ID   SPI1_YEAST              Reviewed;         148 AA.
AC   P40092; D3DM57;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   04-NOV-2026, entry version 156.
DE   RecName: Full=Uncharacterized cell wall protein SPI1;
DE   AltName: Full=Stationary phase-induced protein 1;
DE   Flags: Precursor;
GN   Name=SPI1; OrderedLocusNames=YER150W;
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=9169868; DOI=10.1038/387s078;
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   [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   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [4]
RP   SUBCELLULAR LOCATION.
RX   PubMed=9613572; DOI=10.1007/s004380050706;
RA   Hamada K., Fukuchi S., Arisawa M., Baba M., Kitada K.;
RT   "Screening for glycosylphosphatidylinositol (GPI)-dependent cell wall
RT   proteins in Saccharomyces cerevisiae.";
RL   Mol. Gen. Genet. 258:53-59(1998).
RN   [5]
RP   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=10641036;
RX   DOI=10.1002/(sici)1097-0061(20000130)16:2<139::aid-yea512>3.0.co;2-j;
RA   Puig S., Perez-Ortin J.E.;
RT   "Stress response and expression patterns in wine fermentations of yeast
RT   genes induced at the diauxic shift.";
RL   Yeast 16:139-148(2000).
RN   [7]
RP   INDUCTION.
RX   PubMed=11136466; DOI=10.1046/j.1365-2958.2001.02242.x;
RA   Kapteyn J.C., ter Riet B., Vink E., Blad S., De Nobel H., Van Den Ende H.,
RA   Klis F.M.;
RT   "Low external pH induces HOG1-dependent changes in the organization of the
RT   Saccharomyces cerevisiae cell wall.";
RL   Mol. Microbiol. 39:469-479(2001).
RN   [8]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=16980434; DOI=10.1128/aem.01476-06;
RA   Simoes T., Mira N.P., Fernandes A.R., Sa-Correia I.;
RT   "The SPI1 gene, encoding a glycosylphosphatidylinositol-anchored cell wall
RT   protein, plays a prominent role in the development of yeast resistance to
RT   lipophilic weak-acid food preservatives.";
RL   Appl. Environ. Microbiol. 72:7168-7175(2006).
CC   -!- FUNCTION: Cell wall protein that plays a role in adaptation and
CC       resistance to cell wall stress. {ECO:0000269|PubMed:16980434}.
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall. Membrane; Lipid-anchor, GPI-
CC       anchor. Note=Covalently-linked GPI-modified cell wall protein (GPI-
CC       CWP).
CC   -!- INDUCTION: Induced by transcription factors MSN2 and MSN4 in stationary
CC       phase and by transcription factors MSN2, MSN4 and HAA1 upon weak-acid
CC       stress. Up-regulated by low pH. {ECO:0000269|PubMed:10641036,
CC       ECO:0000269|PubMed:11136466, ECO:0000269|PubMed:16980434}.
CC   -!- PTM: The GPI-anchor is attached to the protein in the endoplasmic
CC       reticulum and serves to target the protein to the cell surface. There,
CC       the glucosamine-inositol phospholipid moiety is cleaved off and the
CC       GPI-modified mannoprotein is covalently attached via its lipidless GPI
CC       glycan remnant to the 1,6-beta-glucan of the outer cell wall layer.
CC   -!- SIMILARITY: Belongs to the SED1 family. {ECO:0000305}.
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DR   EMBL; U18917; AAB64677.1; -; Genomic_DNA.
DR   EMBL; AY557784; AAS56110.1; -; Genomic_DNA.
DR   EMBL; BK006939; DAA07811.1; -; Genomic_DNA.
DR   PIR; S50653; S50653.
DR   RefSeq; NP_011077.1; NM_001179040.1.
DR   AlphaFoldDB; P40092; -.
DR   SMR; P40092; -.
DR   BioGRID; 36899; 38.
DR   DIP; DIP-2064N; -.
DR   FunCoup; P40092; 101.
DR   IntAct; P40092; 7.
DR   STRING; 4932.YER150W; -.
DR   GlyCosmos; P40092; 2 sites, No reported glycans.
DR   GlyGen; P40092; 3 sites.
DR   PaxDb; 4932-YER150W; -.
DR   PeptideAtlas; P40092; -.
DR   EnsemblFungi; YER150W_mRNA; YER150W; YER150W.
DR   GeneID; 856893; -.
DR   KEGG; sce:YER150W; -.
DR   AGR; SGD:S000000952; -.
DR   SGD; S000000952; SPI1.
DR   VEuPathDB; FungiDB:YER150W; -.
DR   eggNOG; ENOG502S7XK; Eukaryota.
DR   HOGENOM; CLU_1760251_0_0_1; -.
DR   InParanoid; P40092; -.
DR   OMA; APIFYNS; -.
DR   OrthoDB; 4094614at2759; -.
DR   BioCyc; YEAST:G3O-30311-MONOMER; -.
DR   BioGRID-ORCS; 856893; 5 hits in 10 CRISPR screens.
DR   PRO; PR:P40092; -.
DR   Proteomes; UP000002311; Chromosome V.
DR   RNAct; P40092; protein.
DR   GO; GO:0071944; C:cell periphery; HDA:SGD.
DR   GO; GO:0009277; C:fungal-type cell wall; IDA:SGD.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005199; F:structural constituent of cell wall; IBA:GO_Central.
DR   GO; GO:0031505; P:fungal-type cell wall organization; IBA:GO_Central.
DR   GO; GO:0010447; P:response to acidic pH; IMP:SGD.
DR   InterPro; IPR038843; Sed1/Spi1.
DR   PANTHER; PTHR35523; CELL WALL PROTEIN SED1; 1.
DR   PANTHER; PTHR35523:SF1; CELL WALL PROTEIN SED1; 1.
PE   2: Evidence at transcript level;
KW   Cell wall; Glycoprotein; GPI-anchor; Lipoprotein; Membrane;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..127
FT                   /note="Uncharacterized cell wall protein SPI1"
FT                   /id="PRO_0000014317"
FT   PROPEP          128..148
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000372448"
FT   LIPID           127
FT                   /note="GPI-anchor amidated asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        41
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        59
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   148 AA;  14996 MW;  F65B20225FE2A5ED CRC64;
     MLSNAKLLLS LAMASTALGL VSNSSSSVIV VPSSDATIAG NDTATPAPEP SSAAPIFYNS
     TATATQYEVV SEFTTYCPEP TTFVTNGATF TVTAPTTLTI TNCPCTIEKP TSETSVSSTH
     DVETNSNAAN ARAIPGALGL AGAVMMLL
//