ID   PRY1_YEAST              Reviewed;         299 AA.
AC   P47032; D6VWA4;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   02-SEP-2026, entry version 170.
DE   RecName: Full=Protein PRY1 {ECO:0000305};
DE   AltName: Full=Pathogenesis-related protein 1 {ECO:0000303|PubMed:23027975};
DE   Flags: Precursor;
GN   Name=PRY1 {ECO:0000303|PubMed:23027975}; OrderedLocusNames=YJL079C;
GN   ORFNames=J1022;
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=7483841; DOI=10.1002/yea.320110709;
RA   Miosga T., Schaaff-Gerstenschlaeger I., Chalwatzis N., Baur A., Boles E.,
RA   Fournier C., Schmitt S., Velten C., Wilhelm N., Zimmermann F.K.;
RT   "Sequence analysis of a 33.1 kb fragment from the left arm of Saccharomyces
RT   cerevisiae chromosome X, including putative proteins with leucine zippers,
RT   a fungal Zn(II)2-Cys6 binuclear cluster domain and a putative alpha 2-SCB-
RT   alpha 2 binding site.";
RL   Yeast 11:681-689(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA   Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA   Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA   Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA   Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA   Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA   Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA   Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA   Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA   To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA   von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL   EMBO J. 15:2031-2049(1996).
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   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   [5]
RP   SUBCELLULAR LOCATION.
RX   PubMed=11935221; DOI=10.1007/s00294-001-0264-9;
RA   Terashima H., Fukuchi S., Nakai K., Arisawa M., Hamada K., Yabuki N.,
RA   Kitada K.;
RT   "Sequence-based approach for identification of cell wall proteins in
RT   Saccharomyces cerevisiae.";
RL   Curr. Genet. 40:311-316(2002).
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   IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, STEROL-BINDING, SUBCELLULAR
RP   LOCATION, AND GLYCOSYLATION.
RX   PubMed=23027975; DOI=10.1073/pnas.1209086109;
RA   Choudhary V., Schneiter R.;
RT   "Pathogen-Related Yeast (PRY) proteins and members of the CAP superfamily
RT   are secreted sterol-binding proteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:16882-16887(2012).
CC   -!- FUNCTION: Secreted protein required for efficient export of lipids such
CC       as acetylated sterols. Acts in detoxification of hydrophobic compounds.
CC       {ECO:0000269|PubMed:23027975}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11935221,
CC       ECO:0000269|PubMed:23027975}.
CC   -!- DOMAIN: The SCP domain is necessary and sufficient for lipid export and
CC       sterol-binding. {ECO:0000269|PubMed:23027975}.
CC   -!- PTM: O-glycosylated. {ECO:0000269|PubMed:23027975}.
CC   -!- MISCELLANEOUS: Present with 556 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the CRISP family. {ECO:0000305}.
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DR   EMBL; Z49354; CAA89372.1; -; Genomic_DNA.
DR   EMBL; X83502; CAA58491.1; -; Genomic_DNA.
DR   EMBL; X88851; CAA61315.1; -; Genomic_DNA.
DR   EMBL; AY558306; AAS56632.1; -; Genomic_DNA.
DR   EMBL; BK006943; DAA08720.1; -; Genomic_DNA.
DR   PIR; S56031; S56031.
DR   RefSeq; NP_012456.1; NM_001181512.1.
DR   PDB; 5JYS; X-ray; 1.90 A; A=2-299.
DR   AlphaFoldDB; P47032; -.
DR   SMR; P47032; -.
DR   BioGRID; 33677; 122.
DR   DIP; DIP-3857N; -.
DR   FunCoup; P47032; 97.
DR   IntAct; P47032; 2.
DR   MINT; P47032; -.
DR   STRING; 4932.YJL079C; -.
DR   PaxDb; 4932-YJL079C; -.
DR   PeptideAtlas; P47032; -.
DR   EnsemblFungi; YJL079C_mRNA; YJL079C; YJL079C.
DR   GeneID; 853366; -.
DR   KEGG; sce:YJL079C; -.
DR   AGR; SGD:S000003615; -.
DR   SGD; S000003615; PRY1.
DR   VEuPathDB; FungiDB:YJL079C; -.
DR   eggNOG; KOG3017; Eukaryota.
DR   HOGENOM; CLU_035730_3_0_1; -.
DR   InParanoid; P47032; -.
