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Conserved domains on  [gi|349577968|dbj|GAA23135|]
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K7_Ret2p [Saccharomyces cerevisiae Kyokai no. 7]

Protein Classification

coatomer subunit delta( domain architecture ID 13000608)

coatomer subunit delta is a component of the coatomer, a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network

Gene Ontology:  GO:0006888|GO:0006886|GO:0003723|GO:0030126
PubMed:  1898986

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AP_delta-COPI_MHD cd09254
Mu homology domain (MHD) of adaptor protein (AP) coat protein I (COPI) delta subunit; COPI ...
 289-543 1.78e-81

Mu homology domain (MHD) of adaptor protein (AP) coat protein I (COPI) delta subunit; COPI complex-coated vesicles function in the early secretory pathway. They mediate the retrograde transport from the Golgi to the ER, and intra-Golgi transport. COPI complex-coated vesicles consist of a small GTPase, ADP-ribosylation factor 1 (ARF1) and a heteroheptameric coatomer composed of two subcomplexes, F-COPI and B-COPI. ARF1 regulates COPI vesicle formation by recruiting the coatomer onto Golgi membranes to initiate its coat function. Coatomer complexes then bind cargo molecules and self-assemble to form spherical cages that yield COPI-coated vesicles. The heterotetrameric F-COPI subcomplex contains beta-, gamma-, delta-, and zeta-COP subunits, where beta- and gamma-COP subunits are related to the large AP subunits, and delta- and zeta-COP subunits are related to the medium and small AP subunits, respectively. Due to the sequence similarity to the AP complexes, the F-COPI subcomplex might play a role in the cargo-binding. The heterotrimeric B-COPI contains alpha-, beta-, and epsilon-COP subunits, which are not related to the adaptins. This subcomplex is thought to participate in the cage-forming and might serve a function similar to that of clathrin. This family corresponds to the mu homology domain of delta-subunit of COPI complex (delta-COP), which is distantly related to the C-terminal domain of mu chains among AP complexes. The delta-COP subunit appears tightly associated with the beta-COP subunit to confer its interaction with ARF1. In addition, both delta- and beta-COP subunits contribute to a common binding site for arginine (R)-based signals, which are sorting motifs conferring transient endoplasmic reticulum (ER) localization to unassembled subunits of multimeric membrane proteins.


:

Pssm-ID: 271162  Cd Length: 237  Bit Score: 254.46  E-value: 1.78e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349577968 289 NGILISIKEVINAEFSRDGTIHSSELKGVLELRINDHDLSHSNLKLADSIDvrdKSFQFKTHPNIDKQSFLSTKLISLRD 368
Cdd:cd09254    1 EGVHITVEEKISATLSRDGGLESLEVKGTLSLRINDEELAHIKLQLANNSD---KGFQFKTHPNVDKKLFTSDSVLGLKD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349577968 369 KSKAFPANDQSlGVLRWRKVAPaeDDSLIPLTLTTWvsPSESQQGFDVIIEYESVLET-ELADVIFTIPVFPQEPVDINt 447
Cdd:cd09254   78 PSKPFPVNDPV-GVLKWRLQGS--DESLLPLTINCW--PSESGGGCDVTIEYELNRDDlELNDVVISIPLPSGDAPVVN- 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349577968 448 esSTCSDAEVVNMDQemGTSIKISKI-AANDAGALAFTIEAPYEDALYPMTVSFeestrdKLAKSFTGMAIQSVVMANDh 526
Cdd:cd09254  152 --SIDGNYEYDSRKN--VLEWKIPVIdASNSSGSLEFSIPADDEDAFFPISVSF------TSSKTFCGVKVVEVVSADD- 220

                        250
                 ....*....|....*..
gi 349577968 527 DQELPYDVITSLKSDEY 543
Cdd:cd09254  221 GEPVPFSLETSLVADKY 237
Delta_COP_N cd14830
delta subunit of the F-COPI complex, N-terminal domain; Delta subunit of the heterotetrameric ...
 4-135 1.48e-59

delta subunit of the F-COPI complex, N-terminal domain; Delta subunit of the heterotetrameric F-COPI complex, which consists of one beta-, one gamma-, one delta-, and one zeta subunit, where beta- and gamma- subunits are related to the large adaptor protein (AP) complex subunits, and delta- and zeta- subunits are related to the medium and small AP subunits, respectively. F-COPI forms a coatomer together with the B-COPI subcomplex, which assembles with a small GTPase, ADP-ribosylation factor 1 (ARF1), playing an important role in the formation of COPI complex-coated vesicles. COPI complex-coated vesicles function in the early secretory pathway mediating the retrograde transport from the Golgi to the ER, and intra-Golgi transport.


