PEA2_YEAST
ID PEA2_YEAST Reviewed; 420 AA.
AC P40091; D3DM56; Q70DC9; Q70DD1; Q70DD2; Q70DD3; Q70DD4; Q70DD6; Q70DD7;
AC Q70DD8;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Protein PEA2;
DE AltName: Full=Protein PPF2;
GN Name=PEA2; Synonyms=PPF2; OrderedLocusNames=YER149C;
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=8909546; DOI=10.1083/jcb.135.3.725;
RA Valtz N.L.M., Herskowitz I.;
RT "Pea2 protein of yeast is localized to sites of polarized growth and is
RT required for efficient mating and bipolar budding.";
RL J. Cell Biol. 135:725-739(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 26109 / X2180;
RA Yorihuzi T., Ohsumi Y.;
RT "A novel yeast gene necessary for pheromone-induced pointed projection
RT formation.";
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-90; THR-117; THR-157;
RP SER-161; ILE-165; ASN-171; LEU-189; MET-210; LYS-249; ARG-253; ASN-325;
RP SER-355; LEU-384 AND MET-409.
RC STRAIN=CLIB 219, CLIB 382, CLIB 388, CLIB 410, CLIB 413, CLIB 556,
RC CLIB 630, CLIB 95, K1, R12, R13, Sigma 1278B, YIIc12, and YIIc17;
RX PubMed=15087486; DOI=10.1093/nar/gkh529;
RA Leh-Louis V., Wirth B., Despons L., Wain-Hobson S., Potier S.,
RA Souciet J.-L.;
RT "Differential evolution of the Saccharomyces cerevisiae DUP240 paralogs and
RT implication of recombination in phylogeny.";
RL Nucleic Acids Res. 32:2069-2078(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
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 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 [LARGE SCALE ANALYSIS] AT SER-230, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, AND IDENTIFICATION BY
RP 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: Localized to sites of polarized growth and is required for
CC efficient mating and bipolar budding.
CC -!- INTERACTION:
CC P40091; P11710: FUS1; NbExp=5; IntAct=EBI-13106, EBI-7179;
CC P40091; P39523: YMR124W; NbExp=6; IntAct=EBI-13106, EBI-27256;
CC -!- MISCELLANEOUS: Present with 7820 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Y07594; CAA68869.1; -; Genomic_DNA.
DR EMBL; D38413; BAA07465.1; -; Genomic_DNA.
DR EMBL; AJ585620; CAE52140.1; -; Genomic_DNA.
DR EMBL; AJ585621; CAE52141.1; -; Genomic_DNA.
DR EMBL; AJ585622; CAE52142.1; -; Genomic_DNA.
DR EMBL; AJ585623; CAE52143.1; -; Genomic_DNA.
DR EMBL; AJ585624; CAE52144.1; -; Genomic_DNA.
DR EMBL; AJ585625; CAE52145.1; -; Genomic_DNA.
DR EMBL; AJ585626; CAE52146.1; -; Genomic_DNA.
DR EMBL; AJ585627; CAE52147.1; -; Genomic_DNA.
DR EMBL; AJ585628; CAE52148.1; -; Genomic_DNA.
DR EMBL; AJ585629; CAE52149.1; -; Genomic_DNA.
DR EMBL; AJ585630; CAE52150.1; -; Genomic_DNA.
DR EMBL; AJ585631; CAE52151.1; -; Genomic_DNA.
DR EMBL; AJ585632; CAE52152.1; -; Genomic_DNA.
DR EMBL; AJ585633; CAE52153.1; -; Genomic_DNA.
DR EMBL; AJ585634; CAE52154.1; -; Genomic_DNA.
DR EMBL; AJ585635; CAE52155.1; -; Genomic_DNA.
DR EMBL; AJ585636; CAE52156.1; -; Genomic_DNA.
DR EMBL; U18917; AAB64676.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07810.1; -; Genomic_DNA.
DR PIR; S50652; S50652.
DR RefSeq; NP_011076.1; NM_001179039.1.
DR AlphaFoldDB; P40091; -.
DR SMR; P40091; -.
DR BioGRID; 36898; 146.
DR ComplexPortal; CPX-3188; Polarisome.
DR DIP; DIP-2463N; -.
DR IntAct; P40091; 9.
DR MINT; P40091; -.
DR STRING; 4932.YER149C; -.
DR iPTMnet; P40091; -.
DR MaxQB; P40091; -.
DR PaxDb; P40091; -.
DR PRIDE; P40091; -.
DR EnsemblFungi; YER149C_mRNA; YER149C; YER149C.
DR GeneID; 856892; -.
DR KEGG; sce:YER149C; -.
DR SGD; S000000951; PEA2.
DR VEuPathDB; FungiDB:YER149C; -.
DR eggNOG; ENOG502QTTD; Eukaryota.
DR HOGENOM; CLU_054089_0_0_1; -.
