BUD5_YEAST
ID BUD5_YEAST Reviewed; 642 AA.
AC P25300; D6VR48; Q06729;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Bud site selection protein 5;
GN Name=BUD5; OrderedLocusNames=YCR038C; ORFNames=YCR38C, YCR526;
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].
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=1789011; DOI=10.1002/yea.320070815;
RA Jacquet M., Buhler J.-M., Iborra F., Francingues-Gaillard M.-C.,
RA Soustelle C.;
RT "The MAT locus revisited within a 9.8 kb fragment of chromosome III
RT containing BUD5 and two new open reading frames.";
RL Yeast 7:881-888(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1905982; DOI=10.1016/0092-8674(91)90017-s;
RA Powers S., Gonzales E., Christensen T., Cubert J., Broek D.;
RT "Functional cloning of BUD5, a CDC25-related gene from S. cerevisiae that
RT can suppress a dominant-negative RAS2 mutant.";
RL Cell 65:1225-1231(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1574125; DOI=10.1038/357038a0;
RA Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA Sgouros J.G.;
RT "The complete DNA sequence of yeast chromosome III.";
RL Nature 357:38-46(1992).
RN [4]
RP SEQUENCE REVISION TO 110; 401; 481 AND N-TERMINUS.
RA Valles G., Volckaerts G.;
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 105-642.
RC STRAIN=SP1;
RX PubMed=1905981; DOI=10.1016/0092-8674(91)90016-r;
RA Chant J., Corrado K., Pringle J.R., Herskowitz I.;
RT "Yeast BUD5, encoding a putative GDP-GTP exchange factor, is necessary for
RT bud site selection and interacts with bud formation gene BEM1.";
RL Cell 65:1213-1224(1991).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 287-642.
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=1964349; DOI=10.1002/yea.320060609;
RA Thierry A., Fairhead C., Dujon B.;
RT "The complete sequence of the 8.2 kb segment left of MAT on chromosome III
RT reveals five ORFs, including a gene for a yeast ribokinase.";
RL Yeast 6:521-534(1990).
RN [8]
RP FUNCTION.
RX PubMed=8234337; DOI=10.1073/pnas.90.21.9926;
RA Bender A.;
RT "Genetic evidence for the roles of the bud-site-selection genes BUD5 and
RT BUD2 in control of the Rsr1p (Bud1p) GTPase in yeast.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:9926-9929(1993).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11378394; DOI=10.1016/s0960-9822(01)00230-5;
RA Marston A.L., Chen T., Yang M.C., Belhumeur P., Chant J.;
RT "A localized GTPase exchange factor, Bud5, determines the orientation of
RT division axes in yeast.";
RL Curr. Biol. 11:803-807(2001).
RN [10]
RP FUNCTION, AND INTERACTION WITH GSP1.
RX PubMed=11589573; DOI=10.1007/s004380100511;
RA Clement M., Lavallee F., Barbes-Morin G., de Repentigny L., Belhumeur P.;
RT "Overexpression of Bud5p can suppress mutations in the Gsp1p guanine
RT nucleotide exchange factor Prp20p in Saccharomyces cerevisiae.";
RL Mol. Genet. Genomics 266:20-27(2001).
RN [11]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH AXL2.
RX PubMed=11313501; DOI=10.1126/science.1060360;
RA Kang P.J., Sanson A., Lee B., Park H.-O.;
RT "A GDP/GTP exchange factor involved in linking a spatial landmark to cell
RT polarity.";
RL Science 292:1376-1378(2001).
RN [12]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH AXL1.
RX PubMed=12176366; DOI=10.1016/s0960-9822(02)01042-4;
RA Lord M., Inose F., Hiroko T., Hata T., Fujita A., Chant J.;
RT "Subcellular localization of Axl1, the cell type-specific regulator of
RT polarity.";
RL Curr. Biol. 12:1347-1352(2002).
RN [13]
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 [14]
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).
CC -!- FUNCTION: GDP-GTP exchange factor (GEF) for the small GTPase BUD1/RSR1.
CC Regulates the activity of BUD1 together with BUD2 which is a GTPase-
CC activating protein (GAP) of BUD1. Required to produce both the axial
CC and bipolar patterns of bud site selection. Determines the orientation
CC of division axis. Overexpression can suppress mutations in PRP20 which
CC is the GEF for GSP1. May be a cytoplasmic GEF for GSP1. Might also act
CC on the Ras-like protein CDC42. Appears to bind to Ras proteins but not
CC to activate them. {ECO:0000269|PubMed:11378394,
CC ECO:0000269|PubMed:11589573, ECO:0000269|PubMed:8234337}.
CC -!- SUBUNIT: Interacts with AXL2, BEM1, GSP1 and in haploid cells with
CC AXL1. {ECO:0000269|PubMed:11313501, ECO:0000269|PubMed:11589573,
CC ECO:0000269|PubMed:12176366}.
CC -!- INTERACTION:
CC P25300; P38928: AXL2; NbExp=2; IntAct=EBI-3853, EBI-3397;
CC P25300; P32835: GSP1; NbExp=2; IntAct=EBI-3853, EBI-7926;
CC -!- SUBCELLULAR LOCATION: Bud neck. Cytoplasm, cell cortex. Note=In haploid
CC cells, forms double rings that encircle the mother-bud neck and split
CC upon cytokinesis, each progeny cell inheriting BUD5 at the axial
CC division remnant. In diploid cells, localizes to the poles of the cell.
CC -!- MISCELLANEOUS: Present with 2110 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA34462.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA45334.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X63853; CAA45334.1; ALT_FRAME; Genomic_DNA.
DR EMBL; M68938; AAA34462.1; ALT_FRAME; Genomic_DNA.
DR EMBL; X59720; CAA42305.2; -; Genomic_DNA.
