PST1_YEAST
ID PST1_YEAST Reviewed; 444 AA.
AC Q12355; D6VS41;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Cell wall mannoprotein PST1;
DE AltName: Full=Haze protective factor 2;
DE AltName: Full=Protoplast secreted protein 1;
DE Flags: Precursor;
GN Name=PST1; Synonyms=HPF2; OrderedLocusNames=YDR055W;
GN ORFNames=D4214, YD9609.09;
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].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8789263;
RX DOI=10.1002/(sici)1097-0061(199601)12:1<85::aid-yea890>3.0.co;2-u;
RA Brandt P., Ramlow S., Otto B., Bloecker H.;
RT "Nucleotide sequence analysis of a 32,500 bp region of the right arm of
RT Saccharomyces cerevisiae chromosome IV.";
RL Yeast 12:85-90(1996).
RN [2]
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 [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 PROTEIN SEQUENCE OF 48-52; 65-71; 126-146; 164-173; 180-185; 201-225;
RP 227-260 AND 327-334, GLYCOSYLATION AT ASN-210; ASN-228; ASN-235; ASN-242
RP AND ASN-329, FUNCTION, AND BIOTECHNOLOGY.
RC STRAIN=Maurivin PDM;
RX PubMed=17024473; DOI=10.1007/s00253-006-0606-0;
RA Brown S.L., Stockdale V.J., Pettolino F., Pocock K.F., de Barros Lopes M.,
RA Williams P.J., Bacic A., Fincher G.B., Hoej P.B., Waters E.J.;
RT "Reducing haziness in white wine by overexpression of Saccharomyces
RT cerevisiae genes YOL155c and YDR055w.";
RL Appl. Microbiol. Biotechnol. 73:1363-1376(2007).
RN [5]
RP GPI-ANCHOR, AND SUBCELLULAR LOCATION.
RX PubMed=10383953; DOI=10.1128/jb.181.13.3886-3889.1999;
RA Hamada K., Terashima H., Arisawa M., Yabuki N., Kitada K.;
RT "Amino acid residues in the omega-minus region participate in cellular
RT localization of yeast glycosylphosphatidylinositol-attached proteins.";
RL J. Bacteriol. 181:3886-3889(1999).
RN [6]
RP INDUCTION.
RX PubMed=10594829; DOI=10.1046/j.1365-2958.1999.01667.x;
RA Jung U.S., Levin D.E.;
RT "Genome-wide analysis of gene expression regulated by the yeast cell wall
RT integrity signalling pathway.";
RL Mol. Microbiol. 34:1049-1057(1999).
RN [7]
RP IDENTIFICATION.
RX PubMed=10234784;
RX DOI=10.1002/(sici)1097-0061(199904)15:6<459::aid-yea387>3.0.co;2-l;
RA Pardo M., Monteoliva L., Pla J., Sanchez M., Gil C., Nombela C.;
RT "Two-dimensional analysis of proteins secreted by Saccharomyces cerevisiae
RT regenerating protoplasts: a novel approach to study the cell wall.";
RL Yeast 15:459-472(1999).
RN [8]
RP GPI-ANCHOR, AND INDUCTION.
RX PubMed=11016834; DOI=10.1007/s004380000285;
RA Terashima H., Yabuki N., Arisawa M., Hamada K., Kitada K.;
RT "Up-regulation of genes encoding glycosylphosphatidylinositol (GPI)-
RT attached proteins in response to cell wall damage caused by disruption of
RT FKS1 in Saccharomyces cerevisiae.";
RL Mol. Gen. Genet. 264:64-74(2000).
RN [9]
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 [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15583168; DOI=10.1099/mic.0.26924-0;
RA Pardo M., Monteoliva L., Vazquez P., Martinez R., Molero G., Nombela C.,
RA Gil C.;
RT "PST1 and ECM33 encode two yeast cell surface GPI proteins important for
RT cell wall integrity.";
RL Microbiology 150:4157-4170(2004).
RN [11]
RP INDUCTION.
RX PubMed=15116342; DOI=10.1002/yea.1109;
RA Boorsma A., de Nobel H., ter Riet B., Bargmann B., Brul S.,
RA Hellingwerf K.J., Klis F.M.;
RT "Characterization of the transcriptional response to cell wall stress in
RT Saccharomyces cerevisiae.";
RL Yeast 21:413-427(2004).
