ID   COPA_HUMAN              Reviewed;        1224 AA.
AC   P53621; Q5T201; Q8IXZ9;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 2.
DT   27-MAR-2024, entry version 231.
DE   RecName: Full=Coatomer subunit alpha;
DE   AltName: Full=Alpha-coat protein;
DE            Short=Alpha-COP;
DE   AltName: Full=HEP-COP;
DE            Short=HEPCOP;
DE   Contains:
DE     RecName: Full=Xenin;
DE     AltName: Full=Xenopsin-related peptide;
DE   Contains:
DE     RecName: Full=Proxenin;
GN   Name=COPA;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=8647451; DOI=10.1016/0378-1119(95)00738-5;
RA   Chow V.T.K., Quek H.H.;
RT   "HEP-COP, a novel human gene whose product is highly homologous to the
RT   alpha-subunit of the yeast coatomer protein complex.";
RL   Gene 169:223-227(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Uterus;
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   [5]
RP   PROTEIN SEQUENCE OF 1-25 (XENIN).
RC   TISSUE=Gastric mucosa;
RX   PubMed=1429581; DOI=10.1016/s0021-9258(18)41670-5;
RA   Feurle G.E., Hamscher G., Kusiek R., Meyer H.E., Metzger J.W.;
RT   "Identification of xenin, a xenopsin-related peptide, in the human gastric
RT   mucosa and its effect on exocrine pancreatic secretion.";
RL   J. Biol. Chem. 267:22305-22309(1992).
RN   [6]
RP   PROTEOLYTIC PROCESSING OF COPA TO PRODUCE XENIN.
RX   PubMed=9365789; DOI=10.1046/j.1469-1809.1997.6140369.x;
RA   Chow V.T.K., Quek H.H.;
RT   "Alpha coat protein COPA (HEP-COP): presence of an Alu repeat in cDNA and
RT   identity of the amino terminus to xenin.";
RL   Ann. Hum. Genet. 61:369-373(1997).
RN   [7]
RP   REVIEW ON XENIN.
RX   PubMed=9533652; DOI=10.1016/s0196-9781(97)00378-1;
RA   Feurle G.E.;
RT   "Xenin -- a review.";
RL   Peptides 19:609-615(1998).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT   networks.";
RL   Cell 127:635-648(2006).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=16964243; DOI=10.1038/nbt1240;
RA   Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT   "A probability-based approach for high-throughput protein phosphorylation
RT   analysis and site localization.";
RL   Nat. Biotechnol. 24:1285-1292(2006).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173 AND SER-895, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT   kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173 AND SER-402, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173 AND THR-185, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [15]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [16]
RP   RNA EDITING OF POSITION 164.
RX   PubMed=21835166; DOI=10.1016/j.bbrc.2011.07.075;
RA   Maas S., Godfried Sie C.P., Stoev I., Dupuis D.E., Latona J., Porman A.M.,
RA   Evans B., Rekawek P., Kluempers V., Mutter M., Gommans W.M., Lopresti D.;
RT   "Genome-wide evaluation and discovery of vertebrate A-to-I RNA editing
RT   sites.";
RL   Biochem. Biophys. Res. Commun. 412:407-412(2011).
RN   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173 AND SER-402, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [18]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [19]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173; THR-591 AND SER-1193,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [20]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-895, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [21]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-965, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Colon carcinoma;
RX   PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA   Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA   Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA   Bedford M.T., Comb M.J.;
RT   "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT   methylation.";
RL   Mol. Cell. Proteomics 13:372-387(2014).
RN   [22]
RP   INTERACTION WITH JAGN1.