:

Pssm-ID: 341434  Cd Length: 130  Bit Score: 193.51  E-value: 1.48e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349577968   4 LAASITTRQGKPLLSRQFKDLSKDRVLELLSNFQNLVSEiSSDHTFVEDKHVRYVYRPFDNYYIILITNRQSNIIKDLAT 83
Cdd:cd14830    1 LSAAICTKGGKILVSRQFVEISRSRIEGLLAAFPKLVGS-GSQHTYVETENVRYVYQPLEDLYLVLITTKNSNILEDLET 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 349577968  84 LNLFSQTINSYLSSFQDQEIFHNAFEILSSFDEIVSMgGYKENLSFTQVQTY 135
Cdd:cd14830   80 LRLLSRVVPEYCPSVDEEEILKNAFDLIFAFDEVISL-GYRENVTLSQIKTF 130
 
Name Accession Description Interval E-value
AP_delta-COPI_MHD cd09254
Mu homology domain (MHD) of adaptor protein (AP) coat protein I (COPI) delta subunit; COPI ...
 289-543 1.78e-81

Mu homology domain (MHD) of adaptor protein (AP) coat protein I (COPI) delta subunit; COPI complex-coated vesicles function in the early secretory pathway. They mediate the retrograde transport from the Golgi to the ER, and intra-Golgi transport. COPI complex-coated vesicles consist of a small GTPase, ADP-ribosylation factor 1 (ARF1) and a heteroheptameric coatomer composed of two subcomplexes, F-COPI and B-COPI. ARF1 regulates COPI vesicle formation by recruiting the coatomer onto Golgi membranes to initiate its coat function. Coatomer complexes then bind cargo molecules and self-assemble to form spherical cages that yield COPI-coated vesicles. The heterotetrameric F-COPI subcomplex contains beta-, gamma-, delta-, and zeta-COP subunits, where beta- and gamma-COP subunits are related to the large AP subunits, and delta- and zeta-COP subunits are related to the medium and small AP subunits, respectively. Due to the sequence similarity to the AP complexes, the F-COPI subcomplex might play a role in the cargo-binding. The heterotrimeric B-COPI contains alpha-, beta-, and epsilon-COP subunits, which are not related to the adaptins. This subcomplex is thought to participate in the cage-forming and might serve a function similar to that of clathrin. This family corresponds to the mu homology domain of delta-subunit of COPI complex (delta-COP), which is distantly related to the C-terminal domain of mu chains among AP complexes. The delta-COP subunit appears tightly associated with the beta-COP subunit to confer its interaction with ARF1. In addition, both delta- and beta-COP subunits contribute to a common binding site for arginine (R)-based signals, which are sorting motifs conferring transient endoplasmic reticulum (ER) localization to unassembled subunits of multimeric membrane proteins.


Pssm-ID: 271162  Cd Length: 237  Bit Score: 254.46  E-value: 1.78e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349577968 289 NGILISIKEVINAEFSRDGTIHSSELKGVLELRINDHDLSHSNLKLADSIDvrdKSFQFKTHPNIDKQSFLSTKLISLRD 368
Cdd:cd09254    1 EGVHITVEEKISATLSRDGGLESLEVKGTLSLRINDEELAHIKLQLANNSD---KGFQFKTHPNVDKKLFTSDSVLGLKD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349577968 369 KSKAFPANDQSlGVLRWRKVAPaeDDSLIPLTLTTWvsPSESQQGFDVIIEYESVLET-ELADVIFTIPVFPQEPVDINt 447
Cdd:cd09254   78 PSKPFPVNDPV-GVLKWRLQGS--DESLLPLTINCW--PSESGGGCDVTIEYELNRDDlELNDVVISIPLPSGDAPVVN- 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349577968 448 esSTCSDAEVVNMDQemGTSIKISKI-AANDAGALAFTIEAPYEDALYPMTVSFeestrdKLAKSFTGMAIQSVVMANDh 526
Cdd:cd09254  152 --SIDGNYEYDSRKN--VLEWKIPVIdASNSSGSLEFSIPADDEDAFFPISVSF------TSSKTFCGVKVVEVVSADD- 220

