COPA_MOUSE
ID COPA_MOUSE Reviewed; 1224 AA.
AC Q8CIE6; E9Q075;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Coatomer subunit alpha;
DE AltName: Full=Alpha-coat protein;
DE Short=Alpha-COP;
DE Contains:
DE RecName: Full=Xenin;
DE AltName: Full=Xenopsin-related peptide;
DE Contains:
DE RecName: Full=Proxenin;
GN Name=Copa;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver, 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173 AND SER-402, AND
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. 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 to 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 -!- FUNCTION: Xenin stimulates exocrine pancreatic secretion. It inhibits
CC pentagastrin-stimulated secretion of acid, to induce exocrine
CC pancreatic secretion and to affect small and large intestinal motility.
CC In the gut, xenin interacts with the neurotensin receptor (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Oligomeric complex that consists of at least the alpha, beta,
CC beta', gamma, delta, epsilon and zeta subunits. Probably interacts with
CC PEX11A. Interacts with SCYL1. Interacts with JAGN1 (By similarity).
CC Interacts with TMEM41B (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:P53621}.
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 -!- SUBCELLULAR LOCATION: [Xenin]: Secreted {ECO:0000250}.
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DR EMBL; AC158930; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC024070; AAH24070.1; -; mRNA.
DR EMBL; BC047429; AAH47429.1; -; mRNA.
DR CCDS; CCDS35780.1; -.
DR RefSeq; NP_034068.3; NM_009938.4.
DR PDB; 5A1U; EM; 13.00 A; C=1-1224.
DR PDB; 5A1V; EM; 21.00 A; C/K/T=1-1224.
DR PDB; 5A1W; EM; 18.00 A; C=1-1224.
DR PDB; 5A1X; EM; 23.00 A; C/K=1-1224.
DR PDB; 5A1Y; EM; 21.00 A; C/K=1-1224.
DR PDB; 5NZR; EM; 9.20 A; A=1-1224.
DR PDB; 5NZS; EM; 10.10 A; A=1-1224.
DR PDB; 5NZT; EM; 17.00 A; A=1-1224.
DR PDB; 5NZU; EM; 15.00 A; A=1-1224.
DR PDB; 5NZV; EM; 17.30 A; A/H=1-1224.
DR PDBsum; 5A1U; -.
DR PDBsum; 5A1V; -.
DR PDBsum; 5A1W; -.
DR PDBsum; 5A1X; -.
DR PDBsum; 5A1Y; -.
DR PDBsum; 5NZR; -.
DR PDBsum; 5NZS; -.
DR PDBsum; 5NZT; -.
DR PDBsum; 5NZU; -.
DR PDBsum; 5NZV; -.
DR AlphaFoldDB; Q8CIE6; -.
DR SMR; Q8CIE6; -.
DR BioGRID; 198835; 55.
DR CORUM; Q8CIE6; -.
DR IntAct; Q8CIE6; 24.
DR MINT; Q8CIE6; -.
DR STRING; 10090.ENSMUSP00000118179; -.
DR iPTMnet; Q8CIE6; -.
DR PhosphoSitePlus; Q8CIE6; -.
DR SwissPalm; Q8CIE6; -.
DR EPD; Q8CIE6; -.
DR jPOST; Q8CIE6; -.
DR MaxQB; Q8CIE6; -.
DR PaxDb; Q8CIE6; -.
DR PeptideAtlas; Q8CIE6; -.
DR PRIDE; Q8CIE6; -.
DR ProteomicsDB; 283606; -.
DR Antibodypedia; 34275; 138 antibodies from 25 providers.
DR DNASU; 12847; -.
DR Ensembl; ENSMUST00000135192; ENSMUSP00000118179; ENSMUSG00000026553.
DR GeneID; 12847; -.
DR KEGG; mmu:12847; -.
DR UCSC; uc007dpn.2; mouse.
DR CTD; 1314; -.
DR MGI; MGI:1334462; Copa.
DR VEuPathDB; HostDB:ENSMUSG00000026553; -.
DR eggNOG; KOG0292; Eukaryota.
DR GeneTree; ENSGT00940000155451; -.
DR HOGENOM; CLU_007565_1_0_1; -.
DR InParanoid; Q8CIE6; -.
DR OrthoDB; 139008at2759; -.
DR TreeFam; TF105693; -.
DR Reactome; R-MMU-6807878; COPI-mediated anterograde transport.
DR Reactome; R-MMU-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR BioGRID-ORCS; 12847; 25 hits in 74 CRISPR screens.
DR ChiTaRS; Copa; mouse.
DR PRO; PR:Q8CIE6; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8CIE6; protein.
DR Bgee; ENSMUSG00000026553; Expressed in vault of skull and 264 other tissues.
DR ExpressionAtlas; Q8CIE6; baseline and differential.
DR Genevisible; Q8CIE6; MM.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0030126; C:COPI vesicle coat; ISO:MGI.
DR GO; GO:0030137; C:COPI-coated vesicle; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030426; C:growth cone; IDA:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IDA: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:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0030157; P:pancreatic juice secretion; ISO:MGI.
DR GO; GO:0099612; P:protein localization to axon; IMP:MGI.
DR GO; GO:1902463; P:protein localization to cell leading edge; IMP:MGI.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR024977; Apc4_WD40_dom.
DR InterPro; IPR016391; Coatomer_asu.
DR InterPro; IPR010714; Coatomer_asu_C.
DR InterPro; IPR006692; Coatomer_WD-assoc_reg.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR011048; Haem_d1_sf.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF12894; ANAPC4_WD40; 1.
DR Pfam; PF04053; Coatomer_WDAD; 1.
DR Pfam; PF06957; COPI_C; 1.
DR Pfam; PF00400; WD40; 3.
DR PIRSF; PIRSF003354; Coatomer_alpha_subunit; 1.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR SUPFAM; SSF51004; SSF51004; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 6.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Cytoplasmic vesicle; ER-Golgi transport;
KW Golgi apparatus; Hormone; Membrane; Methylation; Phosphoprotein;
KW Protein transport; Reference proteome; Repeat; Secreted; Transport;
KW WD repeat.
FT CHAIN 1..1224
FT /note="Coatomer subunit alpha"
FT /id="PRO_0000327496"
FT PEPTIDE 1..35
FT /note="Proxenin"
FT /id="PRO_0000327497"
FT PEPTIDE 1..25
FT /note="Xenin"
FT /id="PRO_0000327498"
FT REPEAT 7..37
FT /note="WD 1"
FT REPEAT 49..79
FT /note="WD 2"
FT REPEAT 91..121
FT /note="WD 3"
FT REPEAT 133..163
FT /note="WD 4"
FT REPEAT 203..233
FT /note="WD 5"
FT REPEAT 247..277
FT /note="WD 6"
FT MOD_RES 173
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 185
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P53621"
FT MOD_RES 402
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 591
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P53621"
FT MOD_RES 965
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P53621"
FT MOD_RES 1193
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53621"
FT CONFLICT 761
FT /note="S -> T (in Ref. 2; AAH24070/AAH47429)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1224 AA; 138432 MW; 48AB72AD9CBDDD6B CRC64;
MLTKFETKSA RVKGLSFHPK RPWILTSLHN GVIQLWDYRM CTLIDKFDEH DGPVRGIDFH
KQQPLFVSGG DDYKIKVWNY KLRRCLFTLL GHLDYIRTTF FHHEYPWILS ASDDQTIRVW
NWQSRTCVCV LTGHNHYVMC AQFHPSEDLV VSASLDQTVR VWDISGLRKK NLSPGAVESD
VRGITGVDLF GTTDAVVKHV LEGHDRGVNW AAFHPTMPLI VSGADDRQVK IWRMNESKAW
EVDTCRGHYN NVSCAVFHPR QELILSNSED KSIRVWDMSK RTGVQTFRRD HDRFWVLAAH
PNLNLFAAGH DGGMIVFKLE RERPAYAVHG NMLHYVKDRF LRQLDFNSSK DVAVMQLRSG
SKFPVFNMSY NPAENAVLLC TRASNLENST YDLYTIPKDA DSQNPDAPEG KRSSGLTAVW
VARNRFAVLD RMHSLLIKNL KNEITKKIQV PNCDEIFYAG TGNLLLRDAD SITLFDVQQK
RTLASVKISK VKYVIWSADM SHVALLAKHA IVICNRKLDA LCNIHENIRV KSGAWDESGV
FIYTTSNHIK YAVTTGDHGI IRTLDLPIYV TRVKGNNVYC LDRECRPRVL TIDPTEFKFK
LALINRKYDE VLHMVRNAKL VGQSIIAYLQ KKGYPEVALH FVKDEKTRFS LALECGNIEI
ALEAAKALDD KNCWEKLGEV ALLQGNHQIV EMCYQRTKNF DKLSFLYLIT GNLEKLRKMM
KIAEIRKDMS GHYQNALYLG DVSERVRILK NCGQKSLAYL SAATHGLDEE AESLKETFDP
EKETIPDIDP NAKLLQPPAP IMPLDTNWPL LTVSKGFFEG SIASKGKGGA LAADIDIDTV
GTEGWGEDAE LQLDEDGFVE APEGLGEDVL GKGQEEGGGW DVEEDLELPP ELDVPSGVSG
SAEDGFFVPP TKGTSPTQIW CNNSQLPVDH ILAGSFETAM RLLHDQVGVI QFGPYKQLFL
QTYARGRTTY QALPCLPSMY SYPNRNWKDA GLKNGVPAVG LKLNDLIQRL QLCYQLTTVG
KFEEAVEKFR SILLSVPLLV VDNKQEIAEA QQLITICREY IVGLCMEIER KKLPKETLDQ
QKRICEMAAY FTHSNLQPVH MILVLRTALN LFFKLKNFKT AATFARRLLE LGPKPEVAQQ
TRKILSACEK NPTDACQLNY DMHNPFDICA ASYRPIYRGK PVEKCPLSGA CYSPEFKGQI
CRVTTVTEIG KDVIGLRISP LQFR