RX   PubMed=25129144; DOI=10.1038/ng.3069;
RA   Boztug K., Jaervinen P.M., Salzer E., Racek T., Moench S., Garncarz W.,
RA   Gertz E.M., Schaeffer A.A., Antonopoulos A., Haslam S.M., Schieck L.,
RA   Puchalka J., Diestelhorst J., Appaswamy G., Lescoeur B., Giambruno R.,
RA   Bigenzahn J.W., Elling U., Pfeifer D., Conde C.D., Albert M.H., Welte K.,
RA   Brandes G., Sherkat R., van der Werff Ten Bosch J., Rezaei N., Etzioni A.,
RA   Bellanne-Chantelot C., Superti-Furga G., Penninger J.M., Bennett K.L.,
RA   von Blume J., Dell A., Donadieu J., Klein C.;
RT   "JAGN1 deficiency causes aberrant myeloid cell homeostasis and congenital
RT   neutropenia.";
RL   Nat. Genet. 46:1021-1027(2014).
RN   [23]
RP   INVOLVEMENT IN AILJK, VARIANTS AILJK ASN-230; HIS-233; LYS-241 AND GLY-243,
RP   AND CHARACTERIZATION OF VARIANTS AILJK ASN-230 AND LYS-241.
RX   PubMed=25894502; DOI=10.1038/ng.3279;
RG   Baylor-Hopkins Center for Mendelian Genomics;
RA   Watkin L.B., Jessen B., Wiszniewski W., Vece T.J., Jan M., Sha Y.,
RA   Thamsen M., Santos-Cortez R.L., Lee K., Gambin T., Forbes L.R., Law C.S.,
RA   Stray-Pedersen A., Cheng M.H., Mace E.M., Anderson M.S., Liu D., Tang L.F.,
RA   Nicholas S.K., Nahmod K., Makedonas G., Canter D.L., Kwok P.Y., Hicks J.,
RA   Jones K.D., Penney S., Jhangiani S.N., Rosenblum M.D., Dell S.D.,
RA   Waterfield M.R., Papa F.R., Muzny D.M., Zaitlen N., Leal S.M.,
RA   Gonzaga-Jauregui C., Boerwinkle E., Eissa N.T., Gibbs R.A., Lupski J.R.,
RA   Orange J.S., Shum A.K.;
RT   "COPA mutations impair ER-Golgi transport and cause hereditary autoimmune-
RT   mediated lung disease and arthritis.";
RL   Nat. Genet. 47:654-660(2015).
RN   [24]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [25]
RP   INTERACTION WITH TMEM41B.
RX   PubMed=30352685; DOI=10.1016/j.bbrc.2018.10.073;
RA   Van Alstyne M., Lotti F., Dal Mas A., Area-Gomez E., Pellizzoni L.;
RT   "Stasimon/Tmem41b localizes to mitochondria-associated ER membranes and is
RT   essential for mouse embryonic development.";
RL   Biochem. Biophys. Res. Commun. 506:463-470(2018).
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.
CC   -!- SUBUNIT: Oligomeric complex that consists of at least the alpha, beta,
CC       beta', gamma, delta, epsilon and zeta subunits (By similarity).
CC       Interacts with SCYL1 (By similarity). Interacts with JAGN1
CC       (PubMed:25129144). Interacts with TMEM41B (PubMed:30352685). Interacts
CC       with SVEP1 (By similarity). Probably interacts with PEX11A.
CC       {ECO:0000250, ECO:0000250|UniProtKB:Q8CIE6,
CC       ECO:0000269|PubMed:25129144, ECO:0000269|PubMed:30352685}.
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}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P53621-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P53621-2; Sequence=VSP_035043;
CC   -!- TISSUE SPECIFICITY: Uniformly expressed in a wide range of adult and
CC       fetal tissues. Xenin is found in gastric, duodenal and jejunal mucosa.
CC       Circulates in the blood. Seems to be confined to specific endocrine
CC       cells.
CC   -!- DEVELOPMENTAL STAGE: Xenin is released into the circulation after a
CC       meal.
CC   -!- RNA EDITING: Modified_positions=164 {ECO:0000269|PubMed:21835166};
CC       Note=Edited at about 31%.;
CC   -!- DISEASE: Autoimmune interstitial lung, joint, and kidney disease
CC       (AILJK) [MIM:616414]: An autoimmune disease characterized by
CC       inflammatory arthritis, interstitial lung disease, and immune complex-
CC       mediated renal disease. {ECO:0000269|PubMed:25894502}. Note=The disease
CC       is caused by variants affecting the gene represented in this entry.