CC -!- FUNCTION: Has a partially redundant function to ECM33 in cell wall
CC integrity. May be involved in a repair mechanism activated in response
CC to cell wall damage. {ECO:0000269|PubMed:15583168,
CC ECO:0000269|PubMed:17024473}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC Secreted, cell wall. Note=Identified as GPI-anchored plasma membrane
CC protein (GPI-PMP) as well as non-covalently-linked, soluble protein of
CC the cell wall. Secreted by regenerating protoplasts. In budded cells,
CC concentrates at the surface of the buds.
CC -!- INDUCTION: Positively regulated by cell integrity signaling through
CC MPK1 in response to cell wall perturbation. Induction is dependent on
CC transcription factor RLM1. {ECO:0000269|PubMed:10594829,
CC ECO:0000269|PubMed:11016834, ECO:0000269|PubMed:15116342}.
CC -!- PTM: Extensively N- and O-mannosylated.
CC -!- BIOTECHNOLOGY: Mannoprotein called haze protective factor from wine
CC that is able to prevent visible wine protein haze formation. This
CC mannoprotein showed haze-protective activity against wine proteins and
CC BSA when either was heated in white wine.
CC {ECO:0000269|PubMed:17024473}.
CC -!- MISCELLANEOUS: Present with 11700 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SPS2 family. {ECO:0000305}.
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DR EMBL; X84162; CAA58971.1; -; Genomic_DNA.
DR EMBL; Z74351; CAA98873.1; -; Genomic_DNA.
DR EMBL; Z49209; CAA89084.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11901.1; -; Genomic_DNA.
DR PIR; S54039; S54039.
DR RefSeq; NP_010340.1; NM_001180363.1.
DR AlphaFoldDB; Q12355; -.
DR SMR; Q12355; -.
DR BioGRID; 32108; 66.
DR DIP; DIP-7811N; -.
DR IntAct; Q12355; 1.
DR MINT; Q12355; -.
DR STRING; 4932.YDR055W; -.
DR iPTMnet; Q12355; -.
DR COMPLUYEAST-2DPAGE; Q12355; -.
DR MaxQB; Q12355; -.
DR PaxDb; Q12355; -.
DR PRIDE; Q12355; -.
DR EnsemblFungi; YDR055W_mRNA; YDR055W; YDR055W.
DR GeneID; 851625; -.
DR KEGG; sce:YDR055W; -.
DR SGD; S000002462; PST1.
DR VEuPathDB; FungiDB:YDR055W; -.
DR eggNOG; ENOG502QUZC; Eukaryota.
DR GeneTree; ENSGT00940000176339; -.
DR HOGENOM; CLU_035846_0_0_1; -.
DR InParanoid; Q12355; -.
DR OMA; QISACKF; -.
DR BioCyc; YEAST:G3O-29664-MON; -.
DR PRO; PR:Q12355; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q12355; protein.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:SGD.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0031505; P:fungal-type cell wall organization; IGI:SGD.
DR Gene3D; 3.80.20.20; -; 2.
DR InterPro; IPR036941; Rcpt_L-dom_sf.
PE 1: Evidence at protein level;
KW Cell membrane; Cell wall; Direct protein sequencing; Glycoprotein;
KW GPI-anchor; Lipoprotein; Membrane; Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..419
FT /note="Cell wall mannoprotein PST1"
FT /id="PRO_0000033193"
FT PROPEP 420..444
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000033194"
FT REGION 359..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..379
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 419
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 76
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17024473"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17024473"
FT CARBOHYD 235
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17024473"
FT CARBOHYD 242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17024473"
FT CARBOHYD 263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 268
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 305
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 329
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17024473"
SQ SEQUENCE 444 AA; 45777 MW; 230F60CACA5921A4 CRC64;
MQLHSLIAST ALLITSALAA TSSSSSIPSS CTISSHATAT AQSDLDKYSR CDTLVGNLTI
GGGLKTGALA NVKEINGSLT IFNATNLTSF AADSLESITD SLNLQSLTIL TSASFGSLQS
VDSIKLITLP AISSFTSNIK SANNIYISDT SLQSVDGFSA LKKVNVFNVN NNKKLTSIKS
PVETVSDSLQ FSFNGNQTKI TFDDLVWANN ISLTDVHSVS FANLQKINSS LGFINNSISS
LNFTKLNTIG QTFSIVSNDY LKNLSFSNLS TIGGALVVAN NTGLQKIGGL DNLTTIGGTL
EVVGNFTSLN LDSLKSVKGG ADVESKSSNF SCNALKALQK KGGIKGESFV CKNGASSTSV
KLSSTSKSQS SQTTAKVSKS SSKAEEKKFT SGDIKAAASA SSVSSSGASS SSSKSSKGNA
AIMAPIGQTT PLVGLLTAII MSIM
