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 27-MAR-2024, entry version 179. 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 SMR; 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; 4932-YCR038C; -. DR PeptideAtlas; P25300; -. DR EnsemblFungi; YCR038C_mRNA; YCR038C; YCR038C. DR GeneID; 850405; -. DR KEGG; sce:YCR038C; -. DR AGR; SGD:S000000634; -. 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 OrthoDB; 68574at2759; -. DR BioCyc; YEAST:G3O-29350-MONOMER; -. DR BioGRID-ORCS; 850405; 0 hits in 10 CRISPR screens. 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:0007265; P:Ras protein signal transduction; IBA:GO_Central. DR CDD; cd00155; RasGEF; 1. DR Gene3D; 1.10.840.10; Ras guanine-nucleotide exchange factors catalytic domain; 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:SF354; BUD SITE SELECTION PROTEIN 5; 1. DR PANTHER; PTHR23113; GUANINE NUCLEOTIDE EXCHANGE FACTOR; 1. DR Pfam; PF00617; RasGEF; 1. DR SMART; SM00147; RasGEF; 1. DR SMART; SM00229; RasGEFN; 1. DR SUPFAM; SSF48366; Ras GEF; 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 //