Full text data of COPA
COPA
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Coatomer subunit alpha (Alpha-coat protein; Alpha-COP; HEP-COP; HEPCOP; Xenin; Xenopsin-related peptide; Proxenin)
Coatomer subunit alpha (Alpha-coat protein; Alpha-COP; HEP-COP; HEPCOP; Xenin; Xenopsin-related peptide; Proxenin)
UniProt
P53621
ID COPA_HUMAN Reviewed; 1224 AA.
AC P53621; Q5T201; Q8IXZ9;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 02-SEP-2008, sequence version 2.
DT 22-JAN-2014, entry version 144.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA 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.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA 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.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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;
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
RT gastric 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=10.1017/S0003480097006295;
RA Chow V.T.K., Quek H.H.;
RT "Alpha coat protein COPA (HEP-COP): presence of an Alu repeat in cDNA
RT and 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 MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, AND MASS
RP SPECTROMETRY.
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
RT phosphorylation 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 MASS SPECTROMETRY.
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
RT the 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 MASS SPECTROMETRY.
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, AND MASS
RP SPECTROMETRY.
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 MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., 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.,
RA Porman A.M., Evans B., Rekawek P., Kluempers V., Mutter M.,
RA 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 MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome 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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: The coatomer is a cytosolic protein complex that binds
CC to dilysine motifs and reversibly associates with Golgi non-
CC clathrin-coated vesicles, which further mediate biosynthetic
CC protein transport from the ER, via the Golgi up to the trans Golgi
CC network. Coatomer complex is required for budding from Golgi
CC membranes, and is essential for the retrograde Golgi-to-ER
CC transport of dilysine-tagged proteins. In mammals, the coatomer
CC can only be recruited by membranes associated to ADP-ribosylation
CC factors (ARFs), which are small GTP-binding proteins; the complex
CC also influences the Golgi structural integrity, as well as the
CC processing, activity, and endocytic recycling of LDL receptors (By
CC similarity).
CC -!- FUNCTION: Xenin stimulates exocrine pancreatic secretion. It
CC inhibits pentagastrin-stimulated secretion of acid, to induce
CC exocrine pancreatic secretion and to affect small and large
CC intestinal motility. In the gut, xenin interacts with the
CC neurotensin receptor.
CC -!- SUBUNIT: Oligomeric complex that consists of at least the alpha,
CC beta, beta', gamma, delta, epsilon and zeta subunits. Probably
CC interacts with PEX11A. Interacts with SCYL1 (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Golgi apparatus
CC membrane; Peripheral membrane protein; Cytoplasmic side (By
CC similarity). Cytoplasmic vesicle, COPI-coated vesicle membrane;
CC Peripheral membrane protein; Cytoplasmic side (By similarity).
CC Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic
CC side of the Golgi, as well as on the vesicles/buds originating
CC from it (By similarity).
CC -!- SUBCELLULAR LOCATION: Xenin: Secreted (By similarity).
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
CC and fetal tissues. Xenin is found in gastric, duodenal and jejunal
CC mucosa. Circulates in the blood. Seems to be confined to specific
CC endocrine cells.
CC -!- DEVELOPMENTAL STAGE: Xenin is released into the circulation after
CC a meal.
CC -!- RNA EDITING: Modified_positions=164; Note=Edited at about 31%.
CC -!- SIMILARITY: Contains 6 WD repeats.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Xenin entry;
CC URL="http://en.wikipedia.org/wiki/Xenin";
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DR EMBL; U24105; AAB70879.1; -; mRNA.
DR EMBL; AL513282; CAI12454.1; -; Genomic_DNA.
DR EMBL; AL445230; CAI12454.1; JOINED; Genomic_DNA.
DR EMBL; AL513282; CAI12455.1; -; Genomic_DNA.
DR EMBL; AL445230; CAI12455.1; JOINED; Genomic_DNA.
DR EMBL; AL445230; CAI15004.1; -; Genomic_DNA.
DR EMBL; AL513282; CAI15004.1; JOINED; Genomic_DNA.
DR EMBL; AL445230; CAI15005.1; -; Genomic_DNA.
DR EMBL; AL513282; CAI15005.1; JOINED; Genomic_DNA.
DR EMBL; CH471121; EAW52723.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW52725.1; -; Genomic_DNA.
DR EMBL; BC038447; AAH38447.1; -; mRNA.
DR PIR; JC4668; ERHUAH.
