PRY3_YEAST
ID PRY3_YEAST Reviewed; 881 AA.
AC P47033; D6VWA5;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Cell wall protein PRY3;
DE AltName: Full=Pathogenesis-related protein 3;
DE Flags: Precursor;
GN Name=PRY3; OrderedLocusNames=YJL078C; ORFNames=J1027;
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 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 INDUCTION.
RX PubMed=11747810; DOI=10.1016/s0092-8674(01)00596-7;
RA Colman-Lerner A., Chin T.E., Brent R.;
RT "Yeast Cbk1 and Mob2 activate daughter-specific genetic programs to induce
RT asymmetric cell fates.";
RL Cell 107:739-750(2001).
RN [6]
RP ALTERNATIVE PROMOTER USAGE.
RX PubMed=16420678; DOI=10.1186/gb-2005-6-13-r111;
RA Law G.L., Bickel K.S., MacKay V.L., Morris D.R.;
RT "The undertranslated transcriptome reveals widespread translational
RT silencing by alternative 5' transcript leaders.";
RL Genome Biol. 6:RESEARCH0111.1-RESEARCH0111.15(2005).
RN [7]
RP SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, AND GPI-ANCHOR.
RX PubMed=15781460; DOI=10.1074/jbc.m500334200;
RA Yin Q.Y., de Groot P.W.J., Dekker H.L., de Jong L., Klis F.M.,
RA de Koster C.G.;
RT "Comprehensive proteomic analysis of Saccharomyces cerevisiae cell walls:
RT identification of proteins covalently attached via
RT glycosylphosphatidylinositol remnants or mild alkali-sensitive linkages.";
RL J. Biol. Chem. 280:20894-20901(2005).
RN [8]
RP ALTERNATIVE PROMOTER USAGE, FUNCTION, AND INDUCTION.
RX PubMed=16940175; DOI=10.1128/mcb.01004-06;
RA Bickel K.S., Morris D.R.;
RT "Role of the transcription activator Ste12p as a repressor of PRY3
RT expression.";
RL Mol. Cell. Biol. 26:7901-7912(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND GLYCOSYLATION AT ASN-101.
RX PubMed=23038983; DOI=10.1021/pr300599f;
RA Bailey U.M., Jamaluddin M.F., Schulz B.L.;
RT "Analysis of congenital disorder of glycosylation-Id in a yeast model
RT system shows diverse site-specific under-glycosylation of glycoproteins.";
RL J. Proteome Res. 11:5376-5383(2012).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
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).
RN [11]
RP FUNCTION.
RX PubMed=23523622; DOI=10.1016/j.jbiotec.2013.03.003;
RA Nishida N., Ozato N., Matsui K., Kuroda K., Ueda M.;
RT "ABC transporters and cell wall proteins involved in organic solvent
RT tolerance in Saccharomyces cerevisiae.";
RL J. Biotechnol. 165:145-152(2013).
CC -!- FUNCTION: [Isoform Long]: The full-length isoform (isoform Long) is a
CC daughter cell-specific cell wall protein required for efficient export
CC of lipids such as acetylated sterols. Acts in detoxification of
CC hydrophobic compounds. Involved in tolerance to organic solvents such
CC as dimethyl sulfoxide (DMSO). Also plays a role as an inhibitor of
CC mating. STE12 is utilized as a repressor of full-length PRY3
CC transcription, ensuring efficient mating.
CC -!- FUNCTION: [Isoform Short]: There is no evidence that production of the
CC short PRY3 transcript (isoform Short) is anything more than an
CC adventitious by-product of the mechanism responsible for the repression
CC of the full-length transcript. Moreover, no disadvantage is detectable
CC for cells unable to make the short transcript (PubMed:16940175).
CC {ECO:0000269|PubMed:16940175}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall. Membrane; Lipid-anchor, GPI-
CC anchor. Note=Covalently-linked GPI-modified cell wall protein (GPI-
CC CWP). The short isoform lacks the predicted signal peptