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Conserved domains on  [gi|553727157|ref|NP_001272789|]
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SH3-containing GRB2-like protein 3-interacting protein 1 isoform d [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) ...
 372-638 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: 575.08  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553727157 372 PVAAAFTETVNAYFKGADPSKCIVKITGEMVLSFPAGITRHFANNPSPAALTFRVVNSSRLEHVLPNPQLLCCDNTQNDA 451
Cdd:cd09266    1 PVAAAFTETVNAYFKGADPSKCIVKITGEMVLSFPAGITRHFANNPSPAALTFRITNYSRLEHVLPNPQLLCCDNTQAKG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553727157 452 NTKEFWVNMPNLMTHLKKVSEQKPQATYYNVDMLKYQVSAQGIQSTPLNLAVNWRCEPASTDLRIDYKYNTDAMSTAVAL 531
Cdd:cd09266   81 NAKEFWVNMPNLMTHLKKVSEQKPQATYYNVDMLKYQVSAQGPQSTPLNLAVSWRCEPSSTDLRIDYKYNGDAMTTPVAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553727157 532 NNVQFLVPIDGGVTKLQAVLPPAVWNAEQQRILWKIPDISQKSENGGVGSLLARFQLSEGPSKPSPLVVQFTSEGSTLSG 611
Cdd:cd09266  161 NNVQFLVPIDGGVTKLQAVLPPAVWNAEQQRILWKIPDISQKSENGGVGSLLARFQLSEGPSKPAPLAVQFTSEGSTLSG 240

                        250       260
                 ....*....|....*....|....*..
gi 553727157 612 CDIELVGAGYRFSLIKKRFAAGKYLAD 638
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) ...
 372-638 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: 575.08  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553727157 372 PVAAAFTETVNAYFKGADPSKCIVKITGEMVLSFPAGITRHFANNPSPAALTFRVVNSSRLEHVLPNPQLLCCDNTQNDA 451
Cdd:cd09266    1 PVAAAFTETVNAYFKGADPSKCIVKITGEMVLSFPAGITRHFANNPSPAALTFRITNYSRLEHVLPNPQLLCCDNTQAKG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553727157 452 NTKEFWVNMPNLMTHLKKVSEQKPQATYYNVDMLKYQVSAQGIQSTPLNLAVNWRCEPASTDLRIDYKYNTDAMSTAVAL 531
Cdd:cd09266   81 NAKEFWVNMPNLMTHLKKVSEQKPQATYYNVDMLKYQVSAQGPQSTPLNLAVSWRCEPSSTDLRIDYKYNGDAMTTPVAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553727157 532 NNVQFLVPIDGGVTKLQAVLPPAVWNAEQQRILWKIPDISQKSENGGVGSLLARFQLSEGPSKPSPLVVQFTSEGSTLSG 611
Cdd:cd09266  161 NNVQFLVPIDGGVTKLQAVLPPAVWNAEQQRILWKIPDISQKSENGGVGSLLARFQLSEGPSKPAPLAVQFTSEGSTLSG 240

                        250       260
                 ....*....|....*....|....*..
gi 553727157 612 CDIELVGAGYRFSLIKKRFAAGKYLAD 638
Cdd:cd09266  241 CDIELVGPGYRFSLIKKRFAAGKYLAD 267
muHD pfam10291
Muniscin C-terminal mu homology domain; The muniscins are a family of endocytic adaptors that ...
 371-636 1.91e-94

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: 291.14  E-value: 1.91e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553727157  371 LPVAAAFTETVNAYFKGADPSKciVKITGEMVLSFPAGITRHFannPSPAALTFRVVNSSRLEHVLPNPQLLCcDNTQND 450
Cdd:pfam10291   1 PGLNASIAETVNAWFKDGDVTK--SKVTGEVALSYPAGIAASF---TPPAVLNFRLNNFSRLEKVAPNPAFVT-DESQSD 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553727157  451 AntkEFWVNMPNLMTHLKKVSeqkpqatyynvdmLKYQVSAQG-IQSTPLNLAVNWRCEPASTDLRIDYKYN-TDAMSTA 528
Cdd:pfam10291  75 G---EFKVNPQFLASRTPLGA-------------LKYQVHIDPlSASCPLILHPVWKCEPHQASLILTYSLNpSLAIASA 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553727157  529 VALNNVQFLVPIDGG-VTKLQAvLPPAVWNAEQQRILWKIPDISQKSENGGvGSLLARFQLSEGPSKPSPLVVQFTSE-G 606
Cdd:pfam10291 139 VVLENLQVVVNLDGShATSAQS-KPQGTFNKEKSRITWKLPELSLTSDGDG-GKLIARFMTEGGASKPGGVAVKFEIEtG 216

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 553727157  607 STLSGCDIELV---------GAGYRFSLIKKRFAAGKYL 636
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) ...
 372-638 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: 575.08  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553727157 372 PVAAAFTETVNAYFKGADPSKCIVKITGEMVLSFPAGITRHFANNPSPAALTFRVVNSSRLEHVLPNPQLLCCDNTQNDA 451
Cdd:cd09266    1 PVAAAFTETVNAYFKGADPSKCIVKITGEMVLSFPAGITRHFANNPSPAALTFRITNYSRLEHVLPNPQLLCCDNTQAKG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553727157 452 NTKEFWVNMPNLMTHLKKVSEQKPQATYYNVDMLKYQVSAQGIQSTPLNLAVNWRCEPASTDLRIDYKYNTDAMSTAVAL 531
Cdd:cd09266   81 NAKEFWVNMPNLMTHLKKVSEQKPQATYYNVDMLKYQVSAQGPQSTPLNLAVSWRCEPSSTDLRIDYKYNGDAMTTPVAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553727157 532 NNVQFLVPIDGGVTKLQAVLPPAVWNAEQQRILWKIPDISQKSENGGVGSLLARFQLSEGPSKPSPLVVQFTSEGSTLSG 611
Cdd:cd09266  161 NNVQFLVPIDGGVTKLQAVLPPAVWNAEQQRILWKIPDISQKSENGGVGSLLARFQLSEGPSKPAPLAVQFTSEGSTLSG 240

                        250       260
                 ....*....|....*....|....*..
gi 553727157 612 CDIELVGAGYRFSLIKKRFAAGKYLAD 638
Cdd:cd09266  241 CDIELVGPGYRFSLIKKRFAAGKYLAD 267
AP_Syp1_like_MHD cd09265
Mu-homology domain (MHD) of endocytic adaptor protein (AP), Syp1; This family corresponds to ...
 372-638 1.09e-174

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: 497.01  E-value: 1.09e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553727157 372 PVAAAFTETVNAYFKGADPSKCIVKITGEMVLSFPAGITRHFANNPSPAALTFRVVNSSRLEHVLPNPQLLCCDNTQNDA 451
Cdd:cd09265    1 PVAAAFTETVHAYFKGADPSKCIVKITGDMMMSFPAGIIRLLTSNPTPAPLTFRLKNASRLEHVLPNKQLIFSDPSQSDS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553727157 452 NTKEFWVNMPNLMTHLKKVSEQKPQATYYNVDMLKYQVSAQGIQSTPLNLAVNWRCEPASTDLRIDYKYNTDAMSTAVAL 531
Cdd:cd09265   81 ETKDFWFNMPALTTYLKRQAEQNPTASYYNVDVLKYQVSPTGPQSTPLQLASYWKCEPSSTDLRVDYKYNPEAMAIATPL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553727157 532 NNVQFLVPIDGGVTKLQAVlPPAVWNAEQQRILWKIPDISQKSENGGVGSLLARFQLSEGPSKPSPLVVQFTSEGSTLSG 611
Cdd:cd09265  161 LNVQFSVPVDGGVTNVQSE-PPATWNAEQKRLLWKLPDISQNSEGGGVGSLRARFELSEGPSKPAPLAVQFNSEGTTLSG 239

                        250       260
                 ....*....|....*....|....*..
gi 553727157 612 CDIELVGAGYRFSLIKKRFAAGKYLAD 638
Cdd:cd09265  240 VDIELVGSGYRLSLIKKRFAAGKYLCD 266
FCHo2_MHD cd09267
mu-homology domain (MHD) of F-BAR domain-containing Fer/Cip4 homology domain-only protein 2 ...
 372-638 1.61e-149

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: 432.91  E-value: 1.61e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553727157 372 PVAAAFTETVNAYFKGADPSKCIVKITGEMVLSFPAGITRHFANNPSPAALTFRVVNSSRLEHVLPNPQLLCCDNTQNDA 451
Cdd:cd09267    1 PVAVALTESVNAYFKGADPTKCIVKITGDMTVSFPSGIIKVFTSNPSPAVLCFRLKNTSRLEQILPNAQLLYSDPSQSDS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553727157 452 NTKEFWVNMPNLMTHLKKVSEQKPQATYYNVDMLKYQVSAQGIQSTPLNLAVNWRCEPASTDLRIDYKYNTDAMSTAVAL 531
Cdd:cd09267   81 NTKDFWMNMQAVTVYLKKSSEQNPAASYYNVDILKYQVSSNGIQSTPLNLATYWKCSASTTDLRVDYKYNPEAMQPPSPL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553727157 532 NNVQFLVPIDGGVTKLQAvLPPAVWNAEQQRILWKIPDISQKSENGGVGSLLARFQLSEGPSKPSPLVVQFTSEGSTLSG 611
Cdd:cd09267  161 SNVQVLVPVDGGVTNMQS-LPPAIWNAEQMKALWKLSSISEKSENGGSGSLRAKFELSEGPSKPATLAVQFFSEGSTLSG 239

