COPB_YEAST
ID COPB_YEAST Reviewed; 973 AA.
AC P41810; D6VSL9; Q03779;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Coatomer subunit beta;
DE AltName: Full=Beta-coat protein;
DE Short=Beta-COP;
GN Name=SEC26; OrderedLocusNames=YDR238C; ORFNames=YD8419.05C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 353-362; 496-514;
RP 645-655 AND 934-942, FUNCTION, PTM, AND DISRUPTION PHENOTYPE.
RC STRAIN=RSY255;
RX PubMed=7929113; DOI=10.1016/s0021-9258(19)51110-3;
RA Duden R., Hosobuchi M., Hamamoto S., Winey M., Byers B., Schekman R.;
RT "Yeast beta- and beta'-coat proteins (COP). Two coatomer subunits essential
RT for endoplasmic reticulum-to-Golgi protein traffic.";
RL J. Biol. Chem. 269:24486-24495(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15356266; DOI=10.1091/mbc.e04-05-0411;
RA Trautwein M., Dengjel J., Schirle M., Spang A.;
RT "Arf1p provides an unexpected link between COPI vesicles and mRNA in
RT Saccharomyces cerevisiae.";
RL Mol. Biol. Cell 15:5021-5037(2004).
RN [7]
RP FUNCTION.
RX PubMed=16135527; DOI=10.1091/mbc.e05-07-0678;
RA Altmann K., Westermann B.;
RT "Role of essential genes in mitochondrial morphogenesis in Saccharomyces
RT cerevisiae.";
RL Mol. Biol. Cell 16:5410-5417(2005).
RN [8]
RP MUTAGENESIS OF 334-ASP--ASP-336.
RX PubMed=17954604; DOI=10.1083/jcb.200704142;
RA Michelsen K., Schmid V., Metz J., Heusser K., Liebel U., Schwede T.,
RA Spang A., Schwappach B.;
RT "Novel cargo-binding site in the beta and delta subunits of coatomer.";
RL J. Cell Biol. 179:209-217(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181 AND SER-540, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
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 Required for mitochondrial morphology. {ECO:0000269|PubMed:16135527,
CC ECO:0000269|PubMed:7929113}.
CC -!- SUBUNIT: Oligomeric complex that consists of at least the alpha, beta,
CC beta', gamma, delta, epsilon and zeta subunits. The complex interacts
CC with ARF1 and PAB1. {ECO:0000269|PubMed:15356266}.
CC -!- INTERACTION:
CC P41810; Q04651: ERV41; NbExp=3; IntAct=EBI-4869, EBI-27850;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus membrane
CC {ECO:0000269|PubMed:14562095}; Peripheral membrane protein
CC {ECO:0000269|PubMed:14562095}; Cytoplasmic side
CC {ECO:0000269|PubMed:14562095}. Cytoplasmic vesicle, COPI-coated vesicle
CC membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250};
CC Cytoplasmic side {ECO:0000250}. 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}.
CC -!- PTM: The N-terminus is blocked.
CC -!- DISRUPTION PHENOTYPE: Causes a block in ER to Golgi transport. Exhibits
CC exaggerated ER structures displaying interconnected networks of ER
CC cisternae. Cells arrest at all stages of the vegetative cycle.
CC {ECO:0000269|PubMed:7929113}.
CC -!- MISCELLANEOUS: Present with 26000 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
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DR EMBL; U11236; AAA61710.1; -; Genomic_DNA.
DR EMBL; Z49701; CAA89724.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12079.1; -; Genomic_DNA.
DR PIR; S54534; S54534.
DR RefSeq; NP_010524.3; NM_001180546.3.
DR AlphaFoldDB; P41810; -.
DR SMR; P41810; -.
DR BioGRID; 32289; 679.
DR ComplexPortal; CPX-1652; COPI vesicle coat complex.
DR DIP; DIP-6467N; -.
DR IntAct; P41810; 36.
DR MINT; P41810; -.
DR STRING; 4932.YDR238C; -.
DR iPTMnet; P41810; -.
DR MaxQB; P41810; -.
DR PaxDb; P41810; -.
DR PRIDE; P41810; -.
DR EnsemblFungi; YDR238C_mRNA; YDR238C; YDR238C.
DR GeneID; 851824; -.
