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

 COPA_BOVIN              Reviewed;        1224 AA.
Q27954; A7Z053;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 1.
23-MAY-2018, entry version 137.
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;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 1-25; 161-168;
296-306; 314-331; 383-398; 413-431; 518-529; 676-691; 728-742;
776-793; 968-980; 1010-1020; 1087-1100 AND 1202-1208.
TISSUE=Liver;
PubMed=8858162; DOI=10.1083/jcb.135.1.53;
Faulstich D., Auerbach S., Orci L., Ravazzola M., Wegehingel S.,
Lottspeich F., Stenbeck G., Harter C., Wieland F.T., Tschochner H.;
"Architecture of coatomer: molecular characterization of delta-COP and
protein interactions within the complex.";
J. Cell Biol. 135:53-61(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Hereford; TISSUE=Uterus;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
[3]
INTERACTION WITH PEX11A.
PubMed=9548716; DOI=10.1083/jcb.141.2.373;
Passreiter M., Anton M., Lay D., Frank R., Harter C., Wieland F.T.,
Gorgas K., Just W.W.;
"Peroxisome biogenesis: involvement of ARF and coatomer.";
J. Cell Biol. 141:373-383(1998).
-!- 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 (By similarity). {ECO:0000250}.
-!- 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. Interacts with JAGN1
(By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P53621}.
-!- INTERACTION:
P35605:COPB2; NbExp=2; IntAct=EBI-620400, EBI-620411;
Q28104:COPE; NbExp=5; IntAct=EBI-620400, EBI-620457;
-!- 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}.
-----------------------------------------------------------------------
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EMBL; X96768; CAA65543.1; -; mRNA.
EMBL; BC153251; AAI53252.1; -; mRNA.
RefSeq; NP_001099115.1; NM_001105645.1.
UniGene; Bt.76408; -.
PDB; 3MKR; X-ray; 2.60 A; B=905-1224.
PDBsum; 3MKR; -.
ProteinModelPortal; Q27954; -.
SMR; Q27954; -.
IntAct; Q27954; 2.
MINT; Q27954; -.
STRING; 9913.ENSBTAP00000005672; -.
PaxDb; Q27954; -.
PeptideAtlas; Q27954; -.
PRIDE; Q27954; -.
GeneID; 100126041; -.
KEGG; bta:100126041; -.
CTD; 1314; -.
eggNOG; KOG0292; Eukaryota.
eggNOG; ENOG410XPZS; LUCA.
HOGENOM; HOG000195913; -.
HOVERGEN; HBG005379; -.
InParanoid; Q27954; -.
KO; K05236; -.
TreeFam; TF105693; -.
EvolutionaryTrace; Q27954; -.
Proteomes; UP000009136; Unplaced.
GO; GO:0030126; C:COPI vesicle coat; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
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; TAS:UniProtKB.
GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to ER; TAS:UniProtKB.
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; 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.
PROSITE; PS00678; WD_REPEATS_1; 1.
PROSITE; PS50082; WD_REPEATS_2; 6.
PROSITE; PS50294; WD_REPEATS_REGION; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Cytoplasmic vesicle;
Direct protein sequencing; ER-Golgi transport; Golgi apparatus;
Hormone; Membrane; Methylation; Phosphoprotein; Protein transport;
Reference proteome; Repeat; Secreted; Transport; WD repeat.
CHAIN 1 1224 Coatomer subunit alpha.
/FTId=PRO_0000223305.
PEPTIDE 1 35 Proxenin.
/FTId=PRO_0000041398.
PEPTIDE 1 25 Xenin.
/FTId=PRO_0000041399.
REPEAT 7 37 WD 1.
REPEAT 49 79 WD 2.
REPEAT 91 121 WD 3.
REPEAT 133 163 WD 4.
REPEAT 203 233 WD 5.
REPEAT 247 277 WD 6.
MOD_RES 173 173 Phosphoserine.
{ECO:0000250|UniProtKB:P53621}.
MOD_RES 185 185 Phosphothreonine.
{ECO:0000250|UniProtKB:P53621}.
MOD_RES 591 591 Phosphothreonine.
{ECO:0000250|UniProtKB:P53621}.
MOD_RES 965 965 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P53621}.
MOD_RES 1193 1193 Phosphoserine.
{ECO:0000250|UniProtKB:P53621}.