                        250       260
                 ....*....|....*....|....*..
gi 553727157 612 CDIELVGAGYRFSLIKKRFAAGKYLAD 638
Cdd:cd09267  240 VDMELVGTGYRLSLNKKRFATGRYMAD 266
FCHo1_MHD cd09268
mu-homology domain (MHD) of F-BAR domain-containing Fer/Cip4 homology domain-only protein 1 ...
 372-637 6.24e-111

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: 334.24  E-value: 6.24e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553727157 372 PVAAAFTETVNAYFKGADPSKCIVKITGEMVLSFPAGITRHFANNPSPAALTFRVVNSSRLEHVLPNPQLLCCDNTQNDA 451
Cdd:cd09268    1 PVAAAFTEYVHAYFRGGALEGCLLRITGELTMSFPAGILRVFASTPTPPVLSFRLVHTSHVEHFAPNSELLFSDPSQSDP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553727157 452 NTKEFWVNMPNLMTHLKKVSEQKPQATYYNVDMLKYQVSAQGIQSTPLNLAVNWRCEPASTDLRIDYKYNTdAMSTAVAL 531
Cdd:cd09268   81 NTKDFWLNMPALTSYLQRMAEQNPQASYYNVTLLKYQVSKSGPSAAPLYLSATWQCGPTSTDVSLDYRQNP-ATAPATFL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553727157 532 NNVQFLVPIDGGVTKLQAVlPPAVWNAEQQRILWKIPDISQKSENGGVGSLLARFQLSEGPSKPSPLVVQFTSEGSTLSG 611
Cdd:cd09268  160 TDVQILLPLDEPFTNLQSQ-PPAAWNAEERRLHWQLPHESAGNEHDGSGRLCASWQPLHAPSRPTSAAAQFTSEGSTLSG 238

                        250       260
                 ....*....|....*....|....*.
gi 553727157 612 CDIELVGAGYRFSLIKKRFAAGKYLA 637
Cdd:cd09268  239 VDIELVGSGYRMSLVKKRFATGKYLV 264
muHD pfam10291
Muniscin C-terminal mu homology domain; The muniscins are a family of endocytic adaptors that ...
 371-636 1.91e-94

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: 291.14  E-value: 1.91e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553727157  371 LPVAAAFTETVNAYFKGADPSKciVKITGEMVLSFPAGITRHFannPSPAALTFRVVNSSRLEHVLPNPQLLCcDNTQND 450
Cdd:pfam10291   1 PGLNASIAETVNAWFKDGDVTK--SKVTGEVALSYPAGIAASF---TPPAVLNFRLNNFSRLEKVAPNPAFVT-DESQSD 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553727157  451 AntkEFWVNMPNLMTHLKKVSeqkpqatyynvdmLKYQVSAQG-IQSTPLNLAVNWRCEPASTDLRIDYKYN-TDAMSTA 528
Cdd:pfam10291  75 G---EFKVNPQFLASRTPLGA-------------LKYQVHIDPlSASCPLILHPVWKCEPHQASLILTYSLNpSLAIASA 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553727157  529 VALNNVQFLVPIDGG-VTKLQAvLPPAVWNAEQQRILWKIPDISQKSENGGvGSLLARFQLSEGPSKPSPLVVQFTSE-G 606
Cdd:pfam10291 139 VVLENLQVVVNLDGShATSAQS-KPQGTFNKEKSRITWKLPELSLTSDGDG-GKLIARFMTEGGASKPGGVAVKFEIEtG 216

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 553727157  607 STLSGCDIELV---------GAGYRFSLIKKRFAAGKYL 636
Cdd:pfam10291 217 DTLSGLGISLVdqvdeedpfGGGWKLVPTKRRLAAGKYL 255
AP_muniscins_like_MHD cd09257
Mu-homology domain (MHD) of muniscins adaptor proteins (AP) and similar proteins; This family ...
 372-638 3.51e-52