DR RefSeq; NP_001091868.1; NM_001098398.1.
DR RefSeq; NP_004362.2; NM_004371.3.
DR UniGene; Hs.162121; -.
DR UniGene; Hs.685025; -.
DR ProteinModelPortal; P53621; -.
DR SMR; P53621; 1-810, 905-1224.
DR IntAct; P53621; 22.
DR MINT; MINT-1144184; -.
DR STRING; 9606.ENSP00000357048; -.
DR PhosphoSite; P53621; -.
DR DMDM; 205371746; -.
DR PaxDb; P53621; -.
DR PRIDE; P53621; -.
DR Ensembl; ENST00000241704; ENSP00000241704; ENSG00000122218.
DR Ensembl; ENST00000368069; ENSP00000357048; ENSG00000122218.
DR GeneID; 1314; -.
DR KEGG; hsa:1314; -.
DR UCSC; uc009wti.3; human.
DR CTD; 1314; -.
DR GeneCards; GC01M160258; -.
DR HGNC; HGNC:2230; COPA.
DR HPA; HPA028024; -.
DR MIM; 601924; gene.
DR neXtProt; NX_P53621; -.
DR PharmGKB; PA26746; -.
DR eggNOG; COG2319; -.
DR HOGENOM; HOG000195913; -.
DR HOVERGEN; HBG005379; -.
DR KO; K05236; -.
DR OMA; FWVLGAH; -.
DR OrthoDB; EOG78WKQX; -.
DR PhylomeDB; P53621; -.
DR Reactome; REACT_11123; Membrane Trafficking.
DR SignaLink; P53621; -.
DR ChiTaRS; COPA; human.
DR GeneWiki; COPA_(gene); -.
DR GenomeRNAi; 1314; -.
DR NextBio; 5373; -.
DR PRO; PR:P53621; -.
DR Bgee; P53621; -.
DR CleanEx; HS_COPA; -.
DR Genevestigator; P53621; -.
DR GO; GO:0030126; C:COPI vesicle coat; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0048205; P:COPI coating of Golgi vesicle; TAS:Reactome.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0030157; P:pancreatic juice secretion; IDA:MGI.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to ER; TAS:Reactome.
DR Gene3D; 2.130.10.10; -; 1.
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.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR017986; WD40_repeat_dom.
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; SSF50978; SSF50978; 2.
DR SUPFAM; SSF51004; SSF51004; 3.
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 Alternative splicing; Complete proteome; Cytoplasm;
KW Cytoplasmic vesicle; Direct protein sequencing; ER-Golgi transport;
KW Golgi apparatus; Hormone; Membrane; Phosphoprotein; Polymorphism;
KW Protein transport; Reference proteome; Repeat; RNA editing; Secreted;
KW Transport; WD repeat.
FT CHAIN 1 1224 Coatomer subunit alpha.
FT /FTId=PRO_0000223307.
FT PEPTIDE 1 35 Proxenin.
FT /FTId=PRO_0000041400.
FT PEPTIDE 1 25 Xenin.
FT /FTId=PRO_0000041401.
FT REPEAT 7 37 WD 1.
FT REPEAT 49 79 WD 2.
FT REPEAT 91 121 WD 3.
FT REPEAT 133 163 WD 4.
FT REPEAT 203 233 WD 5.
FT REPEAT 247 277 WD 6.
FT MOD_RES 173 173 Phosphoserine.
FT MOD_RES 185 185 Phosphothreonine.
FT MOD_RES 402 402 Phosphoserine.
FT MOD_RES 895 895 Phosphoserine.
FT VAR_SEQ 509 509 H -> HEHSCPLPLT (in isoform 2).
FT /FTId=VSP_035043.
FT VARIANT 164 164 I -> V (in RNA edited version).
FT /FTId=VAR_066525.
FT VARIANT 1040 1040 V -> G (in dbSNP:rs34997807).
FT /FTId=VAR_033803.
FT CONFLICT 703 703 L -> V (in Ref. 1; AAB70879).
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
//
ID COPA_HUMAN Reviewed; 1224 AA.
AC P53621; Q5T201; Q8IXZ9;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 02-SEP-2008, sequence version 2.
DT 22-JAN-2014, entry version 144.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA 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.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA 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.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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;
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
RT gastric 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=10.1017/S0003480097006295;
RA Chow V.T.K., Quek H.H.;
RT "Alpha coat protein COPA (HEP-COP): presence of an Alu repeat in cDNA
RT and 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 MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, AND MASS
RP SPECTROMETRY.
