BCP1_YEAST
ID BCP1_YEAST Reviewed; 283 AA.
AC Q06338; D6VSY9;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Protein BCP1;
GN Name=BCP1; OrderedLocusNames=YDR361C;
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, AND SUBCELLULAR LOCATION.
RX PubMed=12912920; DOI=10.1093/emboj/cdg397;
RA Audhya A., Emr S.D.;
RT "Regulation of PI4,5P2 synthesis by nuclear-cytoplasmic shuttling of the
RT Mss4 lipid kinase.";
RL EMBO J. 22:4223-4236(2003).
RN [5]
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 [6]
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 [7]
RP PHOSPHORYLATION BY THE PHO85-PCL1 KINASE COMPLEX.
RX PubMed=16330754; DOI=10.1073/pnas.0509080102;
RA Dephoure N., Howson R.W., Blethrow J.D., Shokat K.M., O'Shea E.K.;
RT "Combining chemical genetics and proteomics to identify protein kinase
RT substrates.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:17940-17945(2005).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-205 AND THR-209, AND
RP 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-205, AND IDENTIFICATION BY
RP 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).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-205 AND THR-209, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Involved in nuclear export of the lipid kinase MSS4 and of
CC the 60S ribosomal subunit. May also play a role in directing MSS4 to
CC the plasma membrane. Plays a role in actin cytoskeleton organization
CC and vesicular transport. {ECO:0000269|PubMed:12912920}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12912920}. Nucleus
CC {ECO:0000269|PubMed:12912920}.
CC -!- PTM: Phosphorylated by the PHO85-PCL1 kinase complex.
CC {ECO:0000269|PubMed:16330754}.
CC -!- MISCELLANEOUS: Present with 4590 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the BCP1 family. {ECO:0000305}.
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DR EMBL; U28372; AAB64795.1; -; Genomic_DNA.
DR EMBL; AY557741; AAS56067.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12199.1; -; Genomic_DNA.
DR PIR; S61156; S61156.
DR RefSeq; NP_010648.3; NM_001180669.3.
DR PDB; 7C4H; X-ray; 1.83 A; A/B=1-283.
DR PDBsum; 7C4H; -.
DR AlphaFoldDB; Q06338; -.
DR SMR; Q06338; -.
DR BioGRID; 32416; 152.
DR DIP; DIP-5127N; -.
DR IntAct; Q06338; 11.
DR MINT; Q06338; -.
DR STRING; 4932.YDR361C; -.
DR iPTMnet; Q06338; -.
DR MaxQB; Q06338; -.
DR PaxDb; Q06338; -.
DR PRIDE; Q06338; -.
DR EnsemblFungi; YDR361C_mRNA; YDR361C; YDR361C.
DR GeneID; 851963; -.
DR KEGG; sce:YDR361C; -.
DR SGD; S000002769; BCP1.
DR VEuPathDB; FungiDB:YDR361C; -.
DR eggNOG; KOG3034; Eukaryota.
DR GeneTree; ENSGT00390000000696; -.
DR HOGENOM; CLU_068770_2_1_1; -.
DR InParanoid; Q06338; -.
DR OMA; MYTMLLE; -.
DR BioCyc; YEAST:G3O-29911-MON; -.
DR PRO; PR:Q06338; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q06338; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0006611; P:protein export from nucleus; IMP:SGD.
DR GO; GO:0000055; P:ribosomal large subunit export from nucleus; IMP:SGD.
DR InterPro; IPR025602; BCP1_family.
DR PANTHER; PTHR13261; PTHR13261; 1.
DR Pfam; PF13862; BCCIP; 1.
DR PIRSF; PIRSF028983; BCP1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Nucleus; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..283
FT /note="Protein BCP1"
FT /id="PRO_0000239628"
FT REGION 12..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..44
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 205
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 209
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT TURN 39..42
FT /evidence="ECO:0007829|PDB:7C4H"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:7C4H"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:7C4H"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:7C4H"
FT HELIX 64..79
FT /evidence="ECO:0007829|PDB:7C4H"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:7C4H"
FT HELIX 85..93
FT /evidence="ECO:0007829|PDB:7C4H"
FT STRAND 95..103
FT /evidence="ECO:0007829|PDB:7C4H"
FT STRAND 110..117
FT /evidence="ECO:0007829|PDB:7C4H"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:7C4H"
FT HELIX 125..133
FT /evidence="ECO:0007829|PDB:7C4H"
FT HELIX 135..144
FT /evidence="ECO:0007829|PDB:7C4H"
FT TURN 145..147
FT /evidence="ECO:0007829|PDB:7C4H"
FT STRAND 152..159
FT /evidence="ECO:0007829|PDB:7C4H"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:7C4H"
FT HELIX 168..183
FT /evidence="ECO:0007829|PDB:7C4H"
FT STRAND 190..200
FT /evidence="ECO:0007829|PDB:7C4H"
FT STRAND 231..235
FT /evidence="ECO:0007829|PDB:7C4H"
FT HELIX 238..244
FT /evidence="ECO:0007829|PDB:7C4H"
FT STRAND 246..250
FT /evidence="ECO:0007829|PDB:7C4H"
FT STRAND 257..265
FT /evidence="ECO:0007829|PDB:7C4H"
FT HELIX 266..276
FT /evidence="ECO:0007829|PDB:7C4H"
FT HELIX 279..283
FT /evidence="ECO:0007829|PDB:7C4H"
SQ SEQUENCE 283 AA; 32661 MW; E64F77EF8F9D0DCE CRC64;
MVQAIKLNDL KNRKRKNVEE ENGSDESEID ISSTDSENEE EQNGEEEIVN IDFDFFGGNP
EVDFHALKNL LRQLFGPQES TRIQLSSLAD LILGSPTTTI KTDGKESDPY CFLSFVDFKA
NHLSDYVKYL QKVDMRLSTF FKTMIDSGNK NCALVLSERL INMPPEVVPP LYKITLEDVA
TALGDDKHYD FYIIVTRKYE VNFDTDDDTD SGKRNKNKDE RSKKRVKADE VDYFHEEDRF
FEKYAKIHFE SEAKKGVISS YMILDHEGLV KSIDELETEI STW
