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 10-JUN-2026, entry version 162. 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; DOI=10.1038/387s093; 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}. 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; 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; 122. DR FunCoup; P53832; 206. DR IntAct; P53832; 18. DR MINT; P53832; -. DR STRING; 4932.YNL283C; -. DR iPTMnet; P53832; -. DR PaxDb; 4932-YNL283C; -. DR PeptideAtlas; P53832; -. DR EnsemblFungi; YNL283C_mRNA; YNL283C; YNL283C. DR GeneID; 855438; -. DR KEGG; sce:YNL283C; -. DR AGR; SGD:S000005227; -. DR SGD; S000005227; WSC2. DR VEuPathDB; FungiDB:YNL283C; -. DR eggNOG; KOG4157; Eukaryota. DR HOGENOM; CLU_024893_1_0_1; -. DR InParanoid; P53832; -. DR OMA; DAHNISK; -. DR OrthoDB; 2019572at2759; -. DR BioCyc; YEAST:G3O-33274-MONOMER; -. DR BioGRID-ORCS; 855438; 1 hit in 10 CRISPR screens. 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:0005935; C:cellular bud neck; IDA:SGD. DR GO; GO:0005737; C:cytoplasm; HDA:SGD. DR GO; GO:0000324; C:fungal-type vacuole; HDA:SGD. 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; IPR051694; Immunoregulatory_rcpt-like. DR InterPro; IPR002889; WSC_carb-bd. DR PANTHER; PTHR15549:SF26; AXIAL BUDDING PATTERN PROTEIN 2-RELATED; 1. DR PANTHER; PTHR15549; PAIRED IMMUNOGLOBULIN-LIKE TYPE 2 RECEPTOR; 1. 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 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 //