....*....|....*....|....*..
gi 21536264 779 CDIELVGAGYRFSLIKKRFAAGKYLAD 805
Cdd:cd09267 240 VDMELVGTGYRLSLNKKRFATGRYMAD 266
FCHo1_MHD cd09268
mu-homology domain (MHD) of F-BAR domain-containing Fer/Cip4 homology domain-only protein 1 ...
 539-804 3.21e-109

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: 334.63  E-value: 3.21e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536264 539 PVAAAFTETVNAYFKGADPSKCIVKITGEMVLSFPAGITRHFANNPSPAALTFRVVNSSRLEHVLPNPQLLCCDNTQNDA 618
Cdd:cd09268   1 PVAAAFTEYVHAYFRGGALEGCLLRITGELTMSFPAGILRVFASTPTPPVLSFRLVHTSHVEHFAPNSELLFSDPSQSDP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536264 619 NTKEFWVNMPNLMTHLKKVSEQKPQATYYNVDMLKYQVSAQGIQSTPLNLAVNWRCEPASTDLRIDYKYNTdAMSTAVAL 698
Cdd:cd09268  81 NTKDFWLNMPALTSYLQRMAEQNPQASYYNVTLLKYQVSKSGPSAAPLYLSATWQCGPTSTDVSLDYRQNP-ATAPATFL 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536264 699 NNVQFLVPIDGGVTKLQAVlPPAVWNAEQQRILWKIPDISQKSENGGVGSLLARFQLSEGPSKPSPLVVQFTSEGSTLSG 778
Cdd:cd09268 160 TDVQILLPLDEPFTNLQSQ-PPAAWNAEERRLHWQLPHESAGNEHDGSGRLCASWQPLHAPSRPTSAAAQFTSEGSTLSG 238

                       250       260
                ....*....|....*....|....*.
gi 21536264 779 CDIELVGAGYRFSLIKKRFAAGKYLA 804
Cdd:cd09268 239 VDIELVGSGYRMSLVKKRFATGKYLV 264
muHD pfam10291
Muniscin C-terminal mu homology domain; The muniscins are a family of endocytic adaptors that ...
 538-803 2.55e-92

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: 289.99  E-value: 2.55e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536264   538 LPVAAAFTETVNAYFKGADPSKciVKITGEMVLSFPAGITRHFannPSPAALTFRVVNSSRLEHVLPNPQLLCcDNTQND 617
Cdd:pfam10291   1 PGLNASIAETVNAWFKDGDVTK--SKVTGEVALSYPAGIAASF---TPPAVLNFRLNNFSRLEKVAPNPAFVT-DESQSD 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536264   618 AntkEFWVNMPNLMTHLKKVSeqkpqatyynvdmLKYQVSAQG-IQSTPLNLAVNWRCEPASTDLRIDYKYN-TDAMSTA 695
Cdd:pfam10291  75 G---EFKVNPQFLASRTPLGA-------------LKYQVHIDPlSASCPLILHPVWKCEPHQASLILTYSLNpSLAIASA 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536264   696 VALNNVQFLVPIDGG-VTKLQAvLPPAVWNAEQQRILWKIPDISQKSENGGvGSLLARFQLSEGPSKPSPLVVQFTSE-G 773
Cdd:pfam10291 139 VVLENLQVVVNLDGShATSAQS-KPQGTFNKEKSRITWKLPELSLTSDGDG-GKLIARFMTEGGASKPGGVAVKFEIEtG 216

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 21536264   774 STLSGCDIELV---------GAGYRFSLIKKRFAAGKYL 803
Cdd:pfam10291 217 DTLSGLGISLVdqvdeedpfGGGWKLVPTKRRLAAGKYL 255
AP_muniscins_like_MHD cd09257
Mu-homology domain (MHD) of muniscins adaptor proteins (AP) and similar proteins; This family ...
 539-805 5.73e-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: 178.72  E-value: 5.73e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536264 539 PVAAAFTETVNAYFKGadPSKCIVKITGEMVLSFPAGITRhfannPSPAALTFRVVNSSRLEHVLPNPQLLCCDntQNDA 618
Cdd:cd09257   1 GVKAALTEELNAEFKG--SSLQSVGVEGEVQLAVPSSDAK-----PKPAPFNLRLNDASSLEKAAPNVAFLNSV--PSGS 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536264 619 NTKEFWVNMPNLmthlkkvseqkpQATYYNVDMLKYQVSAQGIqSTPLNLAVNWRCEPASTDLRIDYKYNTDAmstAVAL 698
Cdd:cd09257  72 SPGEFLVNTKAI------------RASEVGSPILKYSCSSKLR-PVPLRVQTVWRCESHQTSVMLQYVSNPSL---PGPL 135