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
RT phosphorylation 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 MASS SPECTROMETRY.
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
RT the 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 MASS SPECTROMETRY.
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, AND MASS
RP SPECTROMETRY.
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 MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., 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.,
RA Porman A.M., Evans B., Rekawek P., Kluempers V., Mutter M.,
RA 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 MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome 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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: The coatomer is a cytosolic protein complex that binds
CC to dilysine motifs and reversibly associates with Golgi non-
CC clathrin-coated vesicles, which further mediate biosynthetic
CC protein transport from the ER, via the Golgi up to the trans Golgi
CC network. Coatomer complex is required for budding from Golgi
CC membranes, and is essential for the retrograde Golgi-to-ER
CC transport of dilysine-tagged proteins. In mammals, the coatomer
CC can only be recruited by membranes associated to ADP-ribosylation
CC factors (ARFs), which are small GTP-binding proteins; the complex
CC also influences the Golgi structural integrity, as well as the
CC processing, activity, and endocytic recycling of LDL receptors (By
CC similarity).
CC -!- FUNCTION: Xenin stimulates exocrine pancreatic secretion. It
CC inhibits pentagastrin-stimulated secretion of acid, to induce
CC exocrine pancreatic secretion and to affect small and large
CC intestinal motility. In the gut, xenin interacts with the
CC neurotensin receptor.
CC -!- SUBUNIT: Oligomeric complex that consists of at least the alpha,
CC beta, beta', gamma, delta, epsilon and zeta subunits. Probably
CC interacts with PEX11A. Interacts with SCYL1 (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Golgi apparatus
CC membrane; Peripheral membrane protein; Cytoplasmic side (By
CC similarity). Cytoplasmic vesicle, COPI-coated vesicle membrane;
CC Peripheral membrane protein; Cytoplasmic side (By similarity).
CC Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic
CC side of the Golgi, as well as on the vesicles/buds originating
CC from it (By similarity).
CC -!- SUBCELLULAR LOCATION: Xenin: Secreted (By similarity).
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
CC and fetal tissues. Xenin is found in gastric, duodenal and jejunal
CC mucosa. Circulates in the blood. Seems to be confined to specific
CC endocrine cells.
CC -!- DEVELOPMENTAL STAGE: Xenin is released into the circulation after
CC a meal.
CC -!- RNA EDITING: Modified_positions=164; Note=Edited at about 31%.
CC -!- SIMILARITY: Contains 6 WD repeats.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Xenin entry;
CC URL="http://en.wikipedia.org/wiki/Xenin";
CC -----------------------------------------------------------------------
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CC Distributed under the Creative Commons Attribution-NoDerivs License
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DR EMBL; U24105; AAB70879.1; -; mRNA.
DR EMBL; AL513282; CAI12454.1; -; Genomic_DNA.
DR EMBL; AL445230; CAI12454.1; JOINED; Genomic_DNA.
DR EMBL; AL513282; CAI12455.1; -; Genomic_DNA.
DR EMBL; AL445230; CAI12455.1; JOINED; Genomic_DNA.
DR EMBL; AL445230; CAI15004.1; -; Genomic_DNA.
DR EMBL; AL513282; CAI15004.1; JOINED; Genomic_DNA.
DR EMBL; AL445230; CAI15005.1; -; Genomic_DNA.
DR EMBL; AL513282; CAI15005.1; JOINED; Genomic_DNA.
DR EMBL; CH471121; EAW52723.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW52725.1; -; Genomic_DNA.
DR EMBL; BC038447; AAH38447.1; -; mRNA.
DR PIR; JC4668; ERHUAH.
DR RefSeq; NP_001091868.1; NM_001098398.1.
DR RefSeq; NP_004362.2; NM_004371.3.
DR UniGene; Hs.162121; -.
DR UniGene; Hs.685025; -.
DR ProteinModelPortal; P53621; -.
DR SMR; P53621; 1-810, 905-1224.
DR IntAct; P53621; 22.
DR MINT; MINT-1144184; -.
DR STRING; 9606.ENSP00000357048; -.
DR PhosphoSite; P53621; -.
DR DMDM; 205371746; -.
DR PaxDb; P53621; -.
DR PRIDE; P53621; -.
DR Ensembl; ENST00000241704; ENSP00000241704; ENSG00000122218.
