PRY2_YEAST
ID PRY2_YEAST Reviewed; 329 AA.
AC P36110; D6VX78;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Protein PRY2;
DE AltName: Full=Pathogenesis-related protein 2;
DE Flags: Precursor;
GN Name=PRY2; OrderedLocusNames=YKR013W; ORFNames=YK111;
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=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
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=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 [4]
RP FUNCTION, STEROL-BINDING, SUBCELLULAR 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 -!- 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; Z28238; CAA82084.1; -; Genomic_DNA.
DR EMBL; Z28237; CAA82083.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09168.1; -; Genomic_DNA.
DR PIR; S38082; S38082.
DR RefSeq; NP_012938.3; NM_001179803.3.
DR AlphaFoldDB; P36110; -.
DR SMR; P36110; -.
DR BioGRID; 34145; 78.
DR STRING; 4932.YKR013W; -.
DR PaxDb; P36110; -.
DR PRIDE; P36110; -.
DR EnsemblFungi; YKR013W_mRNA; YKR013W; YKR013W.
DR GeneID; 853882; -.
DR KEGG; sce:YKR013W; -.
DR SGD; S000001721; PRY2.
DR VEuPathDB; FungiDB:YKR013W; -.
DR eggNOG; KOG3017; Eukaryota.
DR GeneTree; ENSGT00980000198854; -.
DR HOGENOM; CLU_035730_3_0_1; -.
DR InParanoid; P36110; -.
DR OMA; WTDEVSE; -.
DR BioCyc; YEAST:G3O-31989-MON; -.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR PRO; PR:P36110; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P36110; 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: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 Glycoprotein; Lipid transport; Lipid-binding; Reference proteome; Secreted;
KW Signal; Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..329
FT /note="Protein PRY2"
FT /id="PRO_0000006318"
FT DOMAIN 197..311
FT /note="SCP"
FT REGION 122..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 329 AA; 33780 MW; 43CEEE8853875A3E CRC64;
MKFSKVSLLA ASASVALSAP VAVTVTQHVH QAATVVVQGI VRVENGQTLT TFITKGTQTA
SASPVATTSA PIVVANAQVD SIATSVIQES AVVAESATFE ESSTETSEAF STATATIQAV
QTSASATQDD VTTTLTSSTQ PTSTTTPTTT TTSPTTTTSP TTTASPTTTA SPTTATTTQS
TASSTQSSSS DFSTSMVNEH NTKRALHKDT GSLTWSDTLA TYAQNYADSY DCSGNLVHSG
GPYGENLALG YGTTGSVDAW YNEITSYDYS NPGFSESAGH FTQVVWKGTS EVGCGLKSCG
GEWGDYIICS YKAAGNVIGE FADNVMPLA