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536264 699 NNVQFLVPIDGGVTKLQAVLPPAVWNAEQQRILWKIPDISQkseNGGVGSLLARFQLSEGPS---KPSPLVVQFTSEGST 775
Cdd:cd09257 136 QDVTVIVNVPPGAGENLKSSPGAVWNEEKRRLTWKLPELGV---NGEGGELRARFQIDAGQTaekVPFPVLVRCLSEGST 212

                       250       260       270
                ....*....|....*....|....*....|..
gi 21536264 776 LSGCDIELVGAGYR--FSLIKKRFAAGKYLAD 805
Cdd:cd09257 213 LSGLGLEVVALEEEwaFIEVKVTRRFGVYHAE 244
AP_Syp1_MHD cd09264
mu-homology domain (MHD) of adaptor protein (AP), Syp1, and related proteins; This family ...
 542-769 1.17e-16

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: 80.51  E-value: 1.17e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536264 542 AAFTETVNAYFKGADPSKciVKITGEMVLSFpagitRHFANNPSPAALTFRVVNSSRLEHVLPNPQLLCCDNTQNdantk 621
Cdd:cd09264   4 ASIVETVNASFKDGQLTK--SSVIGEVALNY-----NSDPNVTPTSNINVRLNNFQVLEKVLLNPTFVEPVVSPN----- 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536264 622 EFWVNMPNLMTHLKKVseqkpqatyynvdmLKYQVSAQGIQST-PLNLAVNWRCEPASTDLRIDYKYNTD-AMSTAVALN 699
Cdd:cd09264  72 EFTVNPSLITSKTLGA--------------FKYQLHLDPSASQcPIIVTPVWKFEEHQASLIIFVKLNPSfRNSESLTLE 137

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21536264 700 NVQFLVPIDGGVTKLQAVLPPA-VWNAEQQRILWKIPDISQKSENGgvGSLLARFQlSEGPSKPSPLVVQF 769
Cdd:cd09264 138 NLVLSVALDGAVKATSAQSKPQgSFSREKSRITWRLPDPTVLDDSE--EKLIARFM-TEGLGSEAPGGVEA 205
Adap_comp_sub pfam00928
Adaptor complexes medium subunit family; This family also contains members which are coatomer ...
 648-802 1.08e-05

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


Pssm-ID: 395742  Cd Length: 259  Bit Score: 47.68  E-value: 1.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536264   648 NVDMLKYQVSaqgiqSTPLNLAVNWRCEP--ASTDLRIDYKYNTDA-MSTAVALNNVQFLVPIDGGVTK--LQAVLPPAV 722
Cdd:pfam00928  95 EFELMRYRLS-----TNEVKLPFTVKPIVsvSGDEGRVEIEVKLRSdFPKKLTAENVVISIPVPKEASSpvLRVSDGKAK 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536264   723 WNAEQQRILWKIPDISQKSENGGVGSLLARFQLSEGPSKPS--PLVVQFTSEGSTLSGCDIE---LVGAGYR-FSLIKKR 796
Cdd:pfam00928 170 YDPEENALEWSIKKIPGGNESSLSGELELSVESSSDDEFPSdpPISVEFSIPMFTASGLKVRylkVEEENYKpYKWVRYV 249


                  ....*.
gi 21536264   797 FAAGKY 802
Cdd:pfam00928 250 TQSGSY 255
ATG29_N pfam18388
Atg29 N-terminal domain; This is the N-terminal domain found in fungal Atg proteins such as ...
 719-754 7.40e-03

Atg29 N-terminal domain; This is the N-terminal domain found in fungal Atg proteins such as Atg29. In yeast, the induction of autophagy begins at a single perivacuolar site that is proximal to the vacuole, called the phagophore assembly site (PAS). Atg17-Atg29-Atg31 complex (Atg1 complex) formation is a prerequisite for PAS assembly. Functional analysis indicate that the N-terminal half Atg29 can bind Atg31.


Pssm-ID: 436458  Cd Length: 54  Bit Score: 35.26  E-value: 7.40e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 21536264   719 PPAVWNAEQQRILWKIpdISQKSENGGV--GSLLARFQ 754
Cdd:pfam18388  18 PPVEWDAAKDRALWKI--LSRASKKSDIdwNELAERFD 53
 
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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