BUD8_YEAST
ID BUD8_YEAST Reviewed; 603 AA.
AC P41698; D6VYZ1; Q06482;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Bud site selection protein 8;
GN Name=BUD8; OrderedLocusNames=YLR353W; ORFNames=L9638.3;
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], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11514631; DOI=10.1091/mbc.12.8.2497;
RA Harkins H.A., Page N., Schenkman L.R., De Virgilio C., Shaw S., Bussey H.,
RA Pringle J.R.;
RT "Bud8p and Bud9p, proteins that may mark the sites for bipolar budding in
RT yeast.";
RL Mol. Biol. Cell 12:2497-2518(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [3]
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 [4]
RP IDENTIFICATION BY 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 [5]
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).
CC -!- FUNCTION: May be involved in positioning the distal bud pole signal.
CC {ECO:0000269|PubMed:11514631}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11514631};
CC Multi-pass membrane protein {ECO:0000269|PubMed:11514631}. Note=Found
CC at presumptive bud sites, bud tips, and the distal poles of daughter
CC cells.
CC -!- PTM: N- and O-glycosylated.
CC -!- SIMILARITY: To yeast BUD9. {ECO:0000305}.
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DR EMBL; L37016; AAA64518.1; -; Genomic_DNA.
DR EMBL; U19102; AAB67749.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09657.1; -; Genomic_DNA.
DR PIR; S51461; S51461.
DR RefSeq; NP_013457.1; NM_001182242.1.
DR AlphaFoldDB; P41698; -.
DR SMR; P41698; -.
DR BioGRID; 31615; 106.
DR DIP; DIP-4471N; -.
DR STRING; 4932.YLR353W; -.
DR iPTMnet; P41698; -.
DR MaxQB; P41698; -.
DR PaxDb; P41698; -.
DR PRIDE; P41698; -.
DR EnsemblFungi; YLR353W_mRNA; YLR353W; YLR353W.
DR GeneID; 851067; -.
DR KEGG; sce:YLR353W; -.
DR SGD; S000004345; BUD8.
DR VEuPathDB; FungiDB:YLR353W; -.
DR eggNOG; ENOG502S1HD; Eukaryota.
DR HOGENOM; CLU_037885_0_0_1; -.
DR InParanoid; P41698; -.
DR OMA; HIGHNNE; -.
DR BioCyc; YEAST:G3O-32427-MON; -.
DR PRO; PR:P41698; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P41698; protein.
DR GO; GO:0005934; C:cellular bud tip; IDA:SGD.
DR GO; GO:0000131; C:incipient cellular bud site; IDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IMP:SGD.
DR GO; GO:0000282; P:cellular bud site selection; IMP:SGD.
DR GO; GO:0007124; P:pseudohyphal growth; IMP:SGD.
PE 1: Evidence at protein level;
KW Cell cycle; Cell membrane; Glycoprotein; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..603
FT /note="Bud site selection protein 8"
FT /id="PRO_0000065020"
FT TOPO_DOM 1..515
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 516..536
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 537..577
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 578..598
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 599..603
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 83..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 190..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..359
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..402
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..454
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..479
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 240
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 333
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 396
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 423
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 140
FT /note="R -> W (in Ref. 1; AAA64518)"
FT /evidence="ECO:0000305"
FT CONFLICT 145
FT /note="V -> M (in Ref. 1; AAA64518)"
FT /evidence="ECO:0000305"
FT CONFLICT 221
FT /note="Y -> C (in Ref. 1; AAA64518)"
FT /evidence="ECO:0000305"
FT CONFLICT 350
FT /note="S -> N (in Ref. 1; AAA64518)"
FT /evidence="ECO:0000305"
FT CONFLICT 354
FT /note="T -> M (in Ref. 1; AAA64518)"
FT /evidence="ECO:0000305"
FT CONFLICT 422
FT /note="Missing (in Ref. 1; AAA64518)"
FT /evidence="ECO:0000305"
FT CONFLICT 602
FT /note="R -> L (in Ref. 1; AAA64518)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 603 AA; 66289 MW; 83F8843CA476E6C4 CRC64;
MIQSDEDNLD SSETTASTSY SGTSSVSSRL QLRTSLFFEN LNGAHGNPDA ETEMATVAYE
TTSRGQGFAV YINNERFSQI MGASTSSSSS SNSSSITQFH DTQDNNIPSN TTVRPTSLRR
DNEDTVPLRN VTPSQNAAVR PERAVNSPSS QRLSCALTIS TSVLMGEDVE GSPIEQEHSR
VVSSLYSSLA NRGNDESKNG TPPRPTSIEP NETTEHSFFS YHYDDTLEPD VEEAVRLTKN
KTSNVNFISS TGSKGEGETE DEVIDQYEPV NESKFIPHKL KIPEKAGSIK SSTSDDSHSP
GAPGTSARKI KIPQSPSLIG NILIPSHNSD SSNESSPKDH IGHNNEEKFS SKSTRKPSTS
LEEEGPPIGL PSIPVLRSVS GPSKWTKTPL RLESGNSTKS DPFSRYEGHK TPSPLTKMNK
KKNKTLPEHG QPLVLAPIKS QSSESDTGQN SIIEKPARSI RRKQQEKTDN RKEDRHDAEN
IDLEARMPIQ HIDTASIHSF DSGQNGFRDV YSIENIIVIL LCCSIVPPLF FIIGCSSRRK
LVSDYRLMRL LMNKEHRAAL LQGFIWDVDL RWFRMFCLIL GAAETVIVMA GIAIGFGVGI
TRE
