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

 COPB2_YEAST             Reviewed;         889 AA.
P41811; D6VU12;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 1.
18-JUL-2018, entry version 175.
RecName: Full=Coatomer subunit beta';
AltName: Full=Beta'-coat protein;
Short=Beta'-COP;
Name=SEC27; OrderedLocusNames=YGL137W; ORFNames=G2827;
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], AND PROTEIN SEQUENCE OF 1-11.
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 [GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
PubMed=8840506;
DOI=10.1002/(SICI)1097-0061(199607)12:9<887::AID-YEA971>3.0.CO;2-D;
Escribano V., Eraso P., Portillo F., Mazon M.J.;
"Sequence analysis of a 14.6 kb DNA fragment of Saccharomyces
cerevisiae chromosome VII reveals SEC27, SSM1b, a putative S-
adenosylmethionine-dependent enzyme and six new open reading frames.";
Yeast 12:887-892(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169869;
Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M.,
Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J.,
Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E.,
Clemente M.L., Coblenz A., Coglievina M., Coissac E., Defoor E.,
Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B.,
Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L.,
Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M.,
Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M.,
Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B.,
Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W.,
Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A.,
Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S.,
Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L.,
Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S.,
Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J.,
Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M.,
Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B.,
Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J.,
Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M.,
van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M.,
Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H.,
Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M.,
Zollner A., Kleine K.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
Nature 387:81-84(1997).
[4]
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).
[5]
PROTEIN SEQUENCE OF 1-27.
STRAIN=ATCC 208279 / BJ926;
PubMed=8405452; DOI=10.1016/0014-5793(93)80487-F;
Harter C., Draken E., Lottspeich F., Wieland F.T.;
"Yeast coatomer contains a subunit homologous to mammalian beta'-
COP.";
FEBS Lett. 332:71-73(1993).
[6]
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).
[7]
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).
[8]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH VPS27.
PubMed=17101773; DOI=10.1128/MCB.00577-06;
Gabriely G., Kama R., Gerst J.E.;
"Involvement of specific COPI subunits in protein sorting from the
late endosome to the vacuole in yeast.";
Mol. Cell. Biol. 27:526-540(2007).
[9]
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).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
-!- 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.
{ECO:0000269|PubMed:17101773}.
-!- SUBUNIT: Oligomeric complex that consists of at least the alpha,
beta, beta', gamma, delta, epsilon and zeta subunits. Interacts
with the ESCRT-0 subunit VPS27. {ECO:0000269|PubMed:17101773}.
-!- INTERACTION:
P15790:CKA1; NbExp=2; IntAct=EBI-4898, EBI-9533;
P53622:COP1; NbExp=82; IntAct=EBI-4898, EBI-4860;
P53849:GIS2; NbExp=2; IntAct=EBI-4898, EBI-29244;
P32347:HEM12; NbExp=2; IntAct=EBI-4898, EBI-5711;
P02829:HSP82; NbExp=2; IntAct=EBI-4898, EBI-8659;
Q06147:LCB5; NbExp=2; IntAct=EBI-4898, EBI-2069549;
P32829:MRE11; NbExp=2; IntAct=EBI-4898, EBI-11255;
Q12451:OSH2; NbExp=3; IntAct=EBI-4898, EBI-12621;
P43621:RET2; NbExp=19; IntAct=EBI-4898, EBI-4876;
P53600:RET3; NbExp=6; IntAct=EBI-4898, EBI-4905;
P32074:SEC21; NbExp=11; IntAct=EBI-4898, EBI-4891;
P41810:SEC26; NbExp=16; IntAct=EBI-4898, EBI-4869;
P40509:SEC28; NbExp=28; IntAct=EBI-4898, EBI-4884;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus
membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250};
Cytoplasmic side {ECO:0000250}. 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}.
-!- MISCELLANEOUS: Present with 129000 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the WD repeat COPB2 family. {ECO:0000305}.
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EMBL; U11237; AAA61711.1; -; Genomic_DNA.
EMBL; X92670; CAA63359.1; -; Genomic_DNA.
