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COPE_CAEEL
ID   COPE_CAEEL              Reviewed;         292 AA.
AC   O62246;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 135.
DE   RecName: Full=Coatomer subunit epsilon;
DE   AltName: Full=Epsilon-coat protein;
DE            Short=Epsilon-COP;
GN   Name=cope-1; ORFNames=F45G2.4;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
CC   -!- FUNCTION: The coatomer is a cytosolic protein complex that binds to
CC       dilysine motifs and reversibly associates with Golgi non-clathrin-
CC       coated vesicles, which further mediate biosynthetic protein transport
CC       from the ER, via the Golgi up to the trans Golgi network. The coatomer
CC       complex is required for budding from Golgi membranes, and is essential
CC       for the retrograde Golgi-to-ER transport of dilysine-tagged proteins
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Oligomeric complex that consists of at least the alpha, beta,
CC       beta', gamma, delta, epsilon and zeta subunits. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC       side {ECO:0000250}. Cytoplasmic vesicle, COPI-coated vesicle membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC       side {ECO:0000250}. Note=The coatomer is cytoplasmic or polymerized on
CC       the cytoplasmic side of the Golgi, as well as on the vesicles/buds
CC       originating from it. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the COPE family. {ECO:0000305}.
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DR   EMBL; Z93382; CAB07613.1; -; Genomic_DNA.
DR   PIR; T22236; T22236.
DR   RefSeq; NP_499771.1; NM_067370.4.
DR   AlphaFoldDB; O62246; -.
DR   SMR; O62246; -.
DR   BioGRID; 41935; 13.
DR   DIP; DIP-24766N; -.
DR   IntAct; O62246; 1.
DR   STRING; 6239.F45G2.4.2; -.
DR   EPD; O62246; -.
DR   PaxDb; O62246; -.
DR   PeptideAtlas; O62246; -.
DR   EnsemblMetazoa; F45G2.4.1; F45G2.4.1; WBGene00009732.
DR   GeneID; 176766; -.
DR   KEGG; cel:CELE_F45G2.4; -.
DR   UCSC; F45G2.4.2; c. elegans.
DR   CTD; 176766; -.
DR   WormBase; F45G2.4; CE16047; WBGene00009732; cope-1.
DR   eggNOG; KOG3081; Eukaryota.
DR   GeneTree; ENSGT00390000003478; -.
DR   HOGENOM; CLU_049363_0_0_1; -.
DR   InParanoid; O62246; -.
DR   OMA; MIVLSQH; -.
DR   OrthoDB; 1161199at2759; -.
DR   PhylomeDB; O62246; -.
DR   Reactome; R-CEL-6807878; COPI-mediated anterograde transport.
DR   Reactome; R-CEL-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR   PRO; PR:O62246; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00009732; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR   GO; GO:0030126; C:COPI vesicle coat; IBA:GO_Central.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; HDA:WormBase.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR   GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IBA:GO_Central.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IEA:InterPro.
DR   Gene3D; 1.25.40.10; -; 1.
DR   InterPro; IPR006822; Coatomer_esu.
DR   InterPro; IPR002885; Pentatricopeptide_repeat.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR10805; PTHR10805; 1.
DR   PIRSF; PIRSF016478; Coatomer_esu; 1.
DR   SUPFAM; SSF48452; SSF48452; 1.
DR   TIGRFAMs; TIGR00756; PPR; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Cytoplasmic vesicle; ER-Golgi transport; Golgi apparatus;
KW   Membrane; Protein transport; Reference proteome; Transport.
FT   CHAIN           1..292
FT                   /note="Coatomer subunit epsilon"
FT                   /id="PRO_0000193853"
SQ   SEQUENCE   292 AA;  32803 MW;  A1BC975637EC3B47 CRC64;
     MADKLFSIRN YFFLGSYQSC IGEALKFSSK NEEEKQEKDV YLYRSYIAQG QAFIPLKEIP
     AATKSADLAA VRRYAEFRNN PAAKKKILAE VQEEVASRNI KSEIAAVLAA TILNEADLSQ
     DAFRAVSRFE GLEARASKVF ILIKMNKRKL AIGEVKKMNQ IDEDATLSQL ANALVTSFGA
     SGKVKDALYI YSEMSDKYGR TTDLEMHQAV VSILTQDYAA AEELLESALE RDNKDADVLI
     NSIVSAQLNE KDDDVVERFI SQLKHEHPNH PWVIDFNEKE AEFDRVASDS RA
 
 
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