COPE_MOUSE
ID COPE_MOUSE Reviewed; 308 AA.
AC O89079; Q9JM65;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Coatomer subunit epsilon;
DE AltName: Full=Epsilon-coat protein;
DE Short=Epsilon-COP;
GN Name=Cope; Synonyms=Cope1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Hahn Y., Chung J.H.;
RT "Mouse Cope1 gene for nonclathrin coat protein epsilon-COP.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 155-298.
RC STRAIN=BALB/cJ; TISSUE=Spleen;
RX PubMed=9798653; DOI=10.1016/s0161-5890(98)00031-5;
RA Chu C.C., Paul W.E.;
RT "Expressed genes in interleukin-4 treated B cells identified by cDNA
RT representational difference analysis.";
RL Mol. Immunol. 35:487-502(1998).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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: Phosphorylated by PKA. {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; AB039837; BAA92384.1; -; mRNA.
DR EMBL; BC009170; AAH09170.1; -; mRNA.
DR EMBL; BC083336; AAH83336.1; -; mRNA.
DR EMBL; U89427; AAC36533.1; -; mRNA.
DR CCDS; CCDS22365.1; -.
DR RefSeq; NP_067513.1; NM_021538.1.
DR PDB; 5A1V; EM; 21.00 A; Q/Z=1-308.
DR PDB; 5A1Y; EM; 21.00 A; X/Z=1-308.
DR PDB; 5NZT; EM; 17.00 A; E=1-308.
DR PDB; 5NZV; EM; 17.30 A; E/O=1-308.
DR PDBsum; 5A1V; -.
DR PDBsum; 5A1Y; -.
DR PDBsum; 5NZT; -.
DR PDBsum; 5NZV; -.
DR AlphaFoldDB; O89079; -.
DR SMR; O89079; -.
DR BioGRID; 208506; 16.
DR CORUM; O89079; -.
DR IntAct; O89079; 1.
DR STRING; 10090.ENSMUSP00000071078; -.
DR iPTMnet; O89079; -.
DR PhosphoSitePlus; O89079; -.
DR SwissPalm; O89079; -.
DR REPRODUCTION-2DPAGE; O89079; -.
DR EPD; O89079; -.
DR jPOST; O89079; -.
DR MaxQB; O89079; -.
DR PaxDb; O89079; -.
DR PeptideAtlas; O89079; -.
DR PRIDE; O89079; -.
DR ProteomicsDB; 283607; -.
DR Antibodypedia; 28232; 180 antibodies from 28 providers.
DR DNASU; 59042; -.
DR Ensembl; ENSMUST00000066469; ENSMUSP00000071078; ENSMUSG00000055681.
DR GeneID; 59042; -.
DR KEGG; mmu:59042; -.
DR UCSC; uc009lzx.1; mouse.
DR CTD; 11316; -.
DR MGI; MGI:1891702; Cope.
DR VEuPathDB; HostDB:ENSMUSG00000055681; -.
DR eggNOG; KOG3081; Eukaryota.
DR GeneTree; ENSGT00390000003478; -.
DR HOGENOM; CLU_049363_0_0_1; -.
DR InParanoid; O89079; -.
DR OMA; MIVLSQH; -.
DR OrthoDB; 1161199at2759; -.
DR PhylomeDB; O89079; -.
DR TreeFam; TF313390; -.
DR Reactome; R-MMU-6807878; COPI-mediated anterograde transport.
DR Reactome; R-MMU-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR BioGRID-ORCS; 59042; 16 hits in 74 CRISPR screens.
DR ChiTaRS; Cope; mouse.
DR PRO; PR:O89079; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; O89079; protein.
DR Bgee; ENSMUSG00000055681; Expressed in seminal vesicle and 267 other tissues.
DR ExpressionAtlas; O89079; baseline and differential.
DR Genevisible; O89079; MM.
DR GO; GO:0030126; C:COPI vesicle coat; IBA:GO_Central.
DR GO; GO:0030137; C:COPI-coated vesicle; IDA:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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:0099612; P:protein localization to axon; IMP:MGI.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Cytoplasmic vesicle; ER-Golgi transport;
KW Golgi apparatus; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Transport; Ubl conjugation.
FT CHAIN 1..308
FT /note="Coatomer subunit epsilon"
FT /id="PRO_0000193852"
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"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14579"
FT CONFLICT 291
FT /note="Q -> R (in Ref. 3; AAC36533)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 308 AA; 34567 MW; 81331BDDB1F99270 CRC64;
MAPPVPGAVS GGSGEVDELF DVKNAFYIGS YQQCINEAQR VKLSSPEREV ERDVFLYRAY
LAQRKYGVVL DEIKPSSAPE LQAVRMFAEY LASENQRDSI VLELDREMSR SVDVTNTTFL
LMAASIYFHD QNPDAALRTL HQGDGLECMA MTIQILLKLD RLDLARKELK KMQDQDEDAT
LTQLATAWVN LAVGGEKLQE AYYIFQELAD KCSPTLLLLN GQAACHSAQG RWETAEGVLQ
EALDKDSGHP ETLINLIVLS QHLGKPPEVT NRYLSQLKDA HRAHPFIKEY QAKENDFDRL
AMQYAPSA