                        250
                 ....*....|....*..
gi 349577968 527 DQELPYDVITSLKSDEY 543
Cdd:cd09254  221 GEPVPFSLETSLVADKY 237
Delta_COP_N cd14830
delta subunit of the F-COPI complex, N-terminal domain; Delta subunit of the heterotetrameric ...
 4-135 1.48e-59

delta subunit of the F-COPI complex, N-terminal domain; Delta subunit of the heterotetrameric F-COPI complex, which consists of one beta-, one gamma-, one delta-, and one zeta subunit, where beta- and gamma- subunits are related to the large adaptor protein (AP) complex subunits, and delta- and zeta- subunits are related to the medium and small AP subunits, respectively. F-COPI forms a coatomer together with the B-COPI subcomplex, which assembles with a small GTPase, ADP-ribosylation factor 1 (ARF1), playing an important role in the formation of COPI complex-coated vesicles. COPI complex-coated vesicles function in the early secretory pathway mediating the retrograde transport from the Golgi to the ER, and intra-Golgi transport.


Pssm-ID: 341434  Cd Length: 130  Bit Score: 193.51  E-value: 1.48e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349577968   4 LAASITTRQGKPLLSRQFKDLSKDRVLELLSNFQNLVSEiSSDHTFVEDKHVRYVYRPFDNYYIILITNRQSNIIKDLAT 83
Cdd:cd14830    1 LSAAICTKGGKILVSRQFVEISRSRIEGLLAAFPKLVGS-GSQHTYVETENVRYVYQPLEDLYLVLITTKNSNILEDLET 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 349577968  84 LNLFSQTINSYLSSFQDQEIFHNAFEILSSFDEIVSMgGYKENLSFTQVQTY 135
Cdd:cd14830   80 LRLLSRVVPEYCPSVDEEEILKNAFDLIFAFDEVISL-GYRENVTLSQIKTF 130
Adap_comp_sub pfam00928
Adaptor complexes medium subunit family; This family also contains members which are coatomer ...
 288-437 4.40e-05

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


Pssm-ID: 395742  Cd Length: 259  Bit Score: 45.37  E-value: 4.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349577968  288 NNGILISIKEVINAEFSRDGTIHSSELKGVLELRINDHDLSHSNLKLAD-SIDVRDKSFQFKTHPNIDKqsFLSTKLISl 366
Cdd:pfam00928  12 KNEVFLDVIERVSVIVDKDGGLLNSEVQGTIDLKCFLSGMPELRLGLNDkLLLIELDDVSFHQCVNLDK--FESERVIS- 88

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 349577968  367 rdkskaFPANDQSLGVLRWRKVApaeDDSLIPLTLTTWVspSESQQGFDVIIEYE------SVLETElaDVIFTIPV 437
Cdd:pfam00928  89 ------FIPPDGEFELMRYRLST---NEVKLPFTVKPIV--SVSGDEGRVEIEVKlrsdfpKKLTAE--NVVISIPV 152
APS2 COG5030
Clathrin adaptor complex, small subunit [Intracellular trafficking and secretion];
8-143 1.71e-04

Clathrin adaptor complex, small subunit [Intracellular trafficking and secretion];


Pssm-ID: 227363  Cd Length: 152  Bit Score: 42.01  E-value: 1.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349577968   8 ITTRQGKPLLSRQFKDLSKDRVLELLSNFQNLVSEISSDHT-FVEDKHVRYVYRPFDNYYIILITNRQSNIIKDLATLNL 86
Cdd:COG5030    7 IFNRQGKPRLVKWYTPVSDPEQAKLIADIYELISARKPKESnFIEGKNEKIVYRRYATLYFVFGVDNDDNELIILELIHN 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 349577968  87 FSQTINSYLSSFQDQEIFHNAFEILSSFDEIVSMGGYKENLSFTQVQTYLSMESHEE 143
Cdd:COG5030   87 FVEILDRFFGNVCELDLIFNFQKVYAILDEMILGGEIIESSKNEVLEHVYALDAEST 143
Clat_adaptor_s pfam01217
Clathrin adaptor complex small chain;
8-138 3.72e-04

Clathrin adaptor complex small chain;