DR KEGG; sce:YDR238C; -.
DR SGD; S000002646; SEC26.
DR VEuPathDB; FungiDB:YDR238C; -.
DR eggNOG; KOG1058; Eukaryota.
DR GeneTree; ENSGT00390000005270; -.
DR HOGENOM; CLU_006949_0_0_1; -.
DR InParanoid; P41810; -.
DR OMA; QCGFMAA; -.
DR BioCyc; YEAST:G3O-29813-MON; -.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR Reactome; R-SCE-6807878; COPI-mediated anterograde transport.
DR Reactome; R-SCE-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR PRO; PR:P41810; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P41810; protein.
DR GO; GO:0030126; C:COPI vesicle coat; IDA:SGD.
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; IMP:SGD.
DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0008298; P:intracellular mRNA localization; IMP:SGD.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IC:ComplexPortal.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
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 SMART; SM00185; ARM; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Cytoplasmic vesicle; Direct protein sequencing;
KW ER-Golgi transport; Golgi apparatus; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Repeat; Transport.
FT CHAIN 1..973
FT /note="Coatomer subunit beta"
FT /id="PRO_0000193839"
FT REPEAT 98..133
FT /note="HEAT 1"
FT REPEAT 134..170
FT /note="HEAT 2"
FT REPEAT 279..317
FT /note="HEAT 3"
FT REPEAT 318..354
FT /note="HEAT 4"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 540
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MUTAGEN 334..336
FT /note="DLD->NAN: Loses ability to recognize arginine (R)-
FT based ER localization signals in proteins. Recognition of
FT C-terminal di-lysine signals present in proteins is
FT unimpaired."
FT /evidence="ECO:0000269|PubMed:17954604"
FT CONFLICT 412
FT /note="D -> E (in Ref. 1; AAA61710)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 973 AA; 109019 MW; 885420DB026BCFA3 CRC64;
MTSLSSQPAY TLVFDPSPSM ETYSSTDFQK ALEKGSDEQK IDTMKSILVT MLEGNPMPEL
LMHIIRFVMP SKNKELKKLL YFYWEIVPKL AEDGKLRHEM ILVCNAIQHD LQHPNEYIRG
NTLRFLTKLR EAELLEQMVP SVLACLEYRH AYVRKYAILA VFSIFKVSEH LLPDAKEIIN
SFIVAETDPI CKRNAFIGLA ELDRENALHY LENNIADIEN LDPLLQAVFV QFIRQDANRT
PALKAQYIEL LMELLSTTTS DEVIFETALA LTVLSANPNV LVPAVNKLID LAVKVSDNNI
KLIVLDRIQD INANNVGALE ELTLDILRVL NAEDLDVRSK ALDISMDLAT SRNAEDVVQL
LKKELQTTVN NPDQDKAMQY RQLLIKTIRT VAVNFVEMAA SVVSLLLDFI GDLNSVAASG
IIAFIKEVIE KYPQLRANIL ENMVQTLDKV RSAKAYRGAL WIMGEYAEGE SEIQHCWKHI
RNSVGEVPIL QSEIKKLTQN QEHTEENEVD ATAKPTGPVI LPDGTYATES AFDVKTSQKS
VTDEERDSRP PIRRFVLSGD FYTAAILANT IIKLVLKFEN VSKNKTVINA LKAEALLILV
SIVRVGQSSL VEKKIDEDSL ERVMTSISIL LDEVNPEEKK EEVKLLEVAF LDTTKSSFKR
QIEIAKKNKH KRALKDSCKN IEPIDTPISF RQFAGVDSTN VQKDSIEEDL QLAMKGDAIH
ATSSSSISKL KKIVPLCGFS DPVYAEACIT NNQFDVVLDV LLVNQTKETL KNLHVQFATL
GDLKIIDTPQ KTNVIPHGFH KFTVTVKVSS ADTGVIFGNI IYDGAHGEDA RYVILNDVHV
DIMDYIKPAT ADDEHFRTMW NAFEWENKIS VKSQLPTLHA YLRELVKGTN MGILTPSESL
GEDDCRFLSC NLYAKSSFGE DALANLCIEK DSKTNDVIGY VRIRSKGQGL ALSLGDRVAL
IAKKTNKLAL THV
