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Conserved domains on  [gi|9845242|ref|NP_063930|]
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coatomer subunit zeta-2 [Mus musculus]

Protein Classification

coatomer subunit zeta( domain architecture ID 13000590)

coatomer subunit zeta 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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Zeta-COP cd14829
zeta subunit of the F-COPI complex; Zeta subunit of the heterotetrameric F-COPI complex, which ...
 42-173 9.88e-76

zeta subunit of the F-COPI complex; Zeta 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: 341433  Cd Length: 132  Bit Score: 223.58  E-value: 9.88e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9845242   42 KAVFILDNDGRRLLAKYYDDTFPSVKEQMVFEKNVFNKTSRTESEIAFLGGMTIVYKSSIDIFLYVVGSSSENELMLMSV 121
Cdd:cd14829   1 KAILILDNDGKRVLAKYYDDTFPTVKEQKAFEKKLFDKTHKANAEIILLDGLTVVYKSNIDLTFYVVGSSDENELILASV 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 9845242  122 LACLFDSLSHILRKNVEKRWLLENMDGAFLVLDETVDGGVILESDPQQVIQK 173
Cdd:cd14829  81 LNCLYDALSLLLRKNVEKRALLENLDLVLLALDEIVDGGIILETDPTAIASR 132
 
Name Accession Description Interval E-value
Zeta-COP cd14829
zeta subunit of the F-COPI complex; Zeta subunit of the heterotetrameric F-COPI complex, which ...
 42-173 9.88e-76

zeta subunit of the F-COPI complex; Zeta 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: 341433  Cd Length: 132  Bit Score: 223.58  E-value: 9.88e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9845242   42 KAVFILDNDGRRLLAKYYDDTFPSVKEQMVFEKNVFNKTSRTESEIAFLGGMTIVYKSSIDIFLYVVGSSSENELMLMSV 121
Cdd:cd14829   1 KAILILDNDGKRVLAKYYDDTFPTVKEQKAFEKKLFDKTHKANAEIILLDGLTVVYKSNIDLTFYVVGSSDENELILASV 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 9845242  122 LACLFDSLSHILRKNVEKRWLLENMDGAFLVLDETVDGGVILESDPQQVIQK 173
Cdd:cd14829  81 LNCLYDALSLLLRKNVEKRALLENLDLVLLALDEIVDGGIILETDPTAIASR 132
Clat_adaptor_s pfam01217
Clathrin adaptor complex small chain;
40-177 6.74e-39

Clathrin adaptor complex small chain;


Pssm-ID: 460115  Cd Length: 142  Bit Score: 130.55  E-value: 6.74e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9845242     40 TIKAVFILDNDGRRLLAKYYDdTFPSVKEQMVFEKNVFNKTSRT--ESEIAFLGGMTIVYKSSIDIFLYVVGSSSENELM 117
Cdd:pfam01217   1 MIKAILIFNRQGKPRLAKWYT-PYSDPEQQKLIEQIYALISARKpkMSNFIEFNDLKVIYKRYATLYFVVIVDDQDNELI 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 9845242    118 LMSVLACLFDSLSHILRkNVEKRWLLENMDGAFLVLDETVDGGVILESDPQQVIQKVNFR 177
Cdd:pfam01217  80 ILELIHRFVESLDRYFG-NVCELDLIFNFEKVYLILDEMVMGGEILETSKNEVLHRVALL 138
RET3 COG5541
Vesicle coat complex COPI, zeta subunit [Posttranslational modification, protein turnover, ...
 37-205 3.54e-33

Vesicle coat complex COPI, zeta subunit [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227828  Cd Length: 187  Bit Score: 117.35  E-value: 3.54e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9845242   37 SLYTIKAVFILDNDGRRLLAKYYDDT---------FPSVKEQMVFEKNVFNKTSRTESEIAFLGGMTIVYKSSIDIFLYV 107
Cdd:COG5541   4 SLYDVEALLILDSQGERIYRKYYQPPhrseghqlvFNSVKKEKEFEKKLAEKTAKDRESILMFYDRLVMCKRLDDVLLYI 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9845242  108 VGSSSENELMLMSVLACLFDSLSHILRKNVEKRWLLENMDGAFLVLDETVDGGVILESDPQQVIQKV----NFRTDDSGL 183
Cdd:COG5541  84 VSPMEENEPFLGQVFDEIRAALILIVKTPTDKRNVWENYDQIVLLVDETIDEGVILETKSDEIADRVpkppNFEGQDGMK 163

                       170       180
                ....*....|....*....|..
gi 9845242  184 TEQSVAQVLQSAKEQIKWSLLK 205
Cdd:COG5541 164 VPRGFASFLHKATKKLSERSNK 185
 
Name Accession Description Interval E-value
Zeta-COP cd14829
zeta subunit of the F-COPI complex; Zeta subunit of the heterotetrameric F-COPI complex, which ...
 42-173 9.88e-76

zeta subunit of the F-COPI complex; Zeta 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: 341433  Cd Length: 132  Bit Score: 223.58  E-value: 9.88e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9845242   42 KAVFILDNDGRRLLAKYYDDTFPSVKEQMVFEKNVFNKTSRTESEIAFLGGMTIVYKSSIDIFLYVVGSSSENELMLMSV 121
Cdd:cd14829   1 KAILILDNDGKRVLAKYYDDTFPTVKEQKAFEKKLFDKTHKANAEIILLDGLTVVYKSNIDLTFYVVGSSDENELILASV 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 9845242  122 LACLFDSLSHILRKNVEKRWLLENMDGAFLVLDETVDGGVILESDPQQVIQK 173
Cdd:cd14829  81 LNCLYDALSLLLRKNVEKRALLENLDLVLLALDEIVDGGIILETDPTAIASR 132
AP_longin-like cd14823
Longin-like domains of AP complex subunits; AP complex sigma subunits are part of the ...
 42-172 2.64e-43

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: 141.50  E-value: 2.64e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9845242   42 KAVFILDNDGRRLLAKYYDDTFPSVKEQMVFEKNVFNKTSRTESEIAFLGGMTIVYKSSIDIFLYVVGSSSENELMLMSV 121
Cdd:cd14823   1 KAILVLDNDGKRLFAKYYDDTYPSVKEQKAFEKNIFNKKHRTDSEIVLLEGLRVVYKSSIDLYFVVIGSKNENELLLLEV 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 9845242  122 LACLFDSLSHILRkNVEKRWLLENMDGAFLVLDETVDGGVILESDPQQVIQ 172
Cdd:cd14823  81 LNCLVDVLSEYFR-KVEERAILENFEGLYFALDEIVDGGYIQETDPKQVVH 130
Clat_adaptor_s pfam01217
Clathrin adaptor complex small chain;
40-177 6.74e-39

Clathrin adaptor complex small chain;


Pssm-ID: 460115  Cd Length: 142  Bit Score: 130.55  E-value: 6.74e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9845242     40 TIKAVFILDNDGRRLLAKYYDdTFPSVKEQMVFEKNVFNKTSRT--ESEIAFLGGMTIVYKSSIDIFLYVVGSSSENELM 117
Cdd:pfam01217   1 MIKAILIFNRQGKPRLAKWYT-PYSDPEQQKLIEQIYALISARKpkMSNFIEFNDLKVIYKRYATLYFVVIVDDQDNELI 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 9845242    118 LMSVLACLFDSLSHILRkNVEKRWLLENMDGAFLVLDETVDGGVILESDPQQVIQKVNFR 177
Cdd:pfam01217  80 ILELIHRFVESLDRYFG-NVCELDLIFNFEKVYLILDEMVMGGEILETSKNEVLHRVALL 138
RET3 COG5541
Vesicle coat complex COPI, zeta subunit [Posttranslational modification, protein turnover, ...
 37-205 3.54e-33

Vesicle coat complex COPI, zeta subunit [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227828  Cd Length: 187  Bit Score: 117.35  E-value: 3.54e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9845242   37 SLYTIKAVFILDNDGRRLLAKYYDDT---------FPSVKEQMVFEKNVFNKTSRTESEIAFLGGMTIVYKSSIDIFLYV 107
Cdd:COG5541   4 SLYDVEALLILDSQGERIYRKYYQPPhrseghqlvFNSVKKEKEFEKKLAEKTAKDRESILMFYDRLVMCKRLDDVLLYI 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9845242  108 VGSSSENELMLMSVLACLFDSLSHILRKNVEKRWLLENMDGAFLVLDETVDGGVILESDPQQVIQKV----NFRTDDSGL 183
Cdd:COG5541  84 VSPMEENEPFLGQVFDEIRAALILIVKTPTDKRNVWENYDQIVLLVDETIDEGVILETKSDEIADRVpkppNFEGQDGMK 163

                       170       180
                ....*....|....*....|..
gi 9845242  184 TEQSVAQVLQSAKEQIKWSLLK 205
Cdd:COG5541 164 VPRGFASFLHKATKKLSERSNK 185
longin-like cd14818
Longin-like domains; Longin-like domains are small protein domains present in a variety of ...
 42-156 1.59e-27

Longin-like domains; Longin-like domains are small protein domains present in a variety of proteins and members of protein complexes involved in or required for different steps during the transport of proteins from the ribosome to the ER to the plasma membrane, via the Golgi apparatus. Examples are mu and sigma subunits of the heterotetrameric adaptor protein (AP) complex, zeta and delta subunits of the heterotetrameric F-COPI complex, a subgroup of R-SNARE proteins, a subfamily of the transport protein particle (TRAPP), and the signal recognition particle receptor subunit alpha (SR-alpha).


Pssm-ID: 341426  Cd Length: 117  Bit Score: 100.68  E-value: 1.59e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9845242   42 KAVFILDNDGRRLLAKYYDDTFPSVKEQMVFEKNVFNKTSRTE--SEIAFLGGMTIVYKSSIDIFLYVVGSSSENELMLM 119
Cdd:cd14818   1 LQLAVFDPQGQVLAASNWLGKKPSVKFSLIQIKSFFSKLITSGfdFLTLTIGSYTFHYYLNKGLYFVVITDEQELRQELF 80

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 9845242  120 SVLACLFDSLSHILRKNVEKRWLLENMDGAFLVLDET 156
Cdd:cd14818  81 QTLNLLLKEFNSLHGSEVITKNIEDDLEEFESYLDIK 117
AP3_sigma cd14834
AP-3 complex subunit sigma; AP-3 complex sigma subunit is part of the heterotetrameric adaptor ...
 41-175 1.05e-09

AP-3 complex subunit sigma; AP-3 complex sigma subunit is part of the heterotetrameric adaptor protein (AP)-1 complex which consists of one large delta-, one beta-, one mu-, and one sigma-subunit. 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. AP-3 binds the coat protein clathrin and the phospholipid PI(3)P and it is localized in the endosome. The sigma subunit is comprised of a single longin domain and plays a role in binding dileucine-based sorting signals.


Pssm-ID: 341438  Cd Length: 146  Bit Score: 54.54  E-value: 1.05e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9845242   41 IKAVFILDNDGRRLLAKYYDDtFPSVKEQMVFEKNVFNKTSRTESEIAFLGGMTIVYKSSIDI---------FLYVVgSS 111
Cdd:cd14834   2 IKAILIFNNHGKPRLSKFYQH-YSEEKQQQIIRETFQLVSKRDDNVCNFLEGGSLIGGSDTKLiyrhyatlyFVFCV-DS 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9845242  112 SENELMLMSVLACLFDSLSHILrKNVEKRWLLENMDGAFLVLDETVDGGVILESDPQQVIQKVN 175
Cdd:cd14834  80 SESELGILDLIQVFVETLDKCF-ENVCELDLIFHVDKVHYILDEIVMGGMVLETNMTEILTAIE 142
AP_sigma cd14827
AP complex subunit sigma; AP complex sigma subunits are part of the heterotetrameric adaptor ...
 42-174 1.01e-08

AP complex subunit sigma; 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: 341431  Cd Length: 138  Bit Score: 52.06  E-value: 1.01e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9845242   42 KAVFILDNDGRRLLAKYYddTFPSVKEQMVFEKNVFNK-TSRTESEIAFL--GGMTIVYKSSIDIFLYVVGSSSENELML 118
Cdd:cd14827   1 RFILLFNRQGKTRLAKWY--MQFDDDERQKLIEEIVQVvLSRDAKHCNFVefRNYKLIYRRYASLYFCICVDSNDNELAI 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 9845242  119 MSVLACLFDSLSHILrKNVEKRWLLENMDGAFLVLDETVDGGVILESDPQQVIQKV 174
Cdd:cd14827  79 LEAIHNFVETLDKYF-ENVCELDLIFNFEKVYFIVDEMVLGGEIRETSQTKILKQI 133
AP4_sigma cd14832
AP-4 complex subunit sigma; AP-4 complex sigma subunit is part of the heterotetrameric adaptor ...
 45-175 5.84e-07

AP-4 complex subunit sigma; AP-4 complex sigma subunit is part of the heterotetrameric adaptor protein (AP)-1 complex which consists of one large epsilon-, one beta-, one mu-, and one sigma-subunit. 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. AP-4 does not bind the coat protein clathrin, it is associated with nonclathrin coats. Its phospholipid binding partner is unknown and it is localized in the trans-Golgi network (TGN). The sigma subunit is comprised of a single longin domain and plays a role in binding dileucine-based sorting signals.


Pssm-ID: 341436  Cd Length: 138  Bit Score: 46.84  E-value: 5.84e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9845242   45 FIL--DNDGRRLLAKYYDdtFPSVKEQMVFEKNVFNKT-SRTESEIAFLG--GMTIVYKSSIDIFLYVVGSSSENELMLM 119
Cdd:cd14832   2 FILmvNKQGQTRLAQYYE--FLSIEERVALEGEIIRKClSRSEKQCSFLEyrGYKLVYRRYASLYFIVGVDEDENELAIL 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 9845242  120 SVLACLFDSLSHILrKNVEKRWLLENMDGAFLVLDETVDGGVILESDPQQVIQKVN 175
Cdd:cd14832  80 EFIHNLVETLDKYF-ENVCELDIMFNLEKAHFILDEMVMNGCIVETNKSNILAPIL 134
APS2 COG5030
Clathrin adaptor complex, small subunit [Intracellular trafficking and secretion];
41-174 1.17e-06

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


Pssm-ID: 227363  Cd Length: 152  Bit Score: 46.64  E-value: 1.17e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9845242   41 IKAVFILDNDGRRLLAKYYddTFPSVKEQMVFEKNVFNKTS---RTESEIAFLGGMTIVYKSSIDIFLYVVGSSSENELM 117
Cdd:COG5030   2 IKFVLIFNRQGKPRLVKWY--TPVSDPEQAKLIADIYELISarkPKESNFIEGKNEKIVYRRYATLYFVFGVDNDDNELI 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 9845242  118 LMSVLACLFDSLSHILrKNVEKRWLLENMDGAFLVLDETVDGGVILESDPQQVIQKV 174
Cdd:COG5030  80 ILELIHNFVEILDRFF-GNVCELDLIFNFQKVYAILDEMILGGEIIESSKNEVLEHV 135
AP2_Mu_N cd14836
AP-2 complex subunit mu N-terminal domain; AP-2 complex mu subunit is part of the ...
 41-175 8.66e-04

AP-2 complex subunit mu N-terminal domain; AP-2 complex mu subunit is part of the heterotetrameric adaptor protein (AP)-2 complex which consists of one large alpha-, one beta-, one mu-, and one sigma-subunit. 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 the case of AP-2 the coat protein is clathrin. AP-2 binds the phospholipid PI(4,5)P2 which is important for its localisation to the plasma membrane. The mu subunit is comprised of an N-terminal longin domain followed by a C-terminal domain which is involved in the binding of the Y-X-X-Phi sorting signal.


Pssm-ID: 341440  Cd Length: 140  Bit Score: 38.27  E-value: 8.66e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9845242   41 IKAVFILDNDGRRLLAKYYDDtfpSVKEQM--VFEKNVFNKTSRTESEIAFLGGMTIVYKSSIDIFLYVVGSSSENELML 118
Cdd:cd14836   2 ISALFIYNLKGDVLISRTYRD---DVKRSVadAFRVQVINAKEQVRSPVLTIGSTSFFHVRHGNLYLVAVTRSNVNAAMV 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 9845242  119 MSVLACLFDSLSHILRKNVEKRwLLENMDGAFLVLDETVDGGVILESDPQQVIQKVN 175
Cdd:cd14836  79 FEFLYKLVQLFKSYFGKFNEDS-IKNNFVLIYELLDEILDFGYPQNTEPEALKTYIT 134
 
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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