COPA_BOVIN
ID COPA_BOVIN Reviewed; 1224 AA.
AC Q27954; A7Z053;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 156.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 1-25; 161-168; 296-306;
RP 314-331; 383-398; 413-431; 518-529; 676-691; 728-742; 776-793; 968-980;
RP 1010-1020; 1087-1100 AND 1202-1208.
RC TISSUE=Liver;
RX PubMed=8858162; DOI=10.1083/jcb.135.1.53;
RA Faulstich D., Auerbach S., Orci L., Ravazzola M., Wegehingel S.,
RA Lottspeich F., Stenbeck G., Harter C., Wieland F.T., Tschochner H.;
RT "Architecture of coatomer: molecular characterization of delta-COP and
RT protein interactions within the complex.";
RL J. Cell Biol. 135:53-61(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP INTERACTION WITH PEX11A.
RX PubMed=9548716; DOI=10.1083/jcb.141.2.373;
RA Passreiter M., Anton M., Lay D., Frank R., Harter C., Wieland F.T.,
RA Gorgas K., Just W.W.;
RT "Peroxisome biogenesis: involvement of ARF and coatomer.";
RL J. Cell Biol. 141:373-383(1998).
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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Oligomeric complex that consists of at least the alpha, beta,
CC beta', gamma, delta, epsilon and zeta subunits. Probably interacts with
CC PEX11A. Interacts with SCYL1. Interacts with JAGN1 (By similarity).
CC Interacts with TMEM41B (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:P53621}.
CC -!- INTERACTION:
CC Q27954; P35605: COPB2; NbExp=2; IntAct=EBI-620400, EBI-620411;
CC Q27954; Q28104: COPE; NbExp=5; IntAct=EBI-620400, EBI-620457;
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}.
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DR EMBL; X96768; CAA65543.1; -; mRNA.
DR EMBL; BC153251; AAI53252.1; -; mRNA.
DR RefSeq; NP_001099115.1; NM_001105645.1.
DR PDB; 3MKR; X-ray; 2.60 A; B=905-1224.
DR PDBsum; 3MKR; -.
DR AlphaFoldDB; Q27954; -.
DR SMR; Q27954; -.
DR BioGRID; 780059; 1.
DR IntAct; Q27954; 2.
DR MINT; Q27954; -.
DR STRING; 9913.ENSBTAP00000005672; -.
DR PaxDb; Q27954; -.
DR PeptideAtlas; Q27954; -.
DR PRIDE; Q27954; -.
DR GeneID; 100126041; -.
DR KEGG; bta:100126041; -.
DR CTD; 1314; -.
DR eggNOG; KOG0292; Eukaryota.
DR HOGENOM; CLU_007565_1_0_1; -.
DR InParanoid; Q27954; -.
DR OrthoDB; 139008at2759; -.
DR TreeFam; TF105693; -.
DR EvolutionaryTrace; Q27954; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0030126; C:COPI vesicle coat; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
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; IEA:InterPro.
DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; TAS:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; TAS:UniProtKB.
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; 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 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; Cytoplasm; Cytoplasmic vesicle; Direct protein sequencing;
KW ER-Golgi transport; Golgi apparatus; Hormone; Membrane; Methylation;
KW Phosphoprotein; Protein transport; Reference proteome; Repeat; Secreted;
KW Transport; WD repeat.
FT CHAIN 1..1224
FT /note="Coatomer subunit alpha"
FT /id="PRO_0000223305"
FT PEPTIDE 1..35
FT /note="Proxenin"
FT /id="PRO_0000041398"
FT PEPTIDE 1..25
FT /note="Xenin"
FT /id="PRO_0000041399"
FT REPEAT 7..37
FT /note="WD 1"
FT REPEAT 49..79
FT /note="WD 2"
FT REPEAT 91..121
FT /note="WD 3"
FT REPEAT 133..163
FT /note="WD 4"
FT REPEAT 203..233
FT /note="WD 5"
FT REPEAT 247..277
FT /note="WD 6"
FT MOD_RES 173
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53621"
FT MOD_RES 185
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P53621"
FT MOD_RES 591
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P53621"
FT MOD_RES 965
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P53621"
FT MOD_RES 1193
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53621"
FT CONFLICT 402
FT /note="T -> S (in Ref. 2; AAI53252)"
FT /evidence="ECO:0000305"
FT HELIX 916..923
FT /evidence="ECO:0007829|PDB:3MKR"
FT HELIX 927..932
FT /evidence="ECO:0007829|PDB:3MKR"
FT HELIX 936..946
FT /evidence="ECO:0007829|PDB:3MKR"
FT HELIX 953..955
FT /evidence="ECO:0007829|PDB:3MKR"
FT HELIX 956..963
FT /evidence="ECO:0007829|PDB:3MKR"
FT STRAND 968..970
FT /evidence="ECO:0007829|PDB:3MKR"
FT STRAND 979..981
FT /evidence="ECO:0007829|PDB:3MKR"
FT TURN 985..989
FT /evidence="ECO:0007829|PDB:3MKR"
FT STRAND 992..994
FT /evidence="ECO:0007829|PDB:3MKR"
FT HELIX 1003..1018
FT /evidence="ECO:0007829|PDB:3MKR"
FT HELIX 1022..1035
FT /evidence="ECO:0007829|PDB:3MKR"
FT HELIX 1036..1038
FT /evidence="ECO:0007829|PDB:3MKR"
FT HELIX 1044..1070
FT /evidence="ECO:0007829|PDB:3MKR"
FT HELIX 1078..1091
FT /evidence="ECO:0007829|PDB:3MKR"
FT HELIX 1098..1114
FT /evidence="ECO:0007829|PDB:3MKR"
FT HELIX 1118..1130
FT /evidence="ECO:0007829|PDB:3MKR"
FT HELIX 1135..1150
FT /evidence="ECO:0007829|PDB:3MKR"
FT STRAND 1154..1156
FT /evidence="ECO:0007829|PDB:3MKR"
FT TURN 1170..1172
FT /evidence="ECO:0007829|PDB:3MKR"
FT TURN 1186..1188
FT /evidence="ECO:0007829|PDB:3MKR"
FT HELIX 1194..1196
FT /evidence="ECO:0007829|PDB:3MKR"
FT TURN 1202..1204
FT /evidence="ECO:0007829|PDB:3MKR"
FT STRAND 1205..1210
FT /evidence="ECO:0007829|PDB:3MKR"
FT HELIX 1220..1222
FT /evidence="ECO:0007829|PDB:3MKR"
SQ 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
