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Coatomer subunit alpha (Alpha-coat protein) (Alpha-COP) (HEP-COP) (HEPCOP) [Cleaved into: Xenin (Xenopsin-related peptide); Proxenin]

 COPA_HUMAN              Reviewed;        1224 AA.
P53621; Q5T201; Q8IXZ9;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
02-SEP-2008, sequence version 2.
20-JUN-2018, entry version 194.
RecName: Full=Coatomer subunit alpha;
AltName: Full=Alpha-coat protein;
Short=Alpha-COP;
AltName: Full=HEP-COP;
Short=HEPCOP;
Contains:
RecName: Full=Xenin;
AltName: Full=Xenopsin-related peptide;
Contains:
RecName: Full=Proxenin;
Name=COPA;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=8647451; DOI=10.1016/0378-1119(95)00738-5;
Chow V.T.K., Quek H.H.;
"HEP-COP, a novel human gene whose product is highly homologous to the
alpha-subunit of the yeast coatomer protein complex.";
Gene 169:223-227(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PROTEIN SEQUENCE OF 1-25 (XENIN).
TISSUE=Gastric mucosa;
PubMed=1429581;
Feurle G.E., Hamscher G., Kusiek R., Meyer H.E., Metzger J.W.;
"Identification of xenin, a xenopsin-related peptide, in the human
gastric mucosa and its effect on exocrine pancreatic secretion.";
J. Biol. Chem. 267:22305-22309(1992).
[6]
PROTEOLYTIC PROCESSING OF COPA TO PRODUCE XENIN.
PubMed=9365789; DOI=10.1017/S0003480097006295;
Chow V.T.K., Quek H.H.;
"Alpha coat protein COPA (HEP-COP): presence of an Alu repeat in cDNA
and identity of the amino terminus to xenin.";
Ann. Hum. Genet. 61:369-373(1997).
[7]
REVIEW ON XENIN.
PubMed=9533652; DOI=10.1016/S0196-9781(97)00378-1;
Feurle G.E.;
"Xenin -- a review.";
Peptides 19:609-615(1998).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173 AND SER-895, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173 AND SER-402, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173 AND THR-185, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[16]
RNA EDITING OF POSITION 164.
PubMed=21835166; DOI=10.1016/j.bbrc.2011.07.075;
Maas S., Godfried Sie C.P., Stoev I., Dupuis D.E., Latona J.,
Porman A.M., Evans B., Rekawek P., Kluempers V., Mutter M.,
Gommans W.M., Lopresti D.;
"Genome-wide evaluation and discovery of vertebrate A-to-I RNA editing
sites.";
Biochem. Biophys. Res. Commun. 412:407-412(2011).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173 AND SER-402, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173; THR-591 AND
SER-1193, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-895, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[21]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-965, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[22]
INTERACTION WITH JAGN1.
PubMed=25129144; DOI=10.1038/ng.3069;
Boztug K., Jaervinen P.M., Salzer E., Racek T., Moench S.,
Garncarz W., Gertz E.M., Schaeffer A.A., Antonopoulos A., Haslam S.M.,
Schieck L., Puchalka J., Diestelhorst J., Appaswamy G., Lescoeur B.,
Giambruno R., Bigenzahn J.W., Elling U., Pfeifer D., Conde C.D.,
Albert M.H., Welte K., Brandes G., Sherkat R.,
van der Werff Ten Bosch J., Rezaei N., Etzioni A.,
Bellanne-Chantelot C., Superti-Furga G., Penninger J.M., Bennett K.L.,
von Blume J., Dell A., Donadieu J., Klein C.;
"JAGN1 deficiency causes aberrant myeloid cell homeostasis and
congenital neutropenia.";
Nat. Genet. 46:1021-1027(2014).
[23]
INVOLVEMENT IN AILJK, VARIANTS AILJK ASN-230; HIS-233; LYS-241 AND
GLY-243, AND CHARACTERIZATION OF VARIANTS AILJK ASN-230 AND LYS-241.
PubMed=25894502; DOI=10.1038/ng.3279;
Baylor-Hopkins Center for Mendelian Genomics;
Watkin L.B., Jessen B., Wiszniewski W., Vece T.J., Jan M., Sha Y.,
Thamsen M., Santos-Cortez R.L., Lee K., Gambin T., Forbes L.R.,
Law C.S., Stray-Pedersen A., Cheng M.H., Mace E.M., Anderson M.S.,
Liu D., Tang L.F., Nicholas S.K., Nahmod K., Makedonas G.,
Canter D.L., Kwok P.Y., Hicks J., Jones K.D., Penney S.,
Jhangiani S.N., Rosenblum M.D., Dell S.D., Waterfield M.R., Papa F.R.,
Muzny D.M., Zaitlen N., Leal S.M., Gonzaga-Jauregui C., Boerwinkle E.,
Eissa N.T., Gibbs R.A., Lupski J.R., Orange J.S., Shum A.K.;
"COPA mutations impair ER-Golgi transport and cause hereditary
autoimmune-mediated lung disease and arthritis.";
Nat. Genet. 47:654-660(2015).
