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Coatomer subunit beta (Beta-coat protein) (Beta-COP)

 COPB_YEAST              Reviewed;         973 AA.
P41810; D6VSL9; Q03779;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 2.
25-APR-2018, entry version 168.
RecName: Full=Coatomer subunit beta;
AltName: Full=Beta-coat protein;
Short=Beta-COP;
Name=SEC26; OrderedLocusNames=YDR238C; ORFNames=YD8419.05C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 353-362;
496-514; 645-655 AND 934-942, FUNCTION, PTM, AND DISRUPTION PHENOTYPE.
STRAIN=RSY255;
PubMed=7929113;
Duden R., Hosobuchi M., Hamamoto S., Winey M., Byers B., Schekman R.;
"Yeast beta- and beta'-coat proteins (COP). Two coatomer subunits
essential for endoplasmic reticulum-to-Golgi protein traffic.";
J. Biol. Chem. 269:24486-24495(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169867;
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N.,
Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M.,
Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L.,
Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M.,
Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S.,
Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M.,
Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S.,
Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K.,
Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D.,
Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C.,
Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T.,
Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E.,
Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W.,
Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K.,
Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S.,
Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A.,
Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S.,
Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M.,
Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y.,
Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M.,
Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E.,
Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R.,
Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
Mewes H.-W., Zollner A., Zaccaria P.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
Nature 387:75-78(1997).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[5]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[6]
SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=15356266; DOI=10.1091/mbc.E04-05-0411;
Trautwein M., Dengjel J., Schirle M., Spang A.;
"Arf1p provides an unexpected link between COPI vesicles and mRNA in
Saccharomyces cerevisiae.";
Mol. Biol. Cell 15:5021-5037(2004).
[7]
FUNCTION.
PubMed=16135527; DOI=10.1091/mbc.E05-07-0678;
Altmann K., Westermann B.;
"Role of essential genes in mitochondrial morphogenesis in
Saccharomyces cerevisiae.";
Mol. Biol. Cell 16:5410-5417(2005).
[8]
MUTAGENESIS OF 334-ASP--ASP-336.
PubMed=17954604; DOI=10.1083/jcb.200704142;
Michelsen K., Schmid V., Metz J., Heusser K., Liebel U., Schwede T.,
Spang A., Schwappach B.;
"Novel cargo-binding site in the beta and delta subunits of
coatomer.";
J. Cell Biol. 179:209-217(2007).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181 AND SER-540, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
-!- FUNCTION: The coatomer is a cytosolic protein complex that binds
to dilysine motifs and reversibly associates with Golgi non-
clathrin-coated vesicles, which further mediate biosynthetic
protein transport from the ER, via the Golgi up to the trans Golgi
network. Coatomer complex is required for budding from Golgi
membranes, and is essential for the retrograde Golgi-to-ER
transport of dilysine-tagged proteins. Required for mitochondrial
morphology. {ECO:0000269|PubMed:16135527,
ECO:0000269|PubMed:7929113}.
-!- SUBUNIT: Oligomeric complex that consists of at least the alpha,
beta, beta', gamma, delta, epsilon and zeta subunits. The complex
interacts with ARF1 and PAB1. {ECO:0000269|PubMed:15356266}.
-!- INTERACTION:
P53622:COP1; NbExp=38; IntAct=EBI-4869, EBI-4860;
Q04651:ERV41; NbExp=3; IntAct=EBI-4869, EBI-27850;
P38682:GLO3; NbExp=4; IntAct=EBI-4869, EBI-7679;
P43621:RET2; NbExp=16; IntAct=EBI-4869, EBI-4876;
P53600:RET3; NbExp=3; IntAct=EBI-4869, EBI-4905;
P32074:SEC21; NbExp=3; IntAct=EBI-4869, EBI-4891;
P41811:SEC27; NbExp=16; IntAct=EBI-4869, EBI-4898;
P40509:SEC28; NbExp=17; IntAct=EBI-4869, EBI-4884;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus
membrane {ECO:0000269|PubMed:14562095}; Peripheral membrane
protein {ECO:0000269|PubMed:14562095}; Cytoplasmic side
{ECO:0000269|PubMed:14562095}. Cytoplasmic vesicle, COPI-coated
vesicle membrane {ECO:0000250}; Peripheral membrane protein
{ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=The coatomer
is cytoplasmic or polymerized on the cytoplasmic side of the
Golgi, as well as on the vesicles/buds originating from it.