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=Xenin entry;
CC       URL="https://en.wikipedia.org/wiki/Xenin";
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DR   EMBL; U24105; AAB70879.1; -; mRNA.
DR   EMBL; AL513282; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL445230; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471121; EAW52723.1; -; Genomic_DNA.
DR   EMBL; CH471121; EAW52725.1; -; Genomic_DNA.
DR   EMBL; BC038447; AAH38447.1; -; mRNA.
DR   CCDS; CCDS1202.1; -. [P53621-1]
DR   CCDS; CCDS41424.1; -. [P53621-2]
DR   PIR; JC4668; ERHUAH.
DR   RefSeq; NP_001091868.1; NM_001098398.1. [P53621-2]
DR   RefSeq; NP_004362.2; NM_004371.3. [P53621-1]
DR   PDB; 6PBG; X-ray; 1.72 A; A=1-320.
DR   PDB; 6TZT; X-ray; 3.06 A; B/D=870-1224.
DR   PDB; 6U3V; X-ray; 2.96 A; B/D=835-1224.
DR   PDBsum; 6PBG; -.
DR   PDBsum; 6TZT; -.
DR   PDBsum; 6U3V; -.
DR   AlphaFoldDB; P53621; -.
DR   SMR; P53621; -.
DR   BioGRID; 107709; 397.
DR   ComplexPortal; CPX-7803; COPI vesicle coat complex, COPG1-COPZ1 variant.
DR   ComplexPortal; CPX-7969; COPI vesicle coat complex, COPG2-COPZ1 variant.
DR   ComplexPortal; CPX-7970; COPI vesicle coat complex, COPG1-COPZ2 variant.
DR   IntAct; P53621; 117.
DR   MINT; P53621; -.
DR   STRING; 9606.ENSP00000357048; -.
DR   GlyCosmos; P53621; 2 sites, 1 glycan.
DR   GlyGen; P53621; 2 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; P53621; -.
DR   MetOSite; P53621; -.
DR   PhosphoSitePlus; P53621; -.
DR   SwissPalm; P53621; -.
DR   BioMuta; COPA; -.
DR   DMDM; 205371746; -.
DR   EPD; P53621; -.
DR   jPOST; P53621; -.
DR   MassIVE; P53621; -.
DR   MaxQB; P53621; -.
DR   PaxDb; 9606-ENSP00000357048; -.
DR   PeptideAtlas; P53621; -.
DR   ProteomicsDB; 56593; -. [P53621-1]
DR   ProteomicsDB; 56594; -. [P53621-2]
DR   Pumba; P53621; -.
DR   Antibodypedia; 34275; 157 antibodies from 26 providers.
DR   DNASU; 1314; -.
DR   Ensembl; ENST00000241704.8; ENSP00000241704.7; ENSG00000122218.17. [P53621-1]
DR   Ensembl; ENST00000368069.7; ENSP00000357048.3; ENSG00000122218.17. [P53621-2]
DR   GeneID; 1314; -.
DR   KEGG; hsa:1314; -.
DR   MANE-Select; ENST00000241704.8; ENSP00000241704.7; NM_004371.4; NP_004362.2.
DR   UCSC; uc001fvv.5; human. [P53621-1]
DR   AGR; HGNC:2230; -.
DR   CTD; 1314; -.
DR   DisGeNET; 1314; -.
DR   GeneCards; COPA; -.
DR   HGNC; HGNC:2230; COPA.
DR   HPA; ENSG00000122218; Low tissue specificity.
DR   MalaCards; COPA; -.
DR   MIM; 601924; gene.
DR   MIM; 616414; phenotype.
DR   neXtProt; NX_P53621; -.
DR   OpenTargets; ENSG00000122218; -.
DR   Orphanet; 444092; Autoimmune interstitial lung disease-arthritis syndrome.
