STE5_YEAST
ID STE5_YEAST Reviewed; 917 AA.
AC P32917; D6VS89;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 2.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Protein STE5;
GN Name=STE5; Synonyms=NUL3; OrderedLocusNames=YDR103W; ORFNames=YD8557.12;
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].
RX PubMed=8455598; DOI=10.1128/mcb.13.4.2050-2060.1993;
RA Mukai Y., Harashima S., Oshima Y.;
RT "Function of the ste signal transduction pathway for mating pheromones
RT sustains MAT alpha 1 transcription in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 13:2050-2060(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8516289; DOI=10.1073/pnas.90.12.5474;
RA Perlman R., Yablonski D., Simchen G., Levitzki A.;
RT "Cloning of the STE5 gene of Saccharomyces cerevisiae as a suppressor of
RT the mating defect of cdc25 temperature-sensitive mutants.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:5474-5478(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE.
RA Mackay V.L., Mathewes S., Bell L., O'Hara P.J.;
RT "Sequence and characterization of the STE5 gene required for signal
RT transduction and mating in Saccharomyces cerevisiae.";
RL Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DBY939;
RX PubMed=8246877; DOI=10.1007/bf00284675;
RA Leberer E., Dignard D., Harcus D., Hougan L., Whiteway M., Thomas D.Y.;
RT "Cloning of Saccharomyces cerevisiae STE5 as a suppressor of a Ste20
RT protein kinase mutant: structural and functional similarity of Ste5 to
RT Far1.";
RL Mol. Gen. Genet. 241:241-254(1993).
RN [5]
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 [6]
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 [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-329, AND IDENTIFICATION BY
RP 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 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 [10]
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: Component of the pheromone signal transduction pathway. It
CC mediates pheromone signals acting between STE20 and STE11. It is
CC absolutely required for pheromone-induced transcription of FUS1. May
CC play a role in cell-cycle arrest in response to pheromone.
CC -!- INTERACTION:
CC P32917; P11710: FUS1; NbExp=2; IntAct=EBI-18373, EBI-7179;
CC P32917; P16892: FUS3; NbExp=11; IntAct=EBI-18373, EBI-7193;
CC P32917; P23561: STE11; NbExp=8; IntAct=EBI-18373, EBI-18259;
CC P32917; P18851: STE4; NbExp=3; IntAct=EBI-18373, EBI-7390;
CC P32917; P06784: STE7; NbExp=9; IntAct=EBI-18373, EBI-18389;
CC P32917; Q6FPF2: CAGL0J04290g; Xeno; NbExp=2; IntAct=EBI-18373, EBI-8783845;
CC P32917; Q5A1D3: CEK1; Xeno; NbExp=2; IntAct=EBI-18373, EBI-8783371;
CC P32917; Q6CNR3: KLLA0_E10539g; Xeno; NbExp=2; IntAct=EBI-18373, EBI-8785667;
CC P32917; C8V7D1: mpkB; Xeno; NbExp=2; IntAct=EBI-18373, EBI-8783425;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- PTM: May be regulated at the phosphorylation level, and by the mating
CC type of the cell and depends on an intact pheromone-response pathway.
CC -!- MISCELLANEOUS: Present with 1900 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: To yeast FAR1. {ECO:0000305}.
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DR EMBL; D12917; BAA02301.1; -; Genomic_DNA.
DR EMBL; L01620; AAA35108.1; -; Genomic_DNA.
DR EMBL; L23856; AAA35115.1; -; Genomic_DNA.
DR EMBL; L07865; AAA16896.1; -; Unassigned_DNA.
DR EMBL; Z47746; CAA87679.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11949.1; -; Genomic_DNA.
DR PIR; S51254; S51254.
DR RefSeq; NP_010388.1; NM_001180411.1.
DR PDB; 2KGN; NMR; -; A=44-67.
DR PDB; 2L4U; NMR; -; A=44-67.
DR PDB; 3FZE; X-ray; 1.60 A; A=593-786.
DR PDB; 4F2H; X-ray; 3.19 A; A=583-787.
DR PDBsum; 2KGN; -.
DR PDBsum; 2L4U; -.
DR PDBsum; 3FZE; -.
DR PDBsum; 4F2H; -.
DR AlphaFoldDB; P32917; -.
DR BMRB; P32917; -.
DR SMR; P32917; -.
DR BioGRID; 32160; 61.
DR DIP; DIP-858N; -.
DR IntAct; P32917; 19.
DR MINT; P32917; -.
DR STRING; 4932.YDR103W; -.
DR iPTMnet; P32917; -.
DR MaxQB; P32917; -.
DR PaxDb; P32917; -.
DR PRIDE; P32917; -.
DR EnsemblFungi; YDR103W_mRNA; YDR103W; YDR103W.
DR GeneID; 851680; -.
DR KEGG; sce:YDR103W; -.
DR SGD; S000002510; STE5.
DR VEuPathDB; FungiDB:YDR103W; -.
DR eggNOG; ENOG502QQID; Eukaryota.
DR HOGENOM; CLU_013813_0_0_1; -.
DR InParanoid; P32917; -.
DR OMA; SHQECLI; -.
DR BioCyc; YEAST:G3O-29705-MON; -.
DR EvolutionaryTrace; P32917; -.
DR PRO; PR:P32917; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P32917; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0043332; C:mating projection tip; IDA:SGD.
DR GO; GO:0070867; C:mating projection tip membrane; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IMP:SGD.
DR GO; GO:0031681; F:G-protein beta-subunit binding; IPI:SGD.
DR GO; GO:0019900; F:kinase binding; IEA:InterPro.
DR GO; GO:0005078; F:MAP-kinase scaffold activity; IDA:SGD.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:SGD.
