WSC2_YEAST
ID WSC2_YEAST Reviewed; 503 AA.
AC P53832; D6W0R1;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Cell wall integrity and stress response component 2;
DE Flags: Precursor;
GN Name=WSC2; OrderedLocusNames=YNL283C; ORFNames=N0583;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [2]
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455 AND SER-458, AND
RP IDENTIFICATION BY 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 [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 GLYCOSYLATION [LARGE SCALE ANALYSIS].
RX PubMed=19756047; DOI=10.1038/msb.2009.64;
RA Kung L.A., Tao S.-C., Qian J., Smith M.G., Snyder M., Zhu H.;
RT "Global analysis of the glycoproteome in Saccharomyces cerevisiae reveals
RT new roles for protein glycosylation in eukaryotes.";
RL Mol. Syst. Biol. 5:308-308(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-402; SER-455 AND SER-458, AND
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 -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:19756047}.
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DR EMBL; Z71559; CAA96195.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10277.1; -; Genomic_DNA.
DR PIR; S63257; S63257.
DR RefSeq; NP_014116.1; NM_001183121.1.
DR AlphaFoldDB; P53832; -.
DR SMR; P53832; -.
DR BioGRID; 35558; 119.
DR IntAct; P53832; 18.
DR MINT; P53832; -.
DR STRING; 4932.YNL283C; -.
DR iPTMnet; P53832; -.
DR MaxQB; P53832; -.
DR PaxDb; P53832; -.
DR PRIDE; P53832; -.
DR EnsemblFungi; YNL283C_mRNA; YNL283C; YNL283C.
DR GeneID; 855438; -.
DR KEGG; sce:YNL283C; -.
DR SGD; S000005227; WSC2.
DR VEuPathDB; FungiDB:YNL283C; -.
DR eggNOG; KOG4157; Eukaryota.
DR GeneTree; ENSGT00940000176584; -.
DR HOGENOM; CLU_024893_1_0_1; -.
DR InParanoid; P53832; -.
DR OMA; STHYTTR; -.
DR BioCyc; YEAST:G3O-33274-MON; -.
DR PRO; PR:P53832; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53832; protein.
DR GO; GO:0005933; C:cellular bud; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043332; C:mating projection tip; HDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0030427; C:site of polarized growth; IDA:SGD.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IMP:SGD.
DR GO; GO:0031505; P:fungal-type cell wall organization; IMP:SGD.
DR GO; GO:0009408; P:response to heat; IMP:SGD.
DR GO; GO:0007266; P:Rho protein signal transduction; IMP:SGD.
DR InterPro; IPR002889; WSC_carb-bd.
DR Pfam; PF01822; WSC; 1.
DR SMART; SM00321; WSC; 1.
DR PROSITE; PS51212; WSC; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell wall biogenesis/degradation; Glycoprotein; Membrane;
KW Phosphoprotein; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..503
FT /note="Cell wall integrity and stress response component 2"
FT /id="PRO_0000041484"
FT TOPO_DOM 24..325
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 326..346
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 347..503
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 25..118
FT /note="WSC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00558"
FT REGION 124..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 470..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..485
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 402
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 455
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 458
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
SQ SEQUENCE 503 AA; 52292 MW; F2392A73C5CBAB50 CRC64;
MHLDLIHKSF ILVWLIYIRA ALADQFTYKA CYSASDIRKL GLTYKGVYEY QSVSYCQNEC
PGQAVVALFN GTGCYCGGSV AQLQSLTQVD SSKCDVSCAG WPYQNCGGSS AMNVYINNAA
STADSTSSTA TSTSTTSSSS TSVSSKTSTK LDTKTSTSSS ATHSSSSSST TSTTTSSSET
TTSSSSSSSS SSTSTTSTTS TTSSTTSTSS SPSTTSSSTS ASSSSETSST QATSSSTTST
SSSTSTATVT STPSSTSIGT STHYTTRVVT QSVVSQANQQ ASTIFTTRTS VYATVSSTSS
STSSLLNGKS SSSKSKGLSG GAIAGVVVGV VCGTVALLAL ALFFFVWKKR RQSSQHVDLE
ETKQYQPYSL GDADANPVIP PSASSTNWHI PSRNNTALSK NTASTFATYD LPTRAPGGRD
SIITGDAHNI SKRSHFPSVV YEEPPSIYNG NQRFSATSLP DMMEERQLHI VNPDNVSSNI
GSNVSDGDDD YDDAKDSNNS SLR