DR Ensembl; ENST00000368069; ENSP00000357048; ENSG00000122218.
DR GeneID; 1314; -.
DR KEGG; hsa:1314; -.
DR UCSC; uc009wti.3; human.
DR CTD; 1314; -.
DR GeneCards; GC01M160258; -.
DR HGNC; HGNC:2230; COPA.
DR HPA; HPA028024; -.
DR MIM; 601924; gene.
DR neXtProt; NX_P53621; -.
DR PharmGKB; PA26746; -.
DR eggNOG; COG2319; -.
DR HOGENOM; HOG000195913; -.
DR HOVERGEN; HBG005379; -.
DR KO; K05236; -.
DR OMA; FWVLGAH; -.
DR OrthoDB; EOG78WKQX; -.
DR PhylomeDB; P53621; -.
DR Reactome; REACT_11123; Membrane Trafficking.
DR SignaLink; P53621; -.
DR ChiTaRS; COPA; human.
DR GeneWiki; COPA_(gene); -.
DR GenomeRNAi; 1314; -.
DR NextBio; 5373; -.
DR PRO; PR:P53621; -.
DR Bgee; P53621; -.
DR CleanEx; HS_COPA; -.
DR Genevestigator; P53621; -.
DR GO; GO:0030126; C:COPI vesicle coat; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0048205; P:COPI coating of Golgi vesicle; TAS:Reactome.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0030157; P:pancreatic juice secretion; IDA:MGI.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to ER; TAS:Reactome.
DR Gene3D; 2.130.10.10; -; 1.
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.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR017986; WD40_repeat_dom.
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; SSF50978; SSF50978; 2.
DR SUPFAM; SSF51004; SSF51004; 3.
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 Alternative splicing; Complete proteome; Cytoplasm;
KW Cytoplasmic vesicle; Direct protein sequencing; ER-Golgi transport;
KW Golgi apparatus; Hormone; Membrane; Phosphoprotein; Polymorphism;
KW Protein transport; Reference proteome; Repeat; RNA editing; Secreted;
KW Transport; WD repeat.
FT CHAIN 1 1224 Coatomer subunit alpha.
FT /FTId=PRO_0000223307.
FT PEPTIDE 1 35 Proxenin.
FT /FTId=PRO_0000041400.
FT PEPTIDE 1 25 Xenin.
FT /FTId=PRO_0000041401.
FT REPEAT 7 37 WD 1.
FT REPEAT 49 79 WD 2.
FT REPEAT 91 121 WD 3.
FT REPEAT 133 163 WD 4.
FT REPEAT 203 233 WD 5.
FT REPEAT 247 277 WD 6.
FT MOD_RES 173 173 Phosphoserine.
FT MOD_RES 185 185 Phosphothreonine.
FT MOD_RES 402 402 Phosphoserine.
FT MOD_RES 895 895 Phosphoserine.
FT VAR_SEQ 509 509 H -> HEHSCPLPLT (in isoform 2).
FT /FTId=VSP_035043.
FT VARIANT 164 164 I -> V (in RNA edited version).
FT /FTId=VAR_066525.
FT VARIANT 1040 1040 V -> G (in dbSNP:rs34997807).
FT /FTId=VAR_033803.
FT CONFLICT 703 703 L -> V (in Ref. 1; AAB70879).
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
//
MIM
601924
*RECORD*
*FIELD* NO
601924
*FIELD* TI
*601924 COATOMER PROTEIN COMPLEX, SUBUNIT ALPHA; COPA
;;ALPHA COAT PROTEIN
COATOMER PROTEIN COMPLEX, INCLUDED; COPI, INCLUDED
read more*FIELD* TX
DESCRIPTION
In eukaryotic cells, protein transport between the endoplasmic reticulum
(ER) and Golgi compartments is mediated in part by non-clathrin-coated
vesicular coat proteins (COPs). Seven COP subunits have been recognized,
and represent components of a complex known as coatomer, or COPI. The
subunits are designated alpha-COP, beta-COP (600959), beta-prime-COP,
gamma-COP, delta-COP (600820), epsilon-COP (606942), and zeta-COP.
CLONING
Chow and Quek (1996) reported the cDNA sequence encoding the COPA gene
(called HEP-COP by them). The open reading frame predicts a 1,224-amino
acid polypeptide that shares high sequence similarity with RET1P, the
alpha subunit of the coatomer complex in yeast.