Pssm-ID: 460115  Cd Length: 142  Bit Score: 40.80  E-value: 3.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349577968    8 ITTRQGKPLLSRQFKDLSKDRVLELLSNFQNLVSEISSDHT-FVEDKHVRYVYRPFDNYYIILITNRQSNIIKDLATLNL 86
Cdd:pfam01217   7 IFNRQGKPRLAKWYTPYSDPEQQKLIEQIYALISARKPKMSnFIEFNDLKVIYKRYATLYFVVIVDDQDNELIILELIHR 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 349577968   87 FSQTINSYLSSFQDQEIFHNAFEILSSFDEIVsMGGYKENLSFTQVQTYLSM 138
Cdd:pfam01217  87 FVESLDRYFGNVCELDLIFNFEKVYLILDEMV-MGGEILETSKNEVLHRVAL 137
 
Name Accession Description Interval E-value
AP_delta-COPI_MHD cd09254
Mu homology domain (MHD) of adaptor protein (AP) coat protein I (COPI) delta subunit; COPI ...
 289-543 1.78e-81

Mu homology domain (MHD) of adaptor protein (AP) coat protein I (COPI) delta subunit; COPI complex-coated vesicles function in the early secretory pathway. They mediate the retrograde transport from the Golgi to the ER, and intra-Golgi transport. COPI complex-coated vesicles consist of a small GTPase, ADP-ribosylation factor 1 (ARF1) and a heteroheptameric coatomer composed of two subcomplexes, F-COPI and B-COPI. ARF1 regulates COPI vesicle formation by recruiting the coatomer onto Golgi membranes to initiate its coat function. Coatomer complexes then bind cargo molecules and self-assemble to form spherical cages that yield COPI-coated vesicles. The heterotetrameric F-COPI subcomplex contains beta-, gamma-, delta-, and zeta-COP subunits, where beta- and gamma-COP subunits are related to the large AP subunits, and delta- and zeta-COP subunits are related to the medium and small AP subunits, respectively. Due to the sequence similarity to the AP complexes, the F-COPI subcomplex might play a role in the cargo-binding. The heterotrimeric B-COPI contains alpha-, beta-, and epsilon-COP subunits, which are not related to the adaptins. This subcomplex is thought to participate in the cage-forming and might serve a function similar to that of clathrin. This family corresponds to the mu homology domain of delta-subunit of COPI complex (delta-COP), which is distantly related to the C-terminal domain of mu chains among AP complexes. The delta-COP subunit appears tightly associated with the beta-COP subunit to confer its interaction with ARF1. In addition, both delta- and beta-COP subunits contribute to a common binding site for arginine (R)-based signals, which are sorting motifs conferring transient endoplasmic reticulum (ER) localization to unassembled subunits of multimeric membrane proteins.


Pssm-ID: 271162  Cd Length: 237  Bit Score: 254.46  E-value: 1.78e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349577968 289 NGILISIKEVINAEFSRDGTIHSSELKGVLELRINDHDLSHSNLKLADSIDvrdKSFQFKTHPNIDKQSFLSTKLISLRD 368
Cdd:cd09254    1 EGVHITVEEKISATLSRDGGLESLEVKGTLSLRINDEELAHIKLQLANNSD---KGFQFKTHPNVDKKLFTSDSVLGLKD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349577968 369 KSKAFPANDQSlGVLRWRKVAPaeDDSLIPLTLTTWvsPSESQQGFDVIIEYESVLET-ELADVIFTIPVFPQEPVDINt 447
Cdd:cd09254   78 PSKPFPVNDPV-GVLKWRLQGS--DESLLPLTINCW--PSESGGGCDVTIEYELNRDDlELNDVVISIPLPSGDAPVVN- 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349577968 448 esSTCSDAEVVNMDQemGTSIKISKI-AANDAGALAFTIEAPYEDALYPMTVSFeestrdKLAKSFTGMAIQSVVMANDh 526
Cdd:cd09254  152 --SIDGNYEYDSRKN--VLEWKIPVIdASNSSGSLEFSIPADDEDAFFPISVSF------TSSKTFCGVKVVEVVSADD- 220

                        250
                 ....*....|....*..
gi 349577968 527 DQELPYDVITSLKSDEY 543
Cdd:cd09254  221 GEPVPFSLETSLVADKY 237
Delta_COP_N cd14830
delta subunit of the F-COPI complex, N-terminal domain; Delta subunit of the heterotetrameric ...
 4-135 1.48e-59

delta subunit of the F-COPI complex, N-terminal domain; Delta subunit of the heterotetrameric F-COPI complex, which consists of one beta-, one gamma-, one delta-, and one zeta subunit, where beta- and gamma- subunits are related to the large adaptor protein (AP) complex subunits, and delta- and zeta- subunits are related to the medium and small AP subunits, respectively. F-COPI forms a coatomer together with the B-COPI subcomplex, which assembles with a small GTPase, ADP-ribosylation factor 1 (ARF1), playing an important role in the formation of COPI complex-coated vesicles. COPI complex-coated vesicles function in the early secretory pathway mediating the retrograde transport from the Golgi to the ER, and intra-Golgi transport.


