COPB_CANGA
ID COPB_CANGA Reviewed; 972 AA.
AC Q6FM46;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=Coatomer subunit beta {ECO:0000250|UniProtKB:P41810};
DE AltName: Full=Beta-coat protein {ECO:0000250|UniProtKB:P41810};
DE Short=Beta-COP {ECO:0000250|UniProtKB:P41810};
GN Name=SEC26 {ECO:0000250|UniProtKB:P41810}; OrderedLocusNames=CAGL0K11088g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1] {ECO:0000312|EMBL:CAG61661.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
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.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., 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. 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 (By similarity). {ECO:0000250|UniProtKB:P41810}.
CC -!- SUBUNIT: Oligomeric complex that consists of at least the alpha, beta,
CC beta', gamma, delta, epsilon and zeta subunits.
CC {ECO:0000250|UniProtKB:P41810}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P41810}. Golgi
CC apparatus membrane {ECO:0000250|UniProtKB:P41810}; Peripheral membrane
CC protein {ECO:0000250|UniProtKB:P41810}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P41810}. Cytoplasmic vesicle, COPI-coated
CC vesicle membrane {ECO:0000250|UniProtKB:P41810}; Peripheral membrane
CC protein {ECO:0000250|UniProtKB:P41810}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P41810}. Note=The coatomer is cytoplasmic or
CC polymerized on the cytoplasmic side of the Golgi, as well as on the
CC vesicles/buds originating from it. {ECO:0000250|UniProtKB:P41810}.
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DR EMBL; CR380957; CAG61661.1; -; Genomic_DNA.
DR RefSeq; XP_448698.1; XM_448698.1.
DR AlphaFoldDB; Q6FM46; -.
DR SMR; Q6FM46; -.
DR STRING; 5478.XP_448698.1; -.
DR EnsemblFungi; CAG61661; CAG61661; CAGL0K11088g.
DR GeneID; 2890086; -.
DR KEGG; cgr:CAGL0K11088g; -.
DR CGD; CAL0134965; CAGL0K11088g.
DR VEuPathDB; FungiDB:CAGL0K11088g; -.
DR eggNOG; KOG1058; Eukaryota.
DR HOGENOM; CLU_006949_0_0_1; -.
DR InParanoid; Q6FM46; -.
DR OMA; QCGFMAA; -.
DR Proteomes; UP000002428; Chromosome K.
DR GO; GO:0030126; C:COPI vesicle coat; IEA:EnsemblFungi.
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:EnsemblFungi.
DR GO; GO:0008298; P:intracellular mRNA localization; IEA:EnsemblFungi.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
DR InterPro; IPR011710; Coatomer_bsu_C.
DR InterPro; IPR016460; COPB1.
DR InterPro; IPR029446; COPB1_appendage_platform_dom.
DR PANTHER; PTHR10635; PTHR10635; 1.
DR Pfam; PF01602; Adaptin_N; 1.
DR Pfam; PF07718; Coatamer_beta_C; 1.
DR Pfam; PF14806; Coatomer_b_Cpla; 1.
DR PIRSF; PIRSF005727; Coatomer_beta_subunit; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Cytoplasmic vesicle; ER-Golgi transport; Golgi apparatus;
KW Membrane; Protein transport; Reference proteome; Repeat; Transport.
FT CHAIN 1..972
FT /note="Coatomer subunit beta"
FT /id="PRO_0000408946"
FT REPEAT 79..113
FT /note="HEAT 1"
FT /evidence="ECO:0000255"
FT REPEAT 133..170
FT /note="HEAT 2"
FT /evidence="ECO:0000255"
FT REPEAT 317..354
FT /note="HEAT 3"
FT /evidence="ECO:0000255"
FT REPEAT 397..434
FT /note="HEAT 4"
FT /evidence="ECO:0000255"
FT REPEAT 481..518
FT /note="HEAT 5"
FT /evidence="ECO:0000255"
FT REGION 494..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 972 AA; 108446 MW; 1D98B14F165B1B79 CRC64;
MTAEIDPPAY TLVFNPATNS TPNTVAEFQK ALEKGSDETK IEAMKEILVT MLEGNPLPEM
LMHIIRFVMP SKNKKLKKLL YFYWEIVPKL DQDGKLRHEM ILVCNAIQHD LQHPNEFIRG
NTLRFLTKLR EPELLEQMVP STLACLEYRH AYVRKYAILA VLSIYKVSEH LLPDAKEIIN
TFLLAETDPI CKRNAFLGLS ELDRDNALQY LQDNIDDIES LDPLLQAAFV QFIRKDAIQT
PALKSQYCDL LLELLASATA DEVVFETALA LTILSGNQTV LIKAVSKMID LAVKVSDNNV
KIIVLDRIQD INERNPGCLE ELTLDILRVL NAEDIDVRSK ALTIAMDLVT SRNIEDVVQL
LKKELQTTVI NNEKEKSSDY RSLLIKTIRG IAVRFEEIAA NIVSLLLDFI TDLNSVAANG
VIAFVKDVVE LYPQLRSNIL ENLIAKLESV NSAKAYRGAL WILGEYSTTE SEIQDSWKHI
RQSIGEIPIL QTELKNQRKS QDEDDEATEE SATKQAGPVI LPDGTYATEN AFGSSNNDNK
KKLVENENRP PLRRFVLGGD FYTASILAST IVKLVLRFEK VSERAAVLNA LKAEGLLMLV
SIIRVGESSI VEKNIDEDSQ ERITTAIAIL MDESNPDESS AERELLNIAF LDATKASFKG
QFVAQKKTKL FKSSPVRKHK EAIDQSVSFR LLQENDNTAV SGDAIDEDLQ LAIRGDAARD
TSSIAISKLK KIVPLTGFSD PVYAEACITT NQFDVVLDVL LVNQTKETLK NFHVQFATLG
DLKIVENPPA TNVVPHGFHR VSVTVKVSSA DTGVIFGNII YDGGHGQDAR YVILNDVHVD
LMDYIKPAKT DDESFRTMWN AFEWENKISV KSKLPSLHAY LDELIKGTNM GVLTPVESLG
EKDCRFLCCN LYARSSFGED ALANLCIELD PNTEQVVGYV RIRSKGQGLA LSLGDRVALI
AKQNNKVIVG HV
