ID Q6FQT4_CANGA Unreviewed; 1201 AA.
AC Q6FQT4;
DT 19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 137.
DE RecName: Full=Coatomer subunit alpha {ECO:0000256|PIRNR:PIRNR003354};
GN OrderedLocusNames=CAGL0I03718g {ECO:0000313|CGD:CAL0132570,
GN ECO:0000313|EMBL:CAG60347.1};
OS Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 /
OS NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces.
OX NCBI_TaxID=284593 {ECO:0000313|EMBL:CAG60347.1, ECO:0000313|Proteomes:UP000002428};
RN [1] {ECO:0000313|EMBL:CAG60347.1, ECO:0000313|Proteomes:UP000002428}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65
RC {ECO:0000313|Proteomes:UP000002428};
RX PubMed=15229592; DOI=10.1038/nature02579;
RG Genolevures;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA Wincker P., Souciet J.L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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.
CC {ECO:0000256|PIRNR:PIRNR003354}.
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}. Membrane
CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004287}.
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DR EMBL; CR380955; CAG60347.1; -; Genomic_DNA.
DR RefSeq; XP_447410.1; XM_447410.1.
DR AlphaFoldDB; Q6FQT4; -.
DR STRING; 284593.Q6FQT4; -.
DR EnsemblFungi; CAGL0I03718g-T; CAGL0I03718g-T-p1; CAGL0I03718g.
DR GeneID; 2889149; -.
DR KEGG; cgr:CAGL0I03718g; -.
DR CGD; CAL0132570; CAGL0I03718g.
DR VEuPathDB; FungiDB:CAGL0I03718g; -.
DR eggNOG; KOG0292; Eukaryota.
DR HOGENOM; CLU_007565_1_0_1; -.
DR InParanoid; Q6FQT4; -.
DR OMA; EMTYQKQ; -.
DR Proteomes; UP000002428; Chromosome I.
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:0043130; F:ubiquitin binding; IEA:EnsemblFungi.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IEA:EnsemblFungi.
DR GO; GO:0008298; P:intracellular mRNA localization; IEA:EnsemblFungi.
DR GO; GO:0006886; P:intracellular protein transport; IEA:UniProtKB-UniRule.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IEA:EnsemblFungi.
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; IPR011044; Quino_amine_DH_bsu.
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; 5.
DR PIRSF; PIRSF003354; Coatomer_alpha_subunit; 1.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 8.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR SUPFAM; SSF50969; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 5.
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:UP000002428};
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 49..90
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 91..132
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 133..174
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 205..246
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 249..290
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT DOMAIN 343..770
FT /note="Coatomer WD associated region"
FT /evidence="ECO:0000259|Pfam:PF04053"
FT DOMAIN 842..1199
FT /note="Coatomer alpha subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06957"
FT REGION 833..853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1201 AA; 134960 MW; C09C6D940B66FA9C CRC64;
MKLLTKFESK STRAKGIAFH PSRPWALVAL FSSTIQLWDY RMGTLLHRFE GHEGPVRAVD
FHPTQPIFVS AGDDASIKVW SLETNRCLYT LTGHLDYVRT VFFHSELPWV ISASDDQTVR
IWNWQNRKEL ACLTGHNHFV MCAQFHQTED LVVSASLDET VRVWDISGLR KKHSAPGVTS
YEDSLASQQN LLDGAFGDCK VKFILEGHTR GVNWASFHPT LPLIVTGGDD RQVKLWRMSS
NKAWEVDTCR GHTNNVDCVV FHPDQNLILS VAEDKTLRIW DLDKRTPVKQ FKRENDRFWL
IRSHPNMSLF GAAHDSGIMI FKLDRERPAA TTYQNQLFFV NKEKQLQSFD YGKKVTSLPY
VTLTKLGQAW NSFHSISYNP SQHSVLINEG TDKFGLVVLP KQPTGAVEPT SVIEDSGSCA
TFVARNRFAV YNKSSQSIEV RTLDNKITKT IHVEDPVNDM LYAAPGTVLL LHPKEVVLFD
VQQGKKVAQM HVKNVKYVSW SQDGQYLAMM SKHTITIVNK RLELINSMHE TIRIKSAAWD
ESNVLVYTTL NHIRYSLLNG DHGIIKTLEK TLYIHKVQGK YVYALNRDGE MEVLNIDPTE
YRFKKALVNK NFPEVLRIIR NSNLVGQNII SYLQKSGYPE IALQFVQDPQ ARFDLAIEYG
NLDVASEEAK KLNNDATWNI LSKEALAQGN IALTEMIYQT QNAFDKLSFL YTITGDQNKL
AKMENIAQNH GATSSILMNS FYSNSIDSRA KVFQTAGSLP LAFAVAKANG NDELAAYYLE
EAGLDEQDVV LPDGITPSNS VKTPAITEPL TSWPLKEAEL SYFEKAVLGQ IEEYDADEPS
SDKETTTAAG HEEEAFFDDE EIIGDEEDAW DLGDDDLQIG NDEVEAEAND VDASQDEDTE
TAQWVKNSKL ASVLVASGAF EAAAQALHKQ VGVVDFEPLR SYFIDIYEGS RTYMTGTPEE
LPPIVGHIRS NADTDIPEEA LPKVPGMDIV SAKINEGFKL FKANKLEEAI ETFREVIYRV
LFLTLEDDDE EELAHKALET AKEYILGLSI ELERRSLAPE DVKRNLELAA YFTRSKLVPA
HRCNALQVAM SQNFKNKNYV QASYFASEFL KLMSSGPRAD QARKIKDKAD SLAHDAVEIN
FDPYAEFDIC AATHTPIYKD AAVVEDPLTG AKYHANHKGD IDSIAKISKI GAPSSGLRIR
L
//