By Western blot analysis of protein lysates from human hepatoma cell
lines using antibodies against COPA, Quek and Chow (1997) showed that
COPA, which they called HEP-COP, migrates as an approximately 160-kD
protein. Immunoblotting of subcellular components of Hep3B cells
revealed that COPA protein is located predominantly in the microsomal
and cytosolic fractions; COPA was virtually absent in the nuclear
compartment. Indirect immunofluorescence of Hep3B cells showed that COPA
is located chiefly in the cytoplasm.
GENE FUNCTION
COPI is a heptameric protein recruited to membranes by ARF1 (103180), a
GTP-binding protein. Coat assembly helps in the transport of budding off
membrane between the ER and Golgi apparatus. Using fluorescence
microscopy, Presley et al. (2002) showed that guanine nucleotide
exchange-activated ARF1 at the Golgi membrane recruits and binds
cytoplasmic COPI to the membranes. Photobleaching experiments
demonstrated that COPI remains at the membranes after ARF1-GTP has been
hydrolyzed by ARFGAP1 (608377). COPI binds to membrane cargo,
soluble-cargo receptors, or other Golgi proteins. Uncoating, or the
release of COPI from Golgi membranes to the cytoplasm, then occurs,
which can be inhibited by aluminum fluoride. Presley et al. (2002)
concluded from their kinetic and biochemical analyses that COPI and ARF1
continuously bind and release from Golgi membranes, allowing the
membrane at these sites to recruit cargo, alter their phospholipid
composition, and become larger, phase-separated domains.
Liu et al. (2003) found that a central region of Xenopus Nup153 (603948)
associated with COPI. Nup153 recruited COPI to the nuclear membrane
during mitosis, suggesting that vesiculation is an important step in
nuclear envelope breakdown. Perturbing the function of the COPI complex
impaired nuclear envelope disassembly.
GENE STRUCTURE
Quek and Chow (1997) reported the genomic organization of the COPA gene.
It contains 33 exons ranging in size from 67 to 611 bp. All exon-intron
junctions conform with the GT-AG rule. The 32 introns range from about
80 bp to 4 kb, with the genomic DNA of COPA estimated to span
approximately 37 kb. The untranscribed and noncoding portions of the
5-prime end of the gene lacked TATA and CAAT boxes but displayed a high
GC content, consistent with its being a housekeeping gene.
MAPPING
By fluorescence in situ hybridization, Quek and Chow (1997) mapped the
COPA gene to 1q23-q25.
*FIELD* RF
1. 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. Liu, J.; Prunuske, A. J.; Fager, A. M.; Ullman, K. S.: The COPI
complex functions in nuclear envelope breakdown and is recruited by
the nucleoporin Nup153. Dev. Cell 5: 487-498, 2003.
3. Presley, J. F.; Ward, T. H.; Pfeifer, A. C.; Siggia, E. D.; Phair,
R. D.; Lippincott-Schwartz, J.: Dissection of COPI and Arf1 dynamics
in vivo and role in Golgi membrane transport. Nature 417: 187-193,
2002.
4. Quek, H. H.; Chow, V. T. K.: Molecular and cellular studies of
the human homolog of the 160-kD alpha-subunit of the coatomer protein
complex. DNA Cell Biol. 16: 275-280, 1997.
5. Quek, H. H.; Chow, V. T. K.: Genomic organization and mapping
of the human HEP-COP gene (COPA) to 1q. Cytogenet. Cell Genet. 76:
139-143, 1997.
*FIELD* CN
Patricia A. Hartz - updated: 5/12/2004
Paul J. Converse - updated: 5/10/2002
Patti M. Sherman - updated: 6/13/2000
*FIELD* CD
Victor A. McKusick: 7/25/1997
*FIELD* ED
carol: 08/01/2013
mgross: 8/1/2005
mgross: 5/12/2004
mgross: 5/14/2002
mgross: 5/10/2002
mcapotos: 6/21/2000
psherman: 6/13/2000
terry: 7/25/1997
*RECORD*
*FIELD* NO
601924
*FIELD* TI
*601924 COATOMER PROTEIN COMPLEX, SUBUNIT ALPHA; COPA
;;ALPHA COAT PROTEIN
COATOMER PROTEIN COMPLEX, INCLUDED; COPI, INCLUDED
read more*FIELD* TX
DESCRIPTION
In eukaryotic cells, protein transport between the endoplasmic reticulum
(ER) and Golgi compartments is mediated in part by non-clathrin-coated
vesicular coat proteins (COPs). Seven COP subunits have been recognized,
and represent components of a complex known as coatomer, or COPI. The
subunits are designated alpha-COP, beta-COP (600959), beta-prime-COP,
gamma-COP, delta-COP (600820), epsilon-COP (606942), and zeta-COP.