[24]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
-!- FUNCTION: The coatomer is a cytosolic protein complex that binds
to dilysine motifs and reversibly associates with Golgi non-
clathrin-coated vesicles, which further mediate biosynthetic
protein transport from the ER, via the Golgi up to the trans Golgi
network. Coatomer complex is required for budding from Golgi
membranes, and is essential for the retrograde Golgi-to-ER
transport of dilysine-tagged proteins. In mammals, the coatomer
can only be recruited by membranes associated to ADP-ribosylation
factors (ARFs), which are small GTP-binding proteins; the complex
also influences the Golgi structural integrity, as well as the
processing, activity, and endocytic recycling of LDL receptors (By
similarity). {ECO:0000250}.
-!- FUNCTION: Xenin stimulates exocrine pancreatic secretion. It
inhibits pentagastrin-stimulated secretion of acid, to induce
exocrine pancreatic secretion and to affect small and large
intestinal motility. In the gut, xenin interacts with the
neurotensin receptor.
-!- SUBUNIT: Oligomeric complex that consists of at least the alpha,
beta, beta', gamma, delta, epsilon and zeta subunits. Probably
interacts with PEX11A. Interacts with SCYL1 (By similarity).
Interacts with JAGN1. {ECO:0000250, ECO:0000269|PubMed:25129144}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus
membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250};
Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle, COPI-coated
vesicle membrane {ECO:0000250}; Peripheral membrane protein
{ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=The coatomer
is cytoplasmic or polymerized on the cytoplasmic side of the
Golgi, as well as on the vesicles/buds originating from it.
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Xenin: Secreted {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P53621-1; Sequence=Displayed;
Name=2;
IsoId=P53621-2; Sequence=VSP_035043;
-!- TISSUE SPECIFICITY: Uniformly expressed in a wide range of adult
and fetal tissues. Xenin is found in gastric, duodenal and jejunal
mucosa. Circulates in the blood. Seems to be confined to specific
endocrine cells.
-!- DEVELOPMENTAL STAGE: Xenin is released into the circulation after
a meal.
-!- RNA EDITING: Modified_positions=164 {ECO:0000269|PubMed:21835166};
Note=Edited at about 31%.;
-!- DISEASE: Autoimmune interstitial lung, joint, and kidney disease
(AILJK) [MIM:616414]: An autoimmune disease characterized by
inflammatory arthritis, interstitial lung disease, and immune
complex-mediated renal disease. {ECO:0000269|PubMed:25894502}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- WEB RESOURCE: Name=Wikipedia; Note=Xenin entry;
URL="https://en.wikipedia.org/wiki/Xenin";
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EMBL; U24105; AAB70879.1; -; mRNA.
EMBL; AL513282; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL445230; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471121; EAW52723.1; -; Genomic_DNA.
EMBL; CH471121; EAW52725.1; -; Genomic_DNA.
EMBL; BC038447; AAH38447.1; -; mRNA.
CCDS; CCDS1202.1; -. [P53621-1]
CCDS; CCDS41424.1; -. [P53621-2]
PIR; JC4668; ERHUAH.
RefSeq; NP_001091868.1; NM_001098398.1. [P53621-2]
RefSeq; NP_004362.2; NM_004371.3. [P53621-1]
UniGene; Hs.162121; -.
UniGene; Hs.685025; -.
ProteinModelPortal; P53621; -.
SMR; P53621; -.
BioGrid; 107709; 101.
IntAct; P53621; 65.
MINT; P53621; -.
STRING; 9606.ENSP00000357048; -.
iPTMnet; P53621; -.
PhosphoSitePlus; P53621; -.
SwissPalm; P53621; -.
BioMuta; COPA; -.
DMDM; 205371746; -.
EPD; P53621; -.
MaxQB; P53621; -.
PaxDb; P53621; -.
PeptideAtlas; P53621; -.
PRIDE; P53621; -.
ProteomicsDB; 56593; -.
ProteomicsDB; 56594; -. [P53621-2]
Ensembl; ENST00000241704; ENSP00000241704; ENSG00000122218. [P53621-1]
Ensembl; ENST00000368069; ENSP00000357048; ENSG00000122218. [P53621-2]
GeneID; 1314; -.
KEGG; hsa:1314; -.
UCSC; uc001fvv.5; human. [P53621-1]
CTD; 1314; -.
DisGeNET; 1314; -.
EuPathDB; HostDB:ENSG00000122218.14; -.
GeneCards; COPA; -.
HGNC; HGNC:2230; COPA.
HPA; HPA028024; -.
MalaCards; COPA; -.
MIM; 601924; gene.
