PGA14_YEAST
ID PGA14_YEAST Reviewed; 204 AA.
AC P53872; D6W0Z7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Hydrophilin YNL190W;
DE Flags: Precursor;
GN OrderedLocusNames=YNL190W; ORFNames=N1415;
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 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 [4]
RP GPI-ANCHOR AT ASN-174, 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 [5]
RP INDUCTION.
RX PubMed=10681550; DOI=10.1074/jbc.275.8.5668;
RA Garay-Arroyo A., Colmenero-Flores J.M., Garciarrubio A., Covarrubias A.A.;
RT "Highly hydrophilic proteins in prokaryotes and eukaryotes are common
RT during conditions of water deficit.";
RL J. Biol. Chem. 275:5668-5674(2000).
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 DISRUPTION PHENOTYPE, FUNCTION, AND INDUCTION.
RX PubMed=22442684; DOI=10.1371/journal.pone.0033324;
RA Lopez-Martinez G., Rodriguez-Porrata B., Margalef-Catala M.,
RA Cordero-Otero R.;
RT "The STF2p hydrophilin from Saccharomyces cerevisiae is required for
RT dehydration stress tolerance.";
RL PLoS ONE 7:E33324-E33324(2012).
CC -!- FUNCTION: Hydrophilin which is essential to overcome the simple stress
CC of the desiccation-rehydration process. {ECO:0000269|PubMed:22442684}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:10383953,
CC ECO:0000269|PubMed:9613572}. Membrane {ECO:0000305}; Lipid-anchor, GPI-
CC anchor {ECO:0000305}.
CC -!- INDUCTION: Up-regulated in response to osmotic stress.
CC {ECO:0000269|PubMed:10681550, ECO:0000269|PubMed:22442684}.
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 -!- DISRUPTION PHENOTYPE: Has statistically significant lower desiccation
CC tolerance capacity. {ECO:0000269|PubMed:22442684}.
CC -!- MISCELLANEOUS: Present with 1380 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the PGA14 family. {ECO:0000305}.
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DR EMBL; Z71466; CAA96084.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10363.1; -; Genomic_DNA.
DR PIR; S63145; S63145.
DR RefSeq; NP_014209.1; NM_001183028.1.
DR AlphaFoldDB; P53872; -.
DR BioGRID; 35643; 85.
DR DIP; DIP-4739N; -.
DR IntAct; P53872; 3.
DR MINT; P53872; -.
DR STRING; 4932.YNL190W; -.
DR MaxQB; P53872; -.
DR PaxDb; P53872; -.
DR EnsemblFungi; YNL190W_mRNA; YNL190W; YNL190W.
DR GeneID; 855531; -.
DR KEGG; sce:YNL190W; -.
DR SGD; S000005134; YNL190W.
DR VEuPathDB; FungiDB:YNL190W; -.
DR eggNOG; ENOG502RZ9P; Eukaryota.
DR HOGENOM; CLU_098355_0_0_1; -.
DR InParanoid; P53872; -.
DR OMA; WGRFDHT; -.
DR BioCyc; YEAST:G3O-33201-MON; -.
DR PRO; PR:P53872; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53872; protein.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:SGD.
DR GO; GO:0042631; P:cellular response to water deprivation; IMP:SGD.
PE 1: Evidence at protein level;
KW Cell wall; Glycoprotein; GPI-anchor; Lipoprotein; Membrane;
KW Reference proteome; Repeat; Secreted; Signal; Stress response.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..174
FT /note="Hydrophilin YNL190W"
FT /id="PRO_0000203402"
FT PROPEP 175..204
FT /note="Removed in mature form"
FT /id="PRO_0000424804"
FT REGION 35..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 174
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000269|PubMed:10383953"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 155
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 204 AA; 21966 MW; 0A3F7F821408C8BE CRC64;
MKFSSVTAIT LATVATVATA KKGEHDFTTT LTLSSDGSLT TTTSTHTTHK YGKFNKTSKS
KTPNHTGTHK YGKFNKTSKS KTPNHTGTHK YGKFNKTSKS KTPNHTGTHK YGKFNKTSKS
KTPNHTGTHK YGKFNKTSKS KTPNHTGTHK YGKFNKTKHD TTTYGPGEKA RKNNAAPGPS
NFNSIKLFGV TAGSAAVAGA LLLL