{ECO:0000250}.
-!- PTM: The N-terminus is blocked.
-!- DISRUPTION PHENOTYPE: Causes a block in ER to Golgi transport.
Exhibits exaggerated ER structures displaying interconnected
networks of ER cisternae. Cells arrest at all stages of the
vegetative cycle. {ECO:0000269|PubMed:7929113}.
-!- MISCELLANEOUS: Present with 26000 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U11236; AAA61710.1; -; Genomic_DNA.
EMBL; Z49701; CAA89724.1; -; Genomic_DNA.
EMBL; BK006938; DAA12079.1; -; Genomic_DNA.
PIR; S54534; S54534.
RefSeq; NP_010524.3; NM_001180546.3.
ProteinModelPortal; P41810; -.
BioGrid; 32289; 642.
DIP; DIP-6467N; -.
IntAct; P41810; 42.
MINT; P41810; -.
STRING; 4932.YDR238C; -.
iPTMnet; P41810; -.
MaxQB; P41810; -.
PaxDb; P41810; -.
PRIDE; P41810; -.
EnsemblFungi; YDR238C; YDR238C; YDR238C.
GeneID; 851824; -.
KEGG; sce:YDR238C; -.
EuPathDB; FungiDB:YDR238C; -.
SGD; S000002646; SEC26.
GeneTree; ENSGT00390000005270; -.
HOGENOM; HOG000207417; -.
InParanoid; P41810; -.
KO; K17301; -.
OMA; QCGFMAA; -.
OrthoDB; EOG092C0QZM; -.
BioCyc; YEAST:G3O-29813-MONOMER; -.
Reactome; R-SCE-6798695; Neutrophil degranulation.
Reactome; R-SCE-6807878; COPI-mediated anterograde transport.
Reactome; R-SCE-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
PRO; PR:P41810; -.
Proteomes; UP000002311; Chromosome IV.
GO; GO:0030135; C:coated vesicle; ISS:SGD.
GO; GO:0030126; C:COPI vesicle coat; IGI:SGD.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; IMP:SGD.
GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IBA:GO_Central.
GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to ER; IBA:GO_Central.
Gene3D; 1.25.10.10; -; 1.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR000225; Armadillo.
InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
InterPro; IPR011710; Coatomer_bsu_C.
InterPro; IPR016460; COPB1.
InterPro; IPR029446; COPB1_appendage_platform_dom.
PANTHER; PTHR10635; PTHR10635; 1.
Pfam; PF01602; Adaptin_N; 1.
Pfam; PF07718; Coatamer_beta_C; 1.
Pfam; PF14806; Coatomer_b_Cpla; 1.
PIRSF; PIRSF005727; Coatomer_beta_subunit; 1.
SMART; SM00185; ARM; 1.
SUPFAM; SSF48371; SSF48371; 2.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Cytoplasmic vesicle;
Direct protein sequencing; ER-Golgi transport; Golgi apparatus;
Membrane; Phosphoprotein; Protein transport; Reference proteome;
Repeat; Transport.
CHAIN 1 973 Coatomer subunit beta.
/FTId=PRO_0000193839.
REPEAT 98 133 HEAT 1.
REPEAT 134 170 HEAT 2.
REPEAT 279 317 HEAT 3.
REPEAT 318 354 HEAT 4.
MOD_RES 181 181 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
MOD_RES 540 540 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
MUTAGEN 334 336 DLD->NAN: Loses ability to recognize
arginine (R)-based ER localization
signals in proteins. Recognition of C-
terminal di-lysine signals present in
proteins is unimpaired.
{ECO:0000269|PubMed:17954604}.
CONFLICT 412 412 D -> E (in Ref. 1; AAA61710).
{ECO:0000305}.
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


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