DR   PharmGKB; PA26746; -.
DR   VEuPathDB; HostDB:ENSG00000122218; -.
DR   eggNOG; KOG0292; Eukaryota.
DR   GeneTree; ENSGT00940000155451; -.
DR   HOGENOM; CLU_007565_1_0_1; -.
DR   InParanoid; P53621; -.
DR   OMA; EMTYQKQ; -.
DR   OrthoDB; 20819at2759; -.
DR   PhylomeDB; P53621; -.
DR   TreeFam; TF105693; -.
DR   PathwayCommons; P53621; -.
DR   Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
DR   Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR   SignaLink; P53621; -.
DR   BioGRID-ORCS; 1314; 839 hits in 1126 CRISPR screens.
DR   ChiTaRS; COPA; human.
DR   GeneWiki; COPA_(gene); -.
DR   GenomeRNAi; 1314; -.
DR   Pharos; P53621; Tbio.
DR   PRO; PR:P53621; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; P53621; Protein.
DR   Bgee; ENSG00000122218; Expressed in stromal cell of endometrium and 212 other cell types or tissues.
DR   ExpressionAtlas; P53621; baseline and differential.
DR   GO; GO:0030126; C:COPI vesicle coat; IDA:MGI.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IDA:MGI.
DR   GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR   GO; GO:0030426; C:growth cone; IDA:MGI.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0030133; C:transport vesicle; TAS:Reactome.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
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; IDA: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; P53621; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cytoplasm; Cytoplasmic vesicle;
KW   Direct protein sequencing; Disease variant; ER-Golgi transport;
KW   Golgi apparatus; Hormone; Membrane; Methylation; Phosphoprotein;
KW   Protein transport; Reference proteome; Repeat; RNA editing; Secreted;
KW   Transport; WD repeat.
FT   CHAIN           1..1224
FT                   /note="Coatomer subunit alpha"
FT                   /id="PRO_0000223307"
FT   PEPTIDE         1..35
FT                   /note="Proxenin"
FT                   /id="PRO_0000041400"
FT   PEPTIDE         1..25
FT                   /note="Xenin"
FT                   /id="PRO_0000041401"
FT   REPEAT          3..38
FT                   /note="WD 1"
FT   REPEAT          42..80
FT                   /note="WD 2"
FT   REPEAT          84..122
FT                   /note="WD 3"
FT   REPEAT          126..164
FT                   /note="WD 4"
FT   REPEAT          195..234
FT                   /note="WD 5"
FT   REPEAT          241..278
FT                   /note="WD 6"
FT   REPEAT          282..319
FT                   /note="WD 7"
FT   MOD_RES         173
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:16964243,
FT                   ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         185
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   MOD_RES         402
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:21406692"
FT   MOD_RES         591
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         895
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18691976,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         965
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         1193
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         509
FT                   /note="H -> HEHSCPLPLT (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_035043"
FT   VARIANT         164
FT                   /note="I -> V (in RNA edited version)"
FT                   /id="VAR_066525"
FT   VARIANT         230
FT                   /note="K -> N (in AILJK; causes a defect in retrograde
FT                   transport from the Golgi to the endoplasmic reticulum;