DR EMBL; M63552; AAA34460.1; -; Genomic_DNA.
DR EMBL; X56909; CAA40230.1; -; Genomic_DNA.
DR EMBL; BK006937; DAA07517.1; -; Genomic_DNA.
DR PIR; S19450; BWBYD5.
DR RefSeq; NP_009967.2; NM_001178752.1.
DR AlphaFoldDB; P25300; -.
DR BioGRID; 31021; 19.
DR DIP; DIP-4991N; -.
DR IntAct; P25300; 8.
DR MINT; P25300; -.
DR STRING; 4932.YCR038C; -.
DR iPTMnet; P25300; -.
DR PaxDb; P25300; -.
DR EnsemblFungi; YCR038C_mRNA; YCR038C; YCR038C.
DR GeneID; 850405; -.
DR KEGG; sce:YCR038C; -.
DR SGD; S000000634; BUD5.
DR VEuPathDB; FungiDB:YCR038C; -.
DR eggNOG; KOG3417; Eukaryota.
DR HOGENOM; CLU_448459_0_0_1; -.
DR InParanoid; P25300; -.
DR OMA; THTISYW; -.
DR BioCyc; YEAST:G3O-29350-MON; -.
DR Reactome; R-SCE-354192; Integrin signaling.
DR Reactome; R-SCE-392517; Rap1 signalling.
DR Reactome; R-SCE-416482; G alpha (12/13) signalling events.
DR Reactome; R-SCE-8980692; RHOA GTPase cycle.
DR Reactome; R-SCE-9013148; CDC42 GTPase cycle.
DR PRO; PR:P25300; -.
DR Proteomes; UP000002311; Chromosome III.
DR RNAct; P25300; protein.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0000131; C:incipient cellular bud site; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IGI:SGD.
DR GO; GO:0007120; P:axial cellular bud site selection; IMP:SGD.
DR GO; GO:0007121; P:bipolar cellular bud site selection; IMP:SGD.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IBA:GO_Central.
DR GO; GO:0007265; P:Ras protein signal transduction; IBA:GO_Central.
DR CDD; cd00155; RasGEF; 1.
DR Gene3D; 1.10.840.10; -; 1.
DR InterPro; IPR008937; Ras-like_GEF.
DR InterPro; IPR000651; Ras-like_Gua-exchang_fac_N.
DR InterPro; IPR019804; Ras_G-nucl-exch_fac_CS.
DR InterPro; IPR023578; Ras_GEF_dom_sf.
DR InterPro; IPR001895; RASGEF_cat_dom.
DR InterPro; IPR036964; RASGEF_cat_dom_sf.
DR PANTHER; PTHR23113; PTHR23113; 1.
DR Pfam; PF00617; RasGEF; 1.
DR SMART; SM00147; RasGEF; 1.
DR SMART; SM00229; RasGEFN; 1.
DR SUPFAM; SSF48366; SSF48366; 1.
DR PROSITE; PS00720; RASGEF; 1.
DR PROSITE; PS50009; RASGEF_CAT; 1.
DR PROSITE; PS50212; RASGEF_NTER; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Guanine-nucleotide releasing factor; Reference proteome.
FT CHAIN 1..642
FT /note="Bud site selection protein 5"
FT /id="PRO_0000068859"
FT DOMAIN 224..339
FT /note="N-terminal Ras-GEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00135"
FT DOMAIN 412..640
FT /note="Ras-GEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00168"
FT CONFLICT 110
FT /note="R -> P (in Ref. 1; CAA45334)"
FT /evidence="ECO:0000305"
FT CONFLICT 111
FT /note="Missing (in Ref. 2; AAA34462)"
FT /evidence="ECO:0000305"
FT CONFLICT 225
FT /note="V -> D (in Ref. 6; AAA34460)"
FT /evidence="ECO:0000305"
FT CONFLICT 401
FT /note="L -> P (in Ref. 2; AAA34462 and 7; CAA40230)"
FT /evidence="ECO:0000305"
FT CONFLICT 481
FT /note="S -> A (in Ref. 2; AAA34462 and 7; CAA40230)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 642 AA; 75046 MW; 55E688DF5AFAB74F CRC64;
MSPKNKYVYI CVEYIYIYFA KIHKQSTLSS DTTKMFVLID NVLAYLLEQD DLFVTARFAI
QGQIVSRRVN KIHISNITDV LLQQFISHTL PYNDNIVPKK ILDSMRTAVR QLLEATACVS
RECPLVKRSQ DIKRARKRLL SDWYRLGADA NMDAVLLVVN SAWRFLAVWR PFVNSIQHAT
QELYQNIAHY LLHGNVNIQR VTALIQLVMG QDDLLFSMDD VLQEVFRIQL YLNKMLPHNS
HKWQKPSPFD SANLLLNFRD WTTDNALLQE LLLSYPTINK NKHKNHSVPR LIQIWVESYW
QDSETTLKDI LNFWYSHLAE YYEYQELFAD IVQLFINKKR TRQLKIHYIG LTDKEIEENK
PPLDYENLFL QYEIDKTNAN DELCGATDLS DLLFQWKQGE LLEVEAFALN VSPWSLAKTL
TLLESSLYLD IETIEFTRHF KHNDTTIDSV FTLSNQLSSY VLETTLQQTH TISYWLQVAL
SCLYLRNLNS LASIITSLQN HSIERLSLPI DVKSDHLFQR LKVVVHPNNN YNVYRRTIKH
IFHSQLPCVP FTSLLIRDIT FIRDGNDTFT KDGNNVNMQK FNQITKIVAF AQYLQQKQYE
DIHCSNTTAR SLLGAMIKVH TLYNDNKDRA YQVSIAKVPR LT
