BFR2_YEAST
ID BFR2_YEAST Reviewed; 534 AA.
AC Q06631; D6VSS8; Q66RD8;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Protein BFR2;
DE AltName: Full=Brefeldin A resistance protein 2;
GN Name=BFR2; OrderedLocusNames=YDR299W;
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 [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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP FUNCTION.
RX PubMed=9472076; DOI=10.1007/s002940050304;
RA Chabane S., Gachet E., Kepes F.;
RT "Over-expression of the yeast BFR2 gene partially suppresses the growth
RT defects induced by Brefeldin A and by four ER-to-Golgi mutations.";
RL Curr. Genet. 33:21-28(1998).
RN [5]
RP INDUCTION.
RX PubMed=9645427; DOI=10.1007/pl00008624;
RA Chabane S., Kepes F.;
RT "Expression of the yeast BFR2 gene is regulated at the transcriptional
RT level and through degradation of its product.";
RL Mol. Gen. Genet. 258:215-221(1998).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT "Assigning function to yeast proteins by integration of technologies.";
RL Mol. Cell 12:1353-1365(2003).
RN [7]
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 [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41; SER-44; SER-366 AND
RP SER-379, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41; SER-44; SER-366; SER-372
RP AND SER-379, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41; SER-44; SER-366; SER-372
RP AND SER-379, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Involved in endoplasmic reticulum to Golgi transport.
CC Involved in a protein-transport step blocked by brefeldin A, which
CC disrupts the Golgi apparatus and its incoming protein flux. May also be
CC involved for mass growth or cell proliferation.
CC {ECO:0000269|PubMed:9472076}.
CC -!- INTERACTION:
CC Q06631; P48234: ENP2; NbExp=13; IntAct=EBI-36432, EBI-23354;
CC Q06631; P20448: HCA4; NbExp=5; IntAct=EBI-36432, EBI-5612;
CC Q06631; P40079: LCP5; NbExp=6; IntAct=EBI-36432, EBI-10103;
CC Q06631; P47083: MPP10; NbExp=8; IntAct=EBI-36432, EBI-11168;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:14562095}.
CC -!- INDUCTION: Up-regulated during cold stress and following nutrient
CC replenishment by dilution of cells fron exhausted to fresh minimal
CC medium. {ECO:0000269|PubMed:9645427}.
CC -!- MISCELLANEOUS: Present with 15400 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the AATF family. {ECO:0000305}.
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DR EMBL; U28374; AAB64735.1; -; Genomic_DNA.
DR EMBL; AY723789; AAU09706.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12138.1; -; Genomic_DNA.
DR PIR; S61185; S61185.
DR RefSeq; NP_010585.3; NM_001180607.3.
DR PDB; 6LQP; EM; 3.20 A; RY=1-534.
DR PDB; 6LQQ; EM; 4.10 A; RY=1-534.
DR PDB; 6LQR; EM; 8.60 A; RY=1-534.
DR PDB; 6LQU; EM; 3.70 A; RY=1-534.
DR PDB; 6LQV; EM; 4.80 A; RY=1-534.
DR PDB; 6ZQB; EM; 3.90 A; JK=1-534.
DR PDB; 6ZQC; EM; 3.80 A; JK=1-534.
DR PDB; 7AJT; EM; 4.60 A; JK=1-534.
DR PDB; 7D63; EM; 12.30 A; RY=1-534.
DR PDBsum; 6LQP; -.
DR PDBsum; 6LQQ; -.
DR PDBsum; 6LQR; -.
DR PDBsum; 6LQU; -.
DR PDBsum; 6LQV; -.
DR PDBsum; 6ZQB; -.
DR PDBsum; 6ZQC; -.
DR PDBsum; 7AJT; -.
DR PDBsum; 7D63; -.
DR AlphaFoldDB; Q06631; -.
DR SMR; Q06631; -.
DR BioGRID; 32351; 142.
DR DIP; DIP-1411N; -.
DR IntAct; Q06631; 78.
DR MINT; Q06631; -.
DR STRING; 4932.YDR299W; -.
DR iPTMnet; Q06631; -.
DR MaxQB; Q06631; -.
DR PaxDb; Q06631; -.
DR PRIDE; Q06631; -.
DR EnsemblFungi; YDR299W_mRNA; YDR299W; YDR299W.
DR GeneID; 851893; -.
DR KEGG; sce:YDR299W; -.
DR SGD; S000002707; BFR2.
DR VEuPathDB; FungiDB:YDR299W; -.
DR eggNOG; KOG2773; Eukaryota.
DR GeneTree; ENSGT00390000000288; -.
DR HOGENOM; CLU_018299_2_2_1; -.
DR InParanoid; Q06631; -.
DR OMA; LINFMAP; -.
DR BioCyc; YEAST:G3O-29860-MON; -.
DR PRO; PR:Q06631; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q06631; protein.
DR GO; GO:0030686; C:90S preribosome; HDA:SGD.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0032040; C:small-subunit processome; IMP:SGD.
DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006364; P:rRNA processing; IMP:SGD.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
DR InterPro; IPR025160; AATF.
DR InterPro; IPR039223; AATF/Bfr2.
DR InterPro; IPR012617; AATF_C.
DR PANTHER; PTHR15565; PTHR15565; 1.
DR Pfam; PF13339; AATF-Che1; 1.
DR Pfam; PF08164; TRAUB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; ER-Golgi transport; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..534
FT /note="Protein BFR2"
FT /id="PRO_0000056634"
FT REGION 27..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 86..161
FT /evidence="ECO:0000255"
FT COMPBIAS 27..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..77
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..138
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 366
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 372
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 379
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT CONFLICT 451
FT /note="K -> R (in Ref. 3; AAU09706)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 534 AA; 61203 MW; AE84AD597C2BBD8B CRC64;
MEKSLADQIS DIAIKPVNKD FDIEDEENAS LFQHNEKNGE SDLSDYGNSN TEETKKAHYL
EVEKSKLRAE KGLELNDPKY TGVKGSRQAL YEEVSENEDE EEEEEEEEEK EEDALSFRTD
SEDEEVEIDE EESDADGGET EEAQQKRHAL SKLIQQETKQ AINKLSQSVQ RDASKGYSIL
QQTKLFDNII DLRIKLQKAV IAANKLPLTT ESWEEAKMDD SEETKRLLKE NEKLFNNLFN
RLINFRIKFQ LGDHITQNEE VAKHKLSKKR SLKELYQETN SLDSELKEYR TAVLNKWSTK
VSSASGNAAL SSNKFKAINL PADVQVENQL SDMSRLMKRT KLNRRNITPL YFQKDCANGR
LPELISPVVK DSVDDNENSD DGLDIPKNYD PRRKDNNAID ITENPYVFDD EDFYRVLLND
LIDKKISNAH NSESAAITIT STNARSNNKL KKNIDTKASK GRKLNYSVQD PIANYEAPIT
SGYKWSDDQI DEFFAGLLGQ RVNFNENEDE EQHARIENDE ELEAVKNDDI QIFG