CLONING
Chow and Quek (1996) reported the cDNA sequence encoding the COPA gene
(called HEP-COP by them). The open reading frame predicts a 1,224-amino
acid polypeptide that shares high sequence similarity with RET1P, the
alpha subunit of the coatomer complex in yeast.
By Western blot analysis of protein lysates from human hepatoma cell
lines using antibodies against COPA, Quek and Chow (1997) showed that
COPA, which they called HEP-COP, migrates as an approximately 160-kD
protein. Immunoblotting of subcellular components of Hep3B cells
revealed that COPA protein is located predominantly in the microsomal
and cytosolic fractions; COPA was virtually absent in the nuclear
compartment. Indirect immunofluorescence of Hep3B cells showed that COPA
is located chiefly in the cytoplasm.
GENE FUNCTION
COPI is a heptameric protein recruited to membranes by ARF1 (103180), a
GTP-binding protein. Coat assembly helps in the transport of budding off
membrane between the ER and Golgi apparatus. Using fluorescence
microscopy, Presley et al. (2002) showed that guanine nucleotide
exchange-activated ARF1 at the Golgi membrane recruits and binds
cytoplasmic COPI to the membranes. Photobleaching experiments
demonstrated that COPI remains at the membranes after ARF1-GTP has been
hydrolyzed by ARFGAP1 (608377). COPI binds to membrane cargo,
soluble-cargo receptors, or other Golgi proteins. Uncoating, or the
release of COPI from Golgi membranes to the cytoplasm, then occurs,
which can be inhibited by aluminum fluoride. Presley et al. (2002)
concluded from their kinetic and biochemical analyses that COPI and ARF1
continuously bind and release from Golgi membranes, allowing the
membrane at these sites to recruit cargo, alter their phospholipid
composition, and become larger, phase-separated domains.
Liu et al. (2003) found that a central region of Xenopus Nup153 (603948)
associated with COPI. Nup153 recruited COPI to the nuclear membrane
during mitosis, suggesting that vesiculation is an important step in
nuclear envelope breakdown. Perturbing the function of the COPI complex
impaired nuclear envelope disassembly.
GENE STRUCTURE
Quek and Chow (1997) reported the genomic organization of the COPA gene.
It contains 33 exons ranging in size from 67 to 611 bp. All exon-intron
junctions conform with the GT-AG rule. The 32 introns range from about
80 bp to 4 kb, with the genomic DNA of COPA estimated to span
approximately 37 kb. The untranscribed and noncoding portions of the
5-prime end of the gene lacked TATA and CAAT boxes but displayed a high
GC content, consistent with its being a housekeeping gene.
MAPPING
By fluorescence in situ hybridization, Quek and Chow (1997) mapped the
COPA gene to 1q23-q25.
*FIELD* RF
1. 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. Liu, J.; Prunuske, A. J.; Fager, A. M.; Ullman, K. S.: The COPI
complex functions in nuclear envelope breakdown and is recruited by
the nucleoporin Nup153. Dev. Cell 5: 487-498, 2003.
3. Presley, J. F.; Ward, T. H.; Pfeifer, A. C.; Siggia, E. D.; Phair,
R. D.; Lippincott-Schwartz, J.: Dissection of COPI and Arf1 dynamics
in vivo and role in Golgi membrane transport. Nature 417: 187-193,
2002.
4. Quek, H. H.; Chow, V. T. K.: Molecular and cellular studies of
the human homolog of the 160-kD alpha-subunit of the coatomer protein
complex. DNA Cell Biol. 16: 275-280, 1997.
5. Quek, H. H.; Chow, V. T. K.: Genomic organization and mapping
of the human HEP-COP gene (COPA) to 1q. Cytogenet. Cell Genet. 76:
139-143, 1997.
*FIELD* CN
Patricia A. Hartz - updated: 5/12/2004
Paul J. Converse - updated: 5/10/2002
Patti M. Sherman - updated: 6/13/2000
*FIELD* CD
Victor A. McKusick: 7/25/1997
*FIELD* ED
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mcapotos: 6/21/2000
psherman: 6/13/2000
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