Pssm-ID: 341434  Cd Length: 130  Bit Score: 193.51  E-value: 1.48e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349577968   4 LAASITTRQGKPLLSRQFKDLSKDRVLELLSNFQNLVSEiSSDHTFVEDKHVRYVYRPFDNYYIILITNRQSNIIKDLAT 83
Cdd:cd14830    1 LSAAICTKGGKILVSRQFVEISRSRIEGLLAAFPKLVGS-GSQHTYVETENVRYVYQPLEDLYLVLITTKNSNILEDLET 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 349577968  84 LNLFSQTINSYLSSFQDQEIFHNAFEILSSFDEIVSMgGYKENLSFTQVQTY 135
Cdd:cd14830   80 LRLLSRVVPEYCPSVDEEEILKNAFDLIFAFDEVISL-GYRENVTLSQIKTF 130
AP_longin-like cd14823
Longin-like domains of AP complex subunits; AP complex sigma subunits are part of the ...
 4-135 1.08e-20

Longin-like domains of AP complex subunits; AP complex sigma subunits are part of the heterotetrameric adaptor protein (AP) complex which consists of one large subunit (alpha-, gamma-, delta- or epsilon), one beta-, one mu-, and one sigma-subunit. In general, AP complexes link the cytosolic domains of the cargo proteins to the protein coat that induces vesicle budding in the donor compartment during vesicle transport. In most cases the coat protein is clathrin (AP1 and AP2 complex), but some of the other members of the AP complex family are associated with nonclathrin coats. The sigma subunit is comprised of a single longin domain and plays a role in binding dileucine-based sorting signals.


Pssm-ID: 341427  Cd Length: 131  Bit Score: 87.96  E-value: 1.08e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349577968   4 LAASITTRQGKPLLSRQFKDLSKDRVLELLSNFQNLVSEISSDHTFVEDKHVRYVYRPFDNYYIILITNRQSNIIKDLAT 83
Cdd:cd14823    1 KAILVLDNDGKRLFAKYYDDTYPSVKEQKAFEKNIFNKKHRTDSEIVLLEGLRVVYKSSIDLYFVVIGSKNENELLLLEV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 349577968  84 LNLFSQTINSYLSSFQDQEIFHNAFEILSSFDEIVSmGGYKENLSFTQVQTY 135
Cdd:cd14823   81 LNCLVDVLSEYFRKVEERAILENFEGLYFALDEIVD-GGYIQETDPKQVVHF 131
AP_MHD_Cterm cd07954
C-terminal domain of adaptor protein (AP) complexes medium mu subunits and its homologs (MHD); ...
 290-457 3.05e-11

C-terminal domain of adaptor protein (AP) complexes medium mu subunits and its homologs (MHD); This family corresponds to the C-terminal domain of heterotetrameric AP complexes medium mu subunits and its homologs existing in monomeric stonins, delta-subunit of the heteroheptameric coat protein I (delta-COPI), a protein encoded by a pro-death gene referred as MuD (also known as MUDENG, mu-2 related death-inducing gene), an endocytic adaptor syp1, the mammalian FCH domain only proteins (FCHo1/2), SH3-containing GRB2-like protein 3-interacting protein 1 (SGIP1), and related proteins. AP complexes participate in the formation of intracellular coated transport vesicles and select cargo molecules for incorporation into the coated vesicles in the late secretory and endocytic pathways. Stonins have been characterized as clathrin-dependent AP-2 mu chain related factors and may act as cargo-specific sorting adaptors in endocytosis. Coat protein complex I (COPI)-coated vesicles function in the early secretory pathway. They mediate the retrograde transport from the Golgi to the ER, and intra-Golgi transport. MuD is distantly related to the C-terminal domain of mu2 subunit of AP-2. It is able to induce cell death by itself and plays an important role in cell death in various tissues. Syp1 represents a novel type of endocytic adaptor protein that participates in endocytosis, promotes vesicle tabulation, and contributes to cell polarity and stress responses. It shares the same domain architecture with its two ubiquitously expressed mammalian counterparts, FCHo1/2, which represent key initial proteins ultimately controlling cellular nutrient uptake, receptor regulation, and synaptic vesicle retrieval. 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 SGIP1 does have a C-terminal MHD and has been classified into this family as well. It 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: 271157  Cd Length: 245  Bit Score: 63.58  E-value: 3.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349577968 290 GILISIKEVINAEFSRDGTIHSSELKGVLELRINDHDLSHSNLKLADsIDVRDKSFQFKTHPNIDKQSFLSTKLISlrdk 369
Cdd:cd07954    1 EVFLDVVEKVNLLISKDGSLLNSEVQGEIALKSFLSGMPEIRLGLNN-PDVGIKLDDVSFHPCVRLKRFESERVIS---- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349577968 370 skaFPANDQSLGVLRWRKVapaEDDSLIPLTLTTWVSPSESQQGFDVIIEYESVLETELADVIFTIPVfpqePVDINTES 449
Cdd:cd07954   76 ---FIPPDGEFELMSYRTV---EPWSILPITIFPVVSEEGSQLEVVITLKLSESLQLTAENVEVHIPL----PSGVTSLK 145