MIM; 616414; phenotype.
neXtProt; NX_P53621; -.
OpenTargets; ENSG00000122218; -.
PharmGKB; PA26746; -.
eggNOG; KOG0292; Eukaryota.
eggNOG; ENOG410XPZS; LUCA.
GeneTree; ENSGT00920000149070; -.
HOGENOM; HOG000195913; -.
HOVERGEN; HBG005379; -.
InParanoid; P53621; -.
KO; K05236; -.
OMA; GHDNGVM; -.
OrthoDB; EOG091G00SH; -.
PhylomeDB; P53621; -.
TreeFam; TF105693; -.
Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
SignaLink; P53621; -.
ChiTaRS; COPA; human.
GeneWiki; COPA_(gene); -.
GenomeRNAi; 1314; -.
PRO; PR:P53621; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000122218; -.
CleanEx; HS_COPA; -.
Genevisible; P53621; HS.
GO; GO:0030126; C:COPI vesicle coat; IDA:MGI.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:MGI.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0030133; C:transport vesicle; TAS:Reactome.
GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; IBA:GO_Central.
GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IBA:GO_Central.
GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
GO; GO:0030157; P:pancreatic juice secretion; IDA:MGI.
GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to ER; IBA:GO_Central.
Gene3D; 2.130.10.10; -; 1.
InterPro; IPR024977; Apc4_WD40_dom.
InterPro; IPR016391; Coatomer_asu.
InterPro; IPR010714; Coatomer_asu_C.
InterPro; IPR006692; Coatomer_WD-assoc_reg.
InterPro; IPR020472; G-protein_beta_WD-40_rep.
InterPro; IPR011048; Haem_d1_sf.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR019775; WD40_repeat_CS.
InterPro; IPR017986; WD40_repeat_dom.
InterPro; IPR036322; WD40_repeat_dom_sf.
Pfam; PF12894; ANAPC4_WD40; 1.
Pfam; PF04053; Coatomer_WDAD; 1.
Pfam; PF06957; COPI_C; 1.
Pfam; PF00400; WD40; 3.
PIRSF; PIRSF003354; Coatomer_alpha_subunit; 1.
PRINTS; PR00320; GPROTEINBRPT.
SMART; SM00320; WD40; 7.
SUPFAM; SSF50978; SSF50978; 2.
SUPFAM; SSF51004; SSF51004; 3.
PROSITE; PS00678; WD_REPEATS_1; 1.
PROSITE; PS50082; WD_REPEATS_2; 6.
PROSITE; PS50294; WD_REPEATS_REGION; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Cytoplasm;
Cytoplasmic vesicle; Direct protein sequencing; Disease mutation;
ER-Golgi transport; Golgi apparatus; Hormone; Membrane; Methylation;
Phosphoprotein; Polymorphism; Protein transport; Reference proteome;
Repeat; RNA editing; Secreted; Transport; WD repeat.
CHAIN 1 1224 Coatomer subunit alpha.
/FTId=PRO_0000223307.
PEPTIDE 1 35 Proxenin.
/FTId=PRO_0000041400.
PEPTIDE 1 25 Xenin.
/FTId=PRO_0000041401.
REPEAT 3 38 WD 1.
REPEAT 42 80 WD 2.
REPEAT 84 122 WD 3.
REPEAT 126 164 WD 4.
REPEAT 195 234 WD 5.
REPEAT 241 278 WD 6.
REPEAT 282 319 WD 7.
MOD_RES 173 173 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 185 185 Phosphothreonine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 402 402 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692}.
MOD_RES 591 591 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 895 895 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:24275569}.
MOD_RES 965 965 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 1193 1193 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 509 509 H -> HEHSCPLPLT (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_035043.
VARIANT 164 164 I -> V (in RNA edited version).
/FTId=VAR_066525.
VARIANT 230 230 K -> N (in AILJK; causes a defect in
retrograde transport from the Golgi to
the endoplasmic reticulum;
dbSNP:rs864309710).
{ECO:0000269|PubMed:25894502}.
/FTId=VAR_073844.
VARIANT 233 233 R -> H (in AILJK; dbSNP:rs794727993).
{ECO:0000269|PubMed:25894502}.
/FTId=VAR_073845.
VARIANT 241 241 E -> K (in AILJK; causes a defect in
retrograde transport from the Golgi to
the endoplasmic reticulum;
dbSNP:rs794727995).
{ECO:0000269|PubMed:25894502}.
/FTId=VAR_073846.
VARIANT 243 243 D -> G (in AILJK; dbSNP:rs794727994).
{ECO:0000269|PubMed:25894502}.
/FTId=VAR_073847.
VARIANT 1040 1040 V -> G (in dbSNP:rs34997807).
/FTId=VAR_033803.
CONFLICT 703 703 L -> V (in Ref. 1; AAB70879).
{ECO:0000305}.
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


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