DR GO; GO:0001403; P:invasive growth in response to glucose limitation; IMP:SGD.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; IMP:SGD.
DR GO; GO:0000750; P:pheromone-dependent signal transduction involved in conjugation with cellular fusion; IDA:SGD.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:SGD.
DR GO; GO:0010525; P:regulation of transposition, RNA-mediated; IMP:SGD.
DR DisProt; DP01511; -.
DR Gene3D; 3.40.50.11070; -; 1.
DR InterPro; IPR038382; Ste5_C_sf.
DR InterPro; IPR021651; Ste5_Fus-binding.
DR InterPro; IPR021106; Ste5_Fus3-bd_dom.
DR Pfam; PF11610; Ste5; 1.
DR Pfam; PF12194; Ste5_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Pheromone response; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..917
FT /note="Protein STE5"
FT /id="PRO_0000072266"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 58..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 778..821
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 778..792
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 793..821
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT CONFLICT 331..332
FT /note="LG -> W (in Ref. 2; AAA35108)"
FT /evidence="ECO:0000305"
FT CONFLICT 341..343
FT /note="NSI -> TLS (in Ref. 2; AAA35108)"
FT /evidence="ECO:0000305"
FT CONFLICT 821
FT /note="A -> R (in Ref. 1; BAA02301)"
FT /evidence="ECO:0000305"
FT HELIX 45..48
FT /evidence="ECO:0007829|PDB:2KGN"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:2KGN"
FT TURN 52..54
FT /evidence="ECO:0007829|PDB:2KGN"
FT HELIX 55..58
FT /evidence="ECO:0007829|PDB:2KGN"
FT HELIX 59..63
FT /evidence="ECO:0007829|PDB:2KGN"
FT TURN 64..66
FT /evidence="ECO:0007829|PDB:2KGN"
FT HELIX 593..604
FT /evidence="ECO:0007829|PDB:3FZE"
FT STRAND 608..616
FT /evidence="ECO:0007829|PDB:3FZE"
FT HELIX 618..620
FT /evidence="ECO:0007829|PDB:3FZE"
FT STRAND 622..624
FT /evidence="ECO:0007829|PDB:4F2H"
FT HELIX 625..640
FT /evidence="ECO:0007829|PDB:3FZE"
FT STRAND 645..650
FT /evidence="ECO:0007829|PDB:3FZE"
FT STRAND 653..660
FT /evidence="ECO:0007829|PDB:3FZE"
FT HELIX 661..664
FT /evidence="ECO:0007829|PDB:3FZE"
FT HELIX 668..672
FT /evidence="ECO:0007829|PDB:3FZE"
FT HELIX 673..676
FT /evidence="ECO:0007829|PDB:3FZE"
FT HELIX 685..692
FT /evidence="ECO:0007829|PDB:3FZE"
FT STRAND 701..707
FT /evidence="ECO:0007829|PDB:3FZE"
FT TURN 713..715
FT /evidence="ECO:0007829|PDB:3FZE"
FT HELIX 717..719
FT /evidence="ECO:0007829|PDB:3FZE"
FT HELIX 723..725
FT /evidence="ECO:0007829|PDB:3FZE"
FT STRAND 735..741
FT /evidence="ECO:0007829|PDB:3FZE"
FT TURN 748..750
FT /evidence="ECO:0007829|PDB:4F2H"
FT STRAND 755..758
FT /evidence="ECO:0007829|PDB:3FZE"
FT HELIX 760..770
FT /evidence="ECO:0007829|PDB:3FZE"
SQ SEQUENCE 917 AA; 102727 MW; 0435BDA0196B2D6F CRC64;
MMETPTDNIV SPFHNFGSST QYSGTLSRTP NQIIELEKPS TLSPLSRGKK WTEKLARFQR
SSAKKKRFSP SPISSSTFSF SPKSRVTSSN SSGNEDGNLM NTPSTVSTDY LPQHPHRTSS
LPRPNSNLFH ASNSNLSRAN EPPRAENLSD NIPPKVAPFG YPIQRTSIKK SFLNASCTLC
DEPISNRRKG EKIIELACGH LSHQECLIIS FGTTSKADVR ALFPFCTKCK KDTNKAVQCI
PENDELKDIL ISDFLIHKIP DSELSITPQS RFPPYSPLLP PFGLSYTPVE RQTIYSQAPS
LNPNLILAAP PKERNQIPQK KSNYTFLHSP LGHRRIPSGA NSILADTSVA LSANDSISAV
SNSVRAKDDE TKTTLPLLRS YFIQILLNNF QEELQDWRID GDYGLLRLVD KLMISKDGQR
YIQCWCFLFE DAFVIAEVDN DVDVLEIRLK NLEVFTPIAN LRMTTLEASV LKCTLNKQHC
ADLSDLYIVQ NINSDESTTV QKWISGILNQ DFVFNEDNIT STLPILPIIK NFSKDVGNGR
HETSTFLGLI NPNKVVEVGN VHDNDTVIIR RGFTLNSGEC SRQSTVDSIQ SVLTTISSIL
SLKREKPDNL AIILQIDFTK LKEEDSLIVV YNSLKALTIK FARLQFCFVD RNNYVLDYGS
VLHKIDSLDS ISNLKSKSSS TQFSPIWLKN TLYPENIHEH LGIVAVSNSN MEAKKSILFQ
DYRCFTSFGR RRPNELKIKV GYLNVDYSDK IDELVEASSW TFVLETLCYS FGLSFDEHDD
DDEEDNDDST DNELDNSSGS LSDAESTTTI HIDSPFDNEN ATANMVNDRN LLTEGEHSNI
ENLETVASSV QPALIPNIRF SLHSEEEGTN ENENENDMPV LLLSDMDKGI DGITRRSSFS
SLIESGNNNC PLHMDYI