DR   OMA; DSMRVGC; -.
DR   OrthoDB; 337038at2759; -.
DR   BioCyc; YEAST:G3O-31536-MONOMER; -.
DR   BioGRID-ORCS; 853366; 9 hits in 10 CRISPR screens.
DR   PRO; PR:P47032; -.
DR   Proteomes; UP000002311; Chromosome X.
DR   RNAct; P47032; protein.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR   GO; GO:0005576; C:extracellular region; IDA:SGD.
DR   GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR   GO; GO:0005635; C:nuclear envelope; HDA:SGD.
DR   GO; GO:0005504; F:fatty acid binding; IDA:SGD.
DR   GO; GO:0000287; F:magnesium ion binding; IDA:SGD.
DR   GO; GO:0032934; F:sterol binding; IDA:SGD.
DR   GO; GO:0015908; P:fatty acid transport; IGI:SGD.
DR   GO; GO:0015918; P:sterol transport; IMP:SGD.
DR   CDD; cd05384; CAP_PRY1-like; 1.
DR   FunFam; 3.40.33.10:FF:000012; Secreted protein PRY1; 1.
DR   Gene3D; 3.40.33.10; CAP; 1.
DR   InterPro; IPR018244; Allrgn_V5/Tpx1_CS.
DR   InterPro; IPR014044; CAP_dom.
DR   InterPro; IPR035940; CAP_sf.
DR   InterPro; IPR001283; CRISP-related.
DR   PANTHER; PTHR10334; CYSTEINE-RICH SECRETORY PROTEIN-RELATED; 1.
DR   Pfam; PF00188; CAP; 1.
DR   PRINTS; PR00837; V5TPXLIKE.
DR   SMART; SM00198; SCP; 1.
DR   SUPFAM; SSF55797; PR-1-like; 1.
DR   PROSITE; PS01009; CRISP_1; 1.
DR   PROSITE; PS01010; CRISP_2; 1.
DR   PDBsum; 5JYS; -.
PE   1: Evidence at protein level;
KW   3D-structure; Glycoprotein; Lipid transport; Lipid-binding;
KW   Reference proteome; Secreted; Signal; Transport.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..299
FT                   /note="Protein PRY1"
FT                   /id="PRO_0000006317"
FT   DOMAIN          167..281
FT                   /note="SCP"
FT   REGION          103..157
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   HELIX           161..174
FT                   /evidence="ECO:0007829|PDB:5JYS"
FT   HELIX           181..183
FT                   /evidence="ECO:0007829|PDB:5JYS"
FT   HELIX           187..198
FT                   /evidence="ECO:0007829|PDB:5JYS"
FT   STRAND          212..221
FT                   /evidence="ECO:0007829|PDB:5JYS"
FT   HELIX           223..231
FT                   /evidence="ECO:0007829|PDB:5JYS"
FT   HELIX           232..236
FT                   /evidence="ECO:0007829|PDB:5JYS"
FT   TURN            246..248
FT                   /evidence="ECO:0007829|PDB:5JYS"
FT   HELIX           249..254
FT                   /evidence="ECO:0007829|PDB:5JYS"
FT   STRAND          261..268
FT                   /evidence="ECO:0007829|PDB:5JYS"
FT   TURN            271..273
FT                   /evidence="ECO:0007829|PDB:5JYS"
FT   STRAND          275..283
FT                   /evidence="ECO:0007829|PDB:5JYS"
FT   HELIX           291..294
FT                   /evidence="ECO:0007829|PDB:5JYS"
SQ   SEQUENCE   299 AA;  30634 MW;  A316769CA87C5679 CRC64;
     MKLSKLSILT SALATSALAA PAVVTVTEHA HEAAVVTVQG VVYVENGQTR TTYETLAPAS
     TATPTSTATA LVAPPVAPSS ASSNSDVVLS ALKNLASVWG KTTDSTTTLT SSESTSQSLA
     QATTTSTPAA ASTTSTPAAT TTTSQAAATS SASSSDSDLS DFASSVLAEH NKKRALHKDT
     PALSWSDTLA SYAQDYADNY DCSGTLTHSG GPYGENLALG YDGPAAVDAW YNEISNYDFS
     NPGFSSNTGH FTQVVWKSTT QVGCGIKTCG GAWGDYVICS YDPAGNYEGE YADNVEPLA
//