DR InParanoid; P40091; -.
DR OMA; IMRNEFK; -.
DR BioCyc; YEAST:G3O-30310-MON; -.
DR PRO; PR:P40091; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P40091; protein.
DR GO; GO:0005933; C:cellular bud; IDA:SGD.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0005934; C:cellular bud tip; IDA:SGD.
DR GO; GO:0000131; C:incipient cellular bud site; IDA:SGD.
DR GO; GO:0043332; C:mating projection tip; IDA:SGD.
DR GO; GO:0000133; C:polarisome; IDA:SGD.
DR GO; GO:0007121; P:bipolar cellular bud site selection; IMP:SGD.
DR GO; GO:0007118; P:budding cell apical bud growth; IMP:SGD.
DR GO; GO:0030010; P:establishment of cell polarity; IMP:SGD.
DR GO; GO:0030950; P:establishment or maintenance of actin cytoskeleton polarity; IC:ComplexPortal.
DR GO; GO:0030447; P:filamentous growth; IMP:SGD.
DR GO; GO:2000251; P:positive regulation of actin cytoskeleton reorganization; IMP:SGD.
DR GO; GO:0007124; P:pseudohyphal growth; IMP:SGD.
DR GO; GO:0031384; P:regulation of initiation of mating projection growth; IMP:SGD.
DR GO; GO:0032880; P:regulation of protein localization; IMP:SGD.
DR GO; GO:0031385; P:regulation of termination of mating projection growth; IMP:SGD.
DR GO; GO:0006903; P:vesicle targeting; IC:ComplexPortal.
PE 1: Evidence at protein level;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..420
FT /note="Protein PEA2"
FT /id="PRO_0000058300"
FT REGION 132..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT VARIANT 90
FT /note="H -> R (in strain: CLIB 219)"
FT /evidence="ECO:0000269|PubMed:15087486"
FT VARIANT 117
FT /note="M -> T (in strain: CLIB 630)"
FT /evidence="ECO:0000269|PubMed:15087486"
FT VARIANT 157
FT /note="K -> T (in strain: CLIB 219)"
FT /evidence="ECO:0000269|PubMed:15087486"
FT VARIANT 161
FT /note="G -> S (in strain: CLIB 630)"
FT /evidence="ECO:0000269|PubMed:15087486"
FT VARIANT 165
FT /note="T -> I (in strain: CLIB 630)"
FT /evidence="ECO:0000269|PubMed:15087486"
FT VARIANT 171
FT /note="D -> N (in strain: CLIB 630)"
FT /evidence="ECO:0000269|PubMed:15087486"
FT VARIANT 189
FT /note="Q -> L (in strain: CLIB 382)"
FT /evidence="ECO:0000269|PubMed:15087486"
FT VARIANT 210
FT /note="I -> M (in strain: CLIB 413 haplotype Ha2)"
FT /evidence="ECO:0000269|PubMed:15087486"
FT VARIANT 249
FT /note="E -> K (in strain: CLIB 556)"
FT /evidence="ECO:0000269|PubMed:15087486"
FT VARIANT 253
FT /note="S -> R (in strain: Sigma 1278B)"
FT /evidence="ECO:0000269|PubMed:15087486"
FT VARIANT 325
FT /note="S -> N (in strain: CLIB 219)"
FT /evidence="ECO:0000269|PubMed:15087486"
FT VARIANT 355
FT /note="G -> S (in strain: R12)"
FT /evidence="ECO:0000269|PubMed:15087486"
FT VARIANT 384
FT /note="S -> L (in strain: CLIB 219)"
FT /evidence="ECO:0000269|PubMed:15087486"
FT VARIANT 409
FT /note="L -> M (in strain: CLIB 410, CLIB 413 and Sigma
FT 1278B)"
FT /evidence="ECO:0000269|PubMed:15087486"
SQ SEQUENCE 420 AA; 48165 MW; 594B9A14E71A943D CRC64;
MHKFDLELSR RANPLLFSAE RYEEYPLKYD ELKQYLLSQN PSHPHHNSRP YTSIDYFDYL
LYRSKNDESE IDLDKKLVSE FALYYVQKEH LNSDDLNPTL NELLKLQPKS ADWYEMMLRI
LESINTTGID QLTKENNNSF PNSKRARSST NMGGTDKFNK GAYHTDKADD DKNEILQELT
SFLMSNSIQK GIDIKPIPLD DPVKFLKNGI NSILDTCVSL EKNTSSPPIS PNAAAIQEED
SSKKLEELET AFSDLQLAHN FLTKQFENDR AEYVQDIEKL TRTNRELQDK LLNNHSNLSK
TEKKLHELEQ ENKELEKANN KLNSSRHNFG MSSPASSPVT WDPSSPSSVG SPTSGSGSRS
LSIMTSEFKK VLTSTQRKYE KELSDEREHR FKLERELALL KNAEANTSLA LNRDDPPDML