CONFLICT 402 402 T -> S (in Ref. 2; AAI53252).
{ECO:0000305}.
HELIX 916 923 {ECO:0000244|PDB:3MKR}.
HELIX 927 932 {ECO:0000244|PDB:3MKR}.
HELIX 936 946 {ECO:0000244|PDB:3MKR}.
HELIX 953 955 {ECO:0000244|PDB:3MKR}.
HELIX 956 963 {ECO:0000244|PDB:3MKR}.
STRAND 968 970 {ECO:0000244|PDB:3MKR}.
STRAND 979 981 {ECO:0000244|PDB:3MKR}.
TURN 985 989 {ECO:0000244|PDB:3MKR}.
STRAND 992 994 {ECO:0000244|PDB:3MKR}.
HELIX 1003 1018 {ECO:0000244|PDB:3MKR}.
HELIX 1022 1035 {ECO:0000244|PDB:3MKR}.
HELIX 1036 1038 {ECO:0000244|PDB:3MKR}.
HELIX 1044 1070 {ECO:0000244|PDB:3MKR}.
HELIX 1078 1091 {ECO:0000244|PDB:3MKR}.
HELIX 1098 1114 {ECO:0000244|PDB:3MKR}.
HELIX 1118 1130 {ECO:0000244|PDB:3MKR}.
HELIX 1135 1150 {ECO:0000244|PDB:3MKR}.
STRAND 1154 1156 {ECO:0000244|PDB:3MKR}.
TURN 1170 1172 {ECO:0000244|PDB:3MKR}.
TURN 1186 1188 {ECO:0000244|PDB:3MKR}.
HELIX 1194 1196 {ECO:0000244|PDB:3MKR}.
TURN 1202 1204 {ECO:0000244|PDB:3MKR}.
STRAND 1205 1210 {ECO:0000244|PDB:3MKR}.
HELIX 1220 1222 {ECO:0000244|PDB:3MKR}.
SEQUENCE 1224 AA; 138359 MW; C9350BF2AC00683D CRC64;
MLTKFETKSA RVKGLSFHPK RPWILTSLHN GVIQLWDYRM CTLIDKFDEH DGPVRGIDFH
KQQPLFVSGG DDYKIKVWNY KLRRCLFTLL GHLDYIRTTF FHHEYPWILS ASDDQTIRVW
NWQSRTCVCV LTGHNHYVMC AQFHPSEDLV VSASLDQTVR VWDISGLRKK NLSPGAVESD
VRGITGVDLF GTTDAVVKHV LEGHDRGVNW AAFHPTMPLI VSGADDRQVK IWRMNESKAW
EVDTCRGHYN NVSCAVFHPR QELILSNSED KSIRVWDMSK RTGVQTFRRD HDRFWVLAAH
PNLNLFAAGH DGGMIVFKLE RERPAYAVHG NMLHYVKDRF LRQLDFNSSK DVAVMQLRSG
SKFPVFSMSY NPAENAVLLC TRASNLENST YDLYTIPKDA DTQNPDAPEG KRSSGLTAVW
VARNRFAVLD RMHSLLIKNL KNEITKKVQV PNCDEIFYAG TGNLLLRDAE SITLFDVQQK
RTLASVKISK VKYVIWSADM SHVALLAKHA IVICNRKLEA LCNIHENIRV KSGAWDESGV
FIYTTSNHIK YAVTTGDYGI 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 SIASKGKGGA LAADIDIDTV
GTEGWGEDAE LQLDEDGFVE ATEGLGDDAL GKGQEEGGGW DVEEDLELPP ELDIPPGAAG
GAEDGFFVPP TKGTSPTQIW CNNSQLPVDH ILAGSFETAM RLLHDQVGVT QFGPYKQLFL
QTYARGRTTY QALPCLPSMY GYPNRNWKDA GLKNGVPAVG LKLNDLIQRL QLCYQLTTVG
KFEEAVEKFR SILLSVPLLV VDNKQEIAEA QQLITICREY IVGLSMETER KKLPKETLEQ
QKRICEMAAY FTHSNLQPVH MILVLRTALN LFFKLKNFRT AAAFARRLLE LGPKPEVAQQ
TRKILSACEK NPTDAYQLNY DMHNPFDICA ASYRPIYRGK PVEKCPLSGA CYSPEFKGQI
CKVTTVTEIG KDVIGLRISP LQFR


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