EMBL; Z72659; CAA96848.1; -; Genomic_DNA.
EMBL; BK006941; DAA07973.1; -; Genomic_DNA.
PIR; B55123; B55123.
RefSeq; NP_011378.1; NM_001181002.1.
PDB; 2YNN; X-ray; 1.78 A; A=1-304.
PDB; 2YNO; X-ray; 1.80 A; A/B=1-304.
PDB; 2YNP; X-ray; 2.96 A; A=1-604.
PDB; 4J73; X-ray; 1.44 A; A=1-301.
PDB; 4J77; X-ray; 1.76 A; A/B=1-301.
PDB; 4J78; X-ray; 1.48 A; A=1-301.
PDB; 4J79; X-ray; 1.56 A; A=1-300.
PDB; 4J81; X-ray; 1.74 A; A/B=1-301.
PDB; 4J82; X-ray; 1.46 A; A/B=1-301.
PDB; 4J84; X-ray; 1.47 A; A/B=1-301.
PDB; 4J86; X-ray; 1.48 A; A/B=1-301.
PDBsum; 2YNN; -.
PDBsum; 2YNO; -.
PDBsum; 2YNP; -.
PDBsum; 4J73; -.
PDBsum; 4J77; -.
PDBsum; 4J78; -.
PDBsum; 4J79; -.
PDBsum; 4J81; -.
PDBsum; 4J82; -.
PDBsum; 4J84; -.
PDBsum; 4J86; -.
ProteinModelPortal; P41811; -.
SMR; P41811; -.
BioGrid; 33115; 654.
ComplexPortal; CPX-1652; COPI vesicle coat complex.
DIP; DIP-6468N; -.
IntAct; P41811; 178.
MINT; P41811; -.
STRING; 4932.YGL137W; -.
iPTMnet; P41811; -.
MaxQB; P41811; -.
PaxDb; P41811; -.
PRIDE; P41811; -.
EnsemblFungi; YGL137W; YGL137W; YGL137W.
GeneID; 852740; -.
KEGG; sce:YGL137W; -.
EuPathDB; FungiDB:YGL137W; -.
SGD; S000003105; SEC27.
GeneTree; ENSGT00900000141083; -.
HOGENOM; HOG000163444; -.
KO; K17302; -.
OMA; NHETQTL; -.
OrthoDB; EOG092C10HM; -.
BioCyc; YEAST:G3O-30632-MONOMER; -.
Reactome; R-SCE-6807878; COPI-mediated anterograde transport.
Reactome; R-SCE-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
PRO; PR:P41811; -.
Proteomes; UP000002311; Chromosome VII.
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:0043130; F:ubiquitin binding; IDA:SGD.
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; IBA:GO_Central.
GO; GO:0032511; P:late endosome to vacuole transport via multivesicular body sorting pathway; IMP:SGD.
GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to ER; IMP:SGD.
Gene3D; 2.130.10.10; -; 1.
InterPro; IPR006692; Coatomer_WD-assoc_reg.
InterPro; IPR016453; COPB2.
InterPro; IPR020472; G-protein_beta_WD-40_rep.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR019775; WD40_repeat_CS.
InterPro; IPR017986; WD40_repeat_dom.
InterPro; IPR036322; WD40_repeat_dom_sf.
Pfam; PF04053; Coatomer_WDAD; 1.
Pfam; PF00400; WD40; 4.
PIRSF; PIRSF005567; Coatomer_beta'_subunit; 1.
PRINTS; PR00320; GPROTEINBRPT.
SMART; SM00320; WD40; 7.
SUPFAM; SSF50978; SSF50978; 4.
PROSITE; PS00678; WD_REPEATS_1; 1.
PROSITE; PS50082; WD_REPEATS_2; 5.
PROSITE; PS50294; WD_REPEATS_REGION; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Cytoplasmic vesicle;
Direct protein sequencing; ER-Golgi transport; Golgi apparatus;
Membrane; Phosphoprotein; Protein transport; Reference proteome;
Repeat; Transport; WD repeat.
