COPA_HUMAN
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 03-AUG-2022, entry version 222.
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 Probably interacts with PEX11A (By similarity). Interacts with SCYL1
CC (By similarity). Interacts with JAGN1 (PubMed:25129144). Interacts with
CC TMEM41B (PubMed:30352685). {ECO:0000250, ECO:0000269|PubMed:25129144,
CC 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; 261.
DR IntAct; P53621; 104.
DR MINT; P53621; -.
DR STRING; 9606.ENSP00000357048; -.
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; P53621; -.
DR PeptideAtlas; P53621; -.
DR PRIDE; P53621; -.
DR ProteomicsDB; 56593; -. [P53621-1]
DR ProteomicsDB; 56594; -. [P53621-2]
DR Antibodypedia; 34275; 138 antibodies from 25 providers.
DR DNASU; 1314; -.
DR Ensembl; ENST00000241704.8; ENSP00000241704.7; ENSG00000122218.16. [P53621-1]
DR Ensembl; ENST00000368069.7; ENSP00000357048.3; ENSG00000122218.16. [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 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; ICAEYIV; -.
DR OrthoDB; 139008at2759; -.
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; 806 hits in 1050 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 210 other tissues.
DR ExpressionAtlas; P53621; baseline and differential.
DR Genevisible; P53621; HS.
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 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; 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
