ID A0A151M7D0_ALLMI Unreviewed; 1224 AA.
AC A0A151M7D0;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Coatomer subunit alpha {ECO:0000256|PIRNR:PIRNR003354};
GN Name=COPA {ECO:0000313|EMBL:KYO20438.1};
GN ORFNames=Y1Q_0005892 {ECO:0000313|EMBL:KYO20438.1};
OS Alligator mississippiensis (American alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO20438.1};
RN [1] {ECO:0000313|EMBL:KYO20438.1, ECO:0000313|Proteomes:UP000050525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO20438.1};
RX PubMed=22293439; DOI=10.1186/gb-2012-13-1-415;
RA St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., Gongora J.,
RA Dalzell P., Moran C., Bed'hom B., Abzhanov A., Burgess S.C., Cooksey A.M.,
RA Castoe T.A., Crawford N.G., Densmore L.D., Drew J.C., Edwards S.V.,
RA Faircloth B.C., Fujita M.K., Greenwold M.J., Hoffmann F.G., Howard J.M.,
RA Iguchi T., Janes D.E., Khan S.Y., Kohno S., de Koning A.J., Lance S.L.,
RA McCarthy F.M., McCormack J.E., Merchant M.E., Peterson D.G., Pollock D.D.,
RA Pourmand N., Raney B.J., Roessler K.A., Sanford J.R., Sawyer R.H.,
RA Schmidt C.J., Triplett E.W., Tuberville T.D., Venegas-Anaya M.,
RA Howard J.T., Jarvis E.D., Guillette L.J.Jr., Glenn T.C., Green R.E.,
RA Ray D.A.;
RT "Sequencing three crocodilian genomes to illuminate the evolution of
RT archosaurs and amniotes.";
RL Genome Biol. 13:415-415(2012).
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. {ECO:0000256|ARBA:ARBA00024791}.
CC -!- SUBUNIT: Oligomeric complex that consists of at least the alpha, beta,
CC beta', gamma, delta, epsilon and zeta subunits.
CC {ECO:0000256|PIRNR:PIRNR003354}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR003354}. Golgi
CC apparatus membrane {ECO:0000256|ARBA:ARBA00004255,
CC ECO:0000256|PIRNR:PIRNR003354}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004255, ECO:0000256|PIRNR:PIRNR003354};
CC Cytoplasmic side {ECO:0000256|ARBA:ARBA00004255}. Cytoplasmic vesicle,
CC COPI-coated vesicle membrane {ECO:0000256|ARBA:ARBA00004347};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004347};
CC Cytoplasmic side {ECO:0000256|ARBA:ARBA00004347}. Membrane
CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004287}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KYO20438.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AKHW03006405; KYO20438.1; -; Genomic_DNA.
DR RefSeq; XP_006267538.1; XM_006267476.3.
DR AlphaFoldDB; A0A151M7D0; -.
DR STRING; 8496.A0A151M7D0; -.
DR GeneID; 102560777; -.
DR KEGG; amj:102560777; -.
DR CTD; 1314; -.
DR eggNOG; KOG0292; Eukaryota.
DR OrthoDB; 20819at2759; -.
DR PhylomeDB; A0A151M7D0; -.
DR Proteomes; UP000050525; Unassembled WGS sequence.
DR GO; GO:0030126; C:COPI vesicle coat; IEA:UniProtKB-UniRule.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
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:0006886; P:intracellular protein transport; IEA:UniProtKB-UniRule.
DR CDD; cd22948; Coatomer_WDAD_alpha; 1.
DR CDD; cd00200; WD40; 1.
DR Gene3D; 1.25.40.470; -; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR047312; Coatomer_alpha_WD-assoc_reg.
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; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR19876; COATOMER; 1.
DR PANTHER; PTHR19876:SF1; COATOMER SUBUNIT ALPHA; 1.
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; WD40 repeat-like; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 6.
DR PROSITE; PS50294; WD_REPEATS_REGION; 5.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|PIRNR:PIRNR003354};
KW ER-Golgi transport {ECO:0000256|ARBA:ARBA00022892,
KW ECO:0000256|PIRNR:PIRNR003354};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034,
KW ECO:0000256|PIRNR:PIRNR003354};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR003354};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW ECO:0000256|PIRNR:PIRNR003354};
KW Reference proteome {ECO:0000313|Proteomes:UP000050525};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR003354};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}.
FT REPEAT 5..39
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 47..88
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 89..130
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 131..165
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 201..242
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 245..286
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT DOMAIN 341..766
FT /note="Coatomer WD associated region"
FT /evidence="ECO:0000259|Pfam:PF04053"
FT DOMAIN 815..1224
FT /note="Coatomer alpha subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06957"
SQ SEQUENCE 1224 AA; 138510 MW; 39F2740AB8E35817 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 NVLYYVKDRF LRQLDFNSSK DVAVMQLRSG
SKFPVFNMSY NPAENAVLLC TRASNLENST YDLYTIPKDA DSQNPDAPEG KRSSGLTAVW
VARNRFAVLD RMHSILIKNL KNEITKKVQV PNCDEIFYAG TGNLLLRDAD SITLFDVQQK
RTLASVKISK VKYVIWSADM SHVALLAKHA IMICNRKLES LCNIHENIRV KSGAWDESGV
FIYTTSNHIK YAVTTGDHGI IRTLDLPIYV TRVKGNNVYC LDRECRPRVL TIDPTEFKFK
LALINRKYDE VLHMVRNAKL VGQSIIAYLQ KKGYPEVALH FVKDEKTRFS LALECGNIEI
ALEAAKALDD KNCWEKLGEV ALLQGNHQIV EMCYQRTKNF DRLSFLYLIT GNLEKLRKMM
KIAEIRKDMS GHYQNALYLG DVAERVRILK NCGQKSLAYL TAATHGLDEE AESLKETFDP
EKETIPDIDP DAQLLQPPAP VMPLDTNWPL LTVSKGFFEG TIASKGKGGA MAADIDIDTV
GTEGWGEDAE LQLDEDGFVD AADGFGDEAV GKGQEEGGGW EVEEDLDLPP ELDVPVGPAG
GAEDGFFVPP TKGTSPAQVW CNNSQLPVDH VLAGSFETAM RLLHDQVGVT NFGPYKQLFL
QTYARGRTTY QALPCLPSMY GYPHRNWKEA TLKNAVPAVG LKLNDLIQRL QLCYQLTTSG
KFEEAVEKFR SILLSVPLLV VDNKQEIAEA QQLIAICREY IVGLSMEIER KKLPKETLEQ
QKRICETAAY FTHSNLQPVH MILVLRTALN LFFKLKNFKT AATFARRLLE LGPKPEVAQQ
TRKILSACEK NPTDTYQLNY DMHNPFDICA ASYRPIYRGK PVEKCPLSGA CYYPEYQGQI
CRVTTVTEIG KDVIGLRISP LQFR
//