CHAIN 1 889 Coatomer subunit beta'.
/FTId=PRO_0000050918.
REPEAT 11 41 WD 1.
REPEAT 53 83 WD 2.
REPEAT 95 125 WD 3.
REPEAT 138 169 WD 4.
REPEAT 182 214 WD 5.
REPEAT 226 256 WD 6.
MOD_RES 326 326 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
STRAND 6 12 {ECO:0000244|PDB:4J73}.
STRAND 16 21 {ECO:0000244|PDB:4J73}.
STRAND 23 32 {ECO:0000244|PDB:4J73}.
STRAND 35 41 {ECO:0000244|PDB:4J73}.
TURN 42 45 {ECO:0000244|PDB:4J73}.
STRAND 46 52 {ECO:0000244|PDB:4J73}.
STRAND 58 64 {ECO:0000244|PDB:4J73}.
HELIX 65 67 {ECO:0000244|PDB:4J73}.
STRAND 69 74 {ECO:0000244|PDB:4J73}.
STRAND 77 83 {ECO:0000244|PDB:4J73}.
TURN 84 86 {ECO:0000244|PDB:4J73}.
STRAND 89 94 {ECO:0000244|PDB:4J73}.
STRAND 100 105 {ECO:0000244|PDB:4J73}.
STRAND 107 116 {ECO:0000244|PDB:4J73}.
STRAND 121 125 {ECO:0000244|PDB:4J73}.
TURN 126 130 {ECO:0000244|PDB:4J73}.
STRAND 132 136 {ECO:0000244|PDB:4J73}.
STRAND 143 148 {ECO:0000244|PDB:4J73}.
STRAND 155 160 {ECO:0000244|PDB:4J73}.
STRAND 163 169 {ECO:0000244|PDB:4J73}.
STRAND 176 180 {ECO:0000244|PDB:4J73}.
STRAND 189 192 {ECO:0000244|PDB:4J73}.
STRAND 200 204 {ECO:0000244|PDB:4J73}.
STRAND 208 214 {ECO:0000244|PDB:4J73}.
TURN 215 217 {ECO:0000244|PDB:4J73}.
STRAND 220 225 {ECO:0000244|PDB:4J73}.
STRAND 231 236 {ECO:0000244|PDB:4J73}.
STRAND 238 247 {ECO:0000244|PDB:4J73}.
STRAND 252 256 {ECO:0000244|PDB:4J73}.
TURN 257 259 {ECO:0000244|PDB:4J73}.
STRAND 262 266 {ECO:0000244|PDB:4J73}.
STRAND 269 278 {ECO:0000244|PDB:4J73}.
HELIX 283 285 {ECO:0000244|PDB:4J82}.
STRAND 287 291 {ECO:0000244|PDB:4J73}.
STRAND 294 299 {ECO:0000244|PDB:4J73}.
STRAND 313 318 {ECO:0000244|PDB:2YNP}.
STRAND 321 323 {ECO:0000244|PDB:2YNP}.
STRAND 327 332 {ECO:0000244|PDB:2YNP}.
STRAND 341 343 {ECO:0000244|PDB:2YNP}.
STRAND 350 354 {ECO:0000244|PDB:2YNP}.
STRAND 360 364 {ECO:0000244|PDB:2YNP}.
STRAND 368 375 {ECO:0000244|PDB:2YNP}.
STRAND 378 383 {ECO:0000244|PDB:2YNP}.
TURN 384 386 {ECO:0000244|PDB:2YNP}.
STRAND 389 394 {ECO:0000244|PDB:2YNP}.
STRAND 396 400 {ECO:0000244|PDB:2YNP}.
STRAND 404 410 {ECO:0000244|PDB:2YNP}.
STRAND 416 420 {ECO:0000244|PDB:2YNP}.
STRAND 423 427 {ECO:0000244|PDB:2YNP}.
STRAND 438 440 {ECO:0000244|PDB:2YNP}.
STRAND 442 448 {ECO:0000244|PDB:2YNP}.