                 ....*...
gi 349577968 450 STCSDAEV 457
Cdd:cd07954  146 SKPSDGQA 153
Adap_comp_sub pfam00928
Adaptor complexes medium subunit family; This family also contains members which are coatomer ...
 288-437 4.40e-05

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


Pssm-ID: 395742  Cd Length: 259  Bit Score: 45.37  E-value: 4.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349577968  288 NNGILISIKEVINAEFSRDGTIHSSELKGVLELRINDHDLSHSNLKLAD-SIDVRDKSFQFKTHPNIDKqsFLSTKLISl 366
Cdd:pfam00928  12 KNEVFLDVIERVSVIVDKDGGLLNSEVQGTIDLKCFLSGMPELRLGLNDkLLLIELDDVSFHQCVNLDK--FESERVIS- 88

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 349577968  367 rdkskaFPANDQSLGVLRWRKVApaeDDSLIPLTLTTWVspSESQQGFDVIIEYE------SVLETElaDVIFTIPV 437
Cdd:pfam00928  89 ------FIPPDGEFELMRYRLST---NEVKLPFTVKPIV--SVSGDEGRVEIEVKlrsdfpKKLTAE--NVVISIPV 152
APS2 COG5030
Clathrin adaptor complex, small subunit [Intracellular trafficking and secretion];
8-143 1.71e-04

Clathrin adaptor complex, small subunit [Intracellular trafficking and secretion];


Pssm-ID: 227363  Cd Length: 152  Bit Score: 42.01  E-value: 1.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349577968   8 ITTRQGKPLLSRQFKDLSKDRVLELLSNFQNLVSEISSDHT-FVEDKHVRYVYRPFDNYYIILITNRQSNIIKDLATLNL 86
Cdd:COG5030    7 IFNRQGKPRLVKWYTPVSDPEQAKLIADIYELISARKPKESnFIEGKNEKIVYRRYATLYFVFGVDNDDNELIILELIHN 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 349577968  87 FSQTINSYLSSFQDQEIFHNAFEILSSFDEIVSMGGYKENLSFTQVQTYLSMESHEE 143
Cdd:COG5030   87 FVEILDRFFGNVCELDLIFNFQKVYAILDEMILGGEIIESSKNEVLEHVYALDAEST 143
Clat_adaptor_s pfam01217
Clathrin adaptor complex small chain;
8-138 3.72e-04

Clathrin adaptor complex small chain;


Pssm-ID: 460115  Cd Length: 142  Bit Score: 40.80  E-value: 3.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 349577968    8 ITTRQGKPLLSRQFKDLSKDRVLELLSNFQNLVSEISSDHT-FVEDKHVRYVYRPFDNYYIILITNRQSNIIKDLATLNL 86
Cdd:pfam01217   7 IFNRQGKPRLAKWYTPYSDPEQQKLIEQIYALISARKPKMSnFIEFNDLKVIYKRYATLYFVVIVDDQDNELIILELIHR 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 349577968   87 FSQTINSYLSSFQDQEIFHNAFEILSSFDEIVsMGGYKENLSFTQVQTYLSM 138
Cdd:pfam01217  87 FVESLDRYFGNVCELDLIFNFEKVYLILDEMV-MGGEILETSKNEVLHRVAL 137
 
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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