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: 179.87  E-value: 3.51e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553727157 372 PVAAAFTETVNAYFKGadPSKCIVKITGEMVLSFPAGITRhfannPSPAALTFRVVNSSRLEHVLPNPQLLCCDntQNDA 451
Cdd:cd09257    1 GVKAALTEELNAEFKG--SSLQSVGVEGEVQLAVPSSDAK-----PKPAPFNLRLNDASSLEKAAPNVAFLNSV--PSGS 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553727157 452 NTKEFWVNMPNLmthlkkvseqkpQATYYNVDMLKYQVSAQGIqSTPLNLAVNWRCEPASTDLRIDYKYNTDAmstAVAL 531
Cdd:cd09257   72 SPGEFLVNTKAI------------RASEVGSPILKYSCSSKLR-PVPLRVQTVWRCESHQTSVMLQYVSNPSL---PGPL 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553727157 532 NNVQFLVPIDGGVTKLQAVLPPAVWNAEQQRILWKIPDISQkseNGGVGSLLARFQLSEGPS---KPSPLVVQFTSEGST 608
Cdd:cd09257  136 QDVTVIVNVPPGAGENLKSSPGAVWNEEKRRLTWKLPELGV---NGEGGELRARFQIDAGQTaekVPFPVLVRCLSEGST 212

                        250       260       270
                 ....*....|....*....|....*....|..
gi 553727157 609 LSGCDIELVGAGYR--FSLIKKRFAAGKYLAD 638
Cdd:cd09257  213 LSGLGLEVVALEEEwaFIEVKVTRRFGVYHAE 244
AP_Syp1_MHD cd09264
mu-homology domain (MHD) of adaptor protein (AP), Syp1, and related proteins; This family ...
 375-615 4.90e-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: 81.28  E-value: 4.90e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553727157 375 AAFTETVNAYFKGADPSKciVKITGEMVLSFpagitRHFANNPSPAALTFRVVNSSRLEHVLPNPQLLCCDNTQNdantk 454
Cdd:cd09264    4 ASIVETVNASFKDGQLTK--SSVIGEVALNY-----NSDPNVTPTSNINVRLNNFQVLEKVLLNPTFVEPVVSPN----- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553727157 455 EFWVNMPNLMTHLKKVseqkpqatyynvdmLKYQVSAQGIQST-PLNLAVNWRCEPASTDLRIDYKYNTD-AMSTAVALN 532
Cdd:cd09264   72 EFTVNPSLITSKTLGA--------------FKYQLHLDPSASQcPIIVTPVWKFEEHQASLIIFVKLNPSfRNSESLTLE 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553727157 533 NVQFLVPIDGGVTKLQAVLPPA-VWNAEQQRILWKIPDISQKSENGgvGSLLARFQLS-EGPSKPSPLVVQFT-SEGSTL 609
Cdd:cd09264  138 NLVLSVALDGAVKATSAQSKPQgSFSREKSRITWRLPDPTVLDDSE--EKLIARFMTEgLGSEAPGGVEARFEiTDPDAG 215


                 ....*.
gi 553727157 610 SGCDIE 615
Cdd:cd09264  216 SGLTIS 221
Adap_comp_sub pfam00928
Adaptor complexes medium subunit family; This family also contains members which are coatomer ...
 481-635 7.26e-06

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


Pssm-ID: 395742  Cd Length: 259  Bit Score: 48.07  E-value: 7.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553727157  481 NVDMLKYQVSaqgiqSTPLNLAVNWRCEP--ASTDLRIDYKYNTDA-MSTAVALNNVQFLVPIDGGVTK--LQAVLPPAV 555
Cdd:pfam00928  95 EFELMRYRLS-----TNEVKLPFTVKPIVsvSGDEGRVEIEVKLRSdFPKKLTAENVVISIPVPKEASSpvLRVSDGKAK 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553727157  556 WNAEQQRILWKIPDISQKSENGGVGSLLARFQLSEGPSKPS--PLVVQFTSEGSTLSGCDIE---LVGAGYR-FSLIKKR 629
Cdd:pfam00928 170 YDPEENALEWSIKKIPGGNESSLSGELELSVESSSDDEFPSdpPISVEFSIPMFTASGLKVRylkVEEENYKpYKWVRYV 249


                  ....*.
gi 553727157  630 FAAGKY 635
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 ...
 552-587 4.94e-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: 35.64  E-value: 4.94e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 553727157  552 PPAVWNAEQQRILWKIpdISQKSENGGV--GSLLARFQ 587
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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