STRAND 453 456 {ECO:0000244|PDB:2YNP}.
TURN 458 460 {ECO:0000244|PDB:2YNP}.
STRAND 463 467 {ECO:0000244|PDB:2YNP}.
STRAND 471 476 {ECO:0000244|PDB:2YNP}.
STRAND 480 487 {ECO:0000244|PDB:2YNP}.
TURN 490 493 {ECO:0000244|PDB:2YNP}.
STRAND 496 502 {ECO:0000244|PDB:2YNP}.
HELIX 504 512 {ECO:0000244|PDB:2YNP}.
STRAND 518 520 {ECO:0000244|PDB:2YNP}.
HELIX 523 525 {ECO:0000244|PDB:2YNP}.
STRAND 526 532 {ECO:0000244|PDB:2YNP}.
STRAND 537 542 {ECO:0000244|PDB:2YNP}.
STRAND 545 549 {ECO:0000244|PDB:2YNP}.
STRAND 554 558 {ECO:0000244|PDB:2YNP}.
STRAND 563 568 {ECO:0000244|PDB:2YNP}.
STRAND 573 579 {ECO:0000244|PDB:2YNP}.
TURN 580 583 {ECO:0000244|PDB:2YNP}.
STRAND 584 589 {ECO:0000244|PDB:2YNP}.
STRAND 594 598 {ECO:0000244|PDB:2YNP}.
SEQUENCE 889 AA; 99445 MW; 6A5E50BBEB02CB58 CRC64;
MKLDIKKTFS NRSDRVKGID FHPTEPWVLT TLYSGRVELW NYETQVEVRS IQVTETPVRA
GKFIARKNWI IVGSDDFRIR VFNYNTGEKV VDFEAHPDYI RSIAVHPTKP YVLSGSDDLT
VKLWNWENNW ALEQTFEGHE HFVMCVAFNP KDPSTFASGC LDRTVKVWSL GQSTPNFTLT
TGQERGVNYV DYYPLPDKPY MITASDDLTI KIWDYQTKSC VATLEGHMSN VSFAVFHPTL
PIIISGSEDG TLKIWNSSTY KVEKTLNVGL ERSWCIATHP TGRKNYIASG FDNGFTVLSL
GNDEPTLSLD PVGKLVWSGG KNAAASDIFT AVIRGNEEVE QDEPLSLQTK ELGSVDVFPQ
SLAHSPNGRF VTVVGDGEYV IYTALAWRNK AFGKCQDFVW GPDSNSYALI DETGQIKYYK
NFKEVTSWSV PMHSAIDRLF SGALLGVKSD GFVYFFDWDN GTLVRRIDVN AKDVIWSDNG
ELVMIVNTNS NGDEASGYTL LFNKDAYLEA ANNGNIDDSE GVDEAFDVLY ELSESITSGK
WVGDVFIFTT ATNRLNYFVG GKTYNLAHYT KEMYLLGYLA RDNKVYLADR EVHVYGYEIS
LEVLEFQTLT LRGEIEEAIE NVLPNVEGKD SLTKIARFLE GQEYYEEALN ISPDQDQKFE
LALKVGQLTL ARDLLTDESA EMKWRALGDA SLQRFNFKLA VEAFTNAHDL ESLFLLHSSF
NNKEGLVTLA KDAERAGKFN LAFNAYWIAG DIQGAKDLLI KSQRFSEAAF LGSTYGLGDD
AVNDIVTKWK ENLILNGKNT VSERVCGAEG LPGSSSSGDA QPLIDLDSTP APEQADENKE
AEVEDSEFKE SNSEAVEAEK KEEEAPQQQQ SEQQPEQGEA VPEPVEEES


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GENTAUR France SARL
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Tel 01 43 25 01 50

Fax 01 43 25 01 60
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BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

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GENTAUR GmbH
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Support Karolina Elandt
Tel: 0035929830070
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San Jose, CA 95123
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Tel (408) 780-0908,
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Genprice Inc, Invoices and accounting
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GENTAUR Poland Sp. z o.o.


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