PRY1_YEAST
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 03-AUG-2022, entry version 154.
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}.
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; 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 PDBsum; 5JYS; -.
DR AlphaFoldDB; P47032; -.
DR SMR; P47032; -.
DR BioGRID; 33677; 116.
DR DIP; DIP-3857N; -.
DR IntAct; P47032; 1.
DR MINT; P47032; -.
DR STRING; 4932.YJL079C; -.
DR MaxQB; P47032; -.
DR PaxDb; P47032; -.
DR PRIDE; P47032; -.
DR EnsemblFungi; YJL079C_mRNA; YJL079C; YJL079C.
DR GeneID; 853366; -.
DR KEGG; sce:YJL079C; -.
DR SGD; S000003615; PRY1.
DR VEuPathDB; FungiDB:YJL079C; -.
DR eggNOG; KOG3017; Eukaryota.
DR GeneTree; ENSGT00980000198854; -.
DR HOGENOM; CLU_035730_3_0_1; -.
DR InParanoid; P47032; -.
DR OMA; KDHGANN; -.
DR BioCyc; YEAST:G3O-31536-MON; -.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
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:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR GO; GO:0005635; C:nuclear envelope; HDA:SGD.
DR GO; GO:0015485; F:cholesterol binding; IDA: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 Gene3D; 3.40.33.10; -; 1.
DR InterPro; IPR018244; Allrgn_V5/Tpx1_CS.
DR InterPro; IPR014044; CAP_domain.
DR InterPro; IPR035940; CAP_sf.
DR InterPro; IPR001283; CRISP-related.
DR PANTHER; PTHR10334; PTHR10334; 1.
DR Pfam; PF00188; CAP; 1.
DR PRINTS; PR00837; V5TPXLIKE.
DR SMART; SM00198; SCP; 1.
DR SUPFAM; SSF55797; SSF55797; 1.
DR PROSITE; PS01009; CRISP_1; 1.
DR PROSITE; PS01010; CRISP_2; 1.
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 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
