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   24-JAN-2024, entry version 165.
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,
RC   Pancreas, 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   EMDB; EMD-3722; -.
DR   EMDB; EMD-3724; -.
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; 10090-ENSMUSP00000071078; -.
DR   PeptideAtlas; O89079; -.
DR   ProteomicsDB; 283607; -.
DR   Pumba; O89079; -.
DR   Antibodypedia; 28232; 207 antibodies from 28 providers.
DR   DNASU; 59042; -.
DR   Ensembl; ENSMUST00000066469.14; ENSMUSP00000071078.8; ENSMUSG00000055681.15.
DR   GeneID; 59042; -.
DR   KEGG; mmu:59042; -.
DR   UCSC; uc009lzx.1; mouse.
DR   AGR; MGI:1891702; -.
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; 6256at2759; -.
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; 17 hits in 79 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 269 other cell types or tissues.
DR   ExpressionAtlas; O89079; baseline and differential.
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; Tetratricopeptide repeat domain; 1.
DR   InterPro; IPR006822; Coatomer_esu.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR10805; COATOMER SUBUNIT EPSILON; 1.
DR   PANTHER; PTHR10805:SF0; COATOMER SUBUNIT EPSILON; 1.
DR   Pfam; PF04733; Coatomer_E; 1.
DR   PIRSF; PIRSF016478; Coatomer_esu; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   Genevisible; O89079; MM.
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
//