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   24-JAN-2024, entry version 170.
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,
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).
RN   [5]
RP   INTERACTION WITH SVEP1.
RX   PubMed=36792666; DOI=10.1038/s41467-023-36486-0;
RA   Elenbaas J.S., Pudupakkam U., Ashworth K.J., Kang C.J., Patel V.,
RA   Santana K., Jung I.H., Lee P.C., Burks K.H., Amrute J.M., Mecham R.P.,
RA   Halabi C.M., Alisio A., Di Paola J., Stitziel N.O.;
RT   "SVEP1 is an endogenous ligand for the orphan receptor PEAR1.";
RL   Nat. Commun. 14:850-850(2023).
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. Interacts with SCYL1.
CC       Interacts with JAGN1 (By similarity). Interacts with TMEM41B (By
CC       similarity). Interacts with SVEP1 (PubMed:36792666). Probably interacts
CC       with PEX11A. {ECO:0000250, ECO:0000250|UniProtKB:P53621,
CC       ECO:0000269|PubMed:36792666}.
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   EMDB; EMD-3720; -.
DR   EMDB; EMD-3721; -.
DR   EMDB; EMD-3722; -.
DR   EMDB; EMD-3723; -.
DR   EMDB; EMD-3724; -.
DR   SMR; Q8CIE6; -.
DR   BioGRID; 198835; 56.
DR   CORUM; Q8CIE6; -.
DR   IntAct; Q8CIE6; 24.
DR   MINT; Q8CIE6; -.
DR   STRING; 10090.ENSMUSP00000118179; -.
DR   GlyGen; Q8CIE6; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q8CIE6; -.
DR   MetOSite; Q8CIE6; -.
DR   PhosphoSitePlus; Q8CIE6; -.
DR   SwissPalm; Q8CIE6; -.
DR   EPD; Q8CIE6; -.
DR   jPOST; Q8CIE6; -.
DR   MaxQB; Q8CIE6; -.
DR   PaxDb; 10090-ENSMUSP00000118179; -.
DR   PeptideAtlas; Q8CIE6; -.
DR   ProteomicsDB; 283606; -.
DR   Pumba; Q8CIE6; -.
DR   Antibodypedia; 34275; 157 antibodies from 26 providers.
DR   DNASU; 12847; -.
DR   Ensembl; ENSMUST00000135192.8; ENSMUSP00000118179.2; ENSMUSG00000026553.18.
DR   GeneID; 12847; -.
DR   KEGG; mmu:12847; -.
DR   UCSC; uc007dpn.2; mouse.
DR   AGR; MGI:1334462; -.
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; 20819at2759; -.
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 78 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 268 other cell types or tissues.
DR   ExpressionAtlas; Q8CIE6; baseline and differential.
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   CDD; cd22948; Coatomer_WDAD_alpha; 1.
DR   CDD; cd00200; WD40; 1.
DR   Gene3D; 1.25.40.470; -; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   InterPro; IPR047312; Coatomer_alpha_WD-assoc_reg.
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; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001680; WD40_rpt.
DR   PANTHER; PTHR19876; COATOMER; 1.
DR   PANTHER; PTHR19876:SF1; COATOMER SUBUNIT ALPHA; 1.
DR   Pfam; PF04053; Coatomer_WDAD; 1.
DR   Pfam; PF06957; COPI_C; 1.
DR   Pfam; PF00400; WD40; 6.
DR   PIRSF; PIRSF003354; Coatomer_alpha_subunit; 1.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF51004; C-terminal (heme d1) domain of cytochrome cd1-nitrite reductase; 1.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 6.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
DR   Genevisible; Q8CIE6; MM.
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
//