FT                   dbSNP:rs864309710)"
FT                   /evidence="ECO:0000269|PubMed:25894502"
FT                   /id="VAR_073844"
FT   VARIANT         233
FT                   /note="R -> H (in AILJK; dbSNP:rs794727993)"
FT                   /evidence="ECO:0000269|PubMed:25894502"
FT                   /id="VAR_073845"
FT   VARIANT         241
FT                   /note="E -> K (in AILJK; causes a defect in retrograde
FT                   transport from the Golgi to the endoplasmic reticulum;
FT                   dbSNP:rs794727995)"
FT                   /evidence="ECO:0000269|PubMed:25894502"
FT                   /id="VAR_073846"
FT   VARIANT         243
FT                   /note="D -> G (in AILJK; dbSNP:rs794727994)"
FT                   /evidence="ECO:0000269|PubMed:25894502"
FT                   /id="VAR_073847"
FT   VARIANT         1040
FT                   /note="V -> G (in dbSNP:rs34997807)"
FT                   /id="VAR_033803"
FT   CONFLICT        703
FT                   /note="L -> V (in Ref. 1; AAB70879)"
FT                   /evidence="ECO:0000305"
FT   STRAND          1..6
FT                   /evidence="ECO:0007829|PDB:6PBG"
FT   STRAND          12..17
FT                   /evidence="ECO:0007829|PDB:6PBG"
FT   STRAND          19..28
FT                   /evidence="ECO:0007829|PDB:6PBG"
FT   STRAND          33..37
FT                   /evidence="ECO:0007829|PDB:6PBG"
FT   TURN            38..41
FT                   /evidence="ECO:0007829|PDB:6PBG"
FT   STRAND          42..47
FT                   /evidence="ECO:0007829|PDB:6PBG"
FT   STRAND          50..52
FT                   /evidence="ECO:0007829|PDB:6PBG"
FT   STRAND          54..59
FT                   /evidence="ECO:0007829|PDB:6PBG"
FT   STRAND          61..70
FT                   /evidence="ECO:0007829|PDB:6PBG"
FT   STRAND          75..79
FT                   /evidence="ECO:0007829|PDB:6PBG"
FT   TURN            80..83
FT                   /evidence="ECO:0007829|PDB:6PBG"
FT   STRAND          84..89
FT                   /evidence="ECO:0007829|PDB:6PBG"
FT   STRAND          96..101
FT                   /evidence="ECO:0007829|PDB:6PBG"
FT   STRAND          103..112
FT                   /evidence="ECO:0007829|PDB:6PBG"
FT   STRAND          117..121
FT                   /evidence="ECO:0007829|PDB:6PBG"
FT   TURN            122..125
FT                   /evidence="ECO:0007829|PDB:6PBG"
FT   STRAND          126..131
FT                   /evidence="ECO:0007829|PDB:6PBG"
FT   STRAND          138..143
FT                   /evidence="ECO:0007829|PDB:6PBG"
FT   STRAND          145..154
FT                   /evidence="ECO:0007829|PDB:6PBG"
FT   STRAND          159..163
FT                   /evidence="ECO:0007829|PDB:6PBG"
FT   HELIX           165..172
FT                   /evidence="ECO:0007829|PDB:6PBG"
FT   STRAND          195..201
FT                   /evidence="ECO:0007829|PDB:6PBG"
FT   STRAND          208..213
FT                   /evidence="ECO:0007829|PDB:6PBG"
FT   STRAND          215..224
FT                   /evidence="ECO:0007829|PDB:6PBG"
FT   STRAND          229..234
FT                   /evidence="ECO:0007829|PDB:6PBG"
FT   STRAND          239..245
FT                   /evidence="ECO:0007829|PDB:6PBG"
FT   STRAND          252..257
FT                   /evidence="ECO:0007829|PDB:6PBG"
FT   STRAND          259..268
FT                   /evidence="ECO:0007829|PDB:6PBG"
FT   STRAND          271..277
FT                   /evidence="ECO:0007829|PDB:6PBG"
FT   STRAND          285..288
FT                   /evidence="ECO:0007829|PDB:6PBG"
FT   STRAND          294..299
FT                   /evidence="ECO:0007829|PDB:6PBG"
FT   STRAND          301..304
FT                   /evidence="ECO:0007829|PDB:6PBG"
FT   STRAND          306..310
FT                   /evidence="ECO:0007829|PDB:6PBG"
FT   STRAND          313..319
FT                   /evidence="ECO:0007829|PDB:6PBG"
FT   HELIX           916..923
FT                   /evidence="ECO:0007829|PDB:6U3V"
FT   HELIX           927..932
FT                   /evidence="ECO:0007829|PDB:6U3V"
FT   HELIX           936..947
FT                   /evidence="ECO:0007829|PDB:6U3V"
FT   HELIX           953..955
FT                   /evidence="ECO:0007829|PDB:6U3V"
FT   HELIX           956..964
FT                   /evidence="ECO:0007829|PDB:6U3V"
FT   STRAND          968..970
FT                   /evidence="ECO:0007829|PDB:6U3V"
FT   STRAND          979..981
FT                   /evidence="ECO:0007829|PDB:6U3V"
FT   HELIX           987..989
FT                   /evidence="ECO:0007829|PDB:6U3V"
FT   TURN            991..993
FT                   /evidence="ECO:0007829|PDB:6U3V"
FT   HELIX           1003..1019
FT                   /evidence="ECO:0007829|PDB:6U3V"
FT   HELIX           1022..1035
FT                   /evidence="ECO:0007829|PDB:6U3V"
FT   HELIX           1036..1038
FT                   /evidence="ECO:0007829|PDB:6U3V"
FT   HELIX           1044..1072
FT                   /evidence="ECO:0007829|PDB:6U3V"
FT   HELIX           1078..1091
FT                   /evidence="ECO:0007829|PDB:6U3V"
FT   HELIX           1098..1115
FT                   /evidence="ECO:0007829|PDB:6U3V"
FT   HELIX           1118..1130
FT                   /evidence="ECO:0007829|PDB:6U3V"
FT   HELIX           1135..1149
FT                   /evidence="ECO:0007829|PDB:6U3V"
FT   STRAND          1154..1156
FT                   /evidence="ECO:0007829|PDB:6U3V"
FT   STRAND          1166..1168
FT                   /evidence="ECO:0007829|PDB:6U3V"
FT   TURN            1170..1172
FT                   /evidence="ECO:0007829|PDB:6U3V"
FT   STRAND          1175..1177
FT                   /evidence="ECO:0007829|PDB:6U3V"
FT   TURN            1186..1188
FT                   /evidence="ECO:0007829|PDB:6U3V"
FT   HELIX           1194..1196
FT                   /evidence="ECO:0007829|PDB:6U3V"
FT   TURN            1202..1204
FT                   /evidence="ECO:0007829|PDB:6U3V"
FT   STRAND          1205..1208
FT                   /evidence="ECO:0007829|PDB:6U3V"
FT   HELIX           1220..1222
FT                   /evidence="ECO:0007829|PDB:6U3V"
SQ   SEQUENCE   1224 AA;  138346 MW;  5A8BC35CE78F155D CRC64;
     MLTKFETKSA RVKGLSFHPK RPWILTSLHN GVIQLWDYRM CTLIDKFDEH DGPVRGIDFH
     KQQPLFVSGG DDYKIKVWNY KLRRCLFTLL GHLDYIRTTF FHHEYPWILS ASDDQTIRVW
     NWQSRTCVCV LTGHNHYVMC AQFHPTEDLV 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 KNEITKKVQV 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 TAATHGLDEE AESLKETFDP
     EKETIPDIDP NAKLLQPPAP IMPLDTNWPL LTVSKGFFEG TIASKGKGGA LAADIDIDTV
     GTEGWGEDAE LQLDEDGFVE ATEGLGDDAL GKGQEEGGGW DVEEDLELPP ELDISPGAAG
     GAEDGFFVPP TKGTSPTQIW CNNSQLPVDH ILAGSFETAM RLLHDQVGVI QFGPYKQLFL
     QTYARGRTTY QALPCLPSMY GYPNRNWKDA GLKNGVPAVG LKLNDLIQRL QLCYQLTTVG
     KFEEAVEKFR SILLSVPLLV VDNKQEIAEA QQLITICREY IVGLSVETER KKLPKETLEQ
     QKRICEMAAY FTHSNLQPVH MILVLRTALN LFFKLKNFKT AATFARRLLE LGPKPEVAQQ
     TRKILSACEK NPTDAYQLNY DMHNPFDICA ASYRPIYRGK PVEKCPLSGA CYSPEFKGQI
     CRVTTVTEIG KDVIGLRISP LQFR
//