ID   COPE_CRIGR              Reviewed;         308 AA.
AC   Q60445;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=Coatomer subunit epsilon;
DE   AltName: Full=Epsilon-coat protein;
DE            Short=Epsilon-COP;
DE   AltName: Full=LDLF;
GN   Name=COPE;
OS   Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Cricetulus.
OX   NCBI_TaxID=10029;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8207054; DOI=10.1083/jcb.125.6.1213;
RA   Guo Q., Vasile E., Krieger M.;
RT   "Disruptions in Golgi structure and membrane traffic in a conditional
RT   lethal mammalian cell mutant are corrected by epsilon-COP.";
RL   J. Cell Biol. 125:1213-1224(1994).
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       In mammals, the coatomer can only be recruited by membranes associated
CC       with ADP-ribosylation factors (ARFs), which are small GTP-binding
CC       proteins; the complex also influences the Golgi structural integrity,
CC       as well as the processing, activity, and endocytic recycling of LDL
CC       receptors (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Oligomeric complex that consists of at least the alpha, beta,
CC       beta', gamma, delta, epsilon and zeta subunits.
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   -!- PTM: Polyubiquitinated by RCHY1 in the presence of androgen, leading to
CC       proteasomal degradation. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the COPE family. {ECO:0000305}.
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DR   EMBL; Z32554; CAA83551.1; -; mRNA.
DR   PIR; I48080; I48080.
DR   RefSeq; NP_001233606.1; NM_001246677.1.
DR   AlphaFoldDB; Q60445; -.
DR   SMR; Q60445; -.
DR   STRING; 10029.NP_001233606.1; -.
DR   Ensembl; ENSCGRT00001031411; ENSCGRP00001027164; ENSCGRG00001024248.
DR   Ensembl; ENSCGRT00001031417; ENSCGRP00001027170; ENSCGRG00001024248.
DR   GeneID; 100689412; -.
DR   KEGG; cge:100689412; -.
DR   CTD; 11316; -.
DR   eggNOG; KOG3081; Eukaryota.
DR   GeneTree; ENSGT00390000003478; -.
DR   OMA; MIVLSQH; -.
DR   OrthoDB; 1161199at2759; -.
DR   GO; GO:0030663; C:COPI-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0099612; P:protein localization to axon; IEA:Ensembl.
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; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR10805; PTHR10805; 1.
DR   PIRSF; PIRSF016478; Coatomer_esu; 1.
DR   SUPFAM; SSF48452; SSF48452; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Cytoplasmic vesicle; ER-Golgi transport; Golgi apparatus;
KW   Membrane; Phosphoprotein; Protein transport; Transport; Ubl conjugation.
FT   CHAIN           1..308
FT                   /note="Coatomer subunit epsilon"
FT                   /id="PRO_0000193850"
FT   MOD_RES         13
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O14579"
FT   MOD_RES         45
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O14579"
SQ   SEQUENCE   308 AA;  34523 MW;  33086CAA3759BEBE CRC64;
     MAPPAPGAAS GGSGEVDELF DVKNAFYIGS YQQCINEAQR VKLSSPDREV ERDVFLYRAY
     IAQRKYGVVL DEIKPSSAPE LQAVRMFADY LATENRRDAI VVELDREMSR SVDVTNTTFL
     LMAASVYFHD QNPDAALRTL HQGDSLECMA MTIQILLKLD RLDLARKELK KMQDQDEDAT
     LTQLATAWVN LAVGGEKLQE AYYIFQELAD KCSPTLLLLN GQAACHSAQG RWETAEGVLQ
     EALDKDSGHP ETLINLIVLS QHLGKPPEVT NRYLSQLKDA HRTHPFIKEY QAKENDFDRL
     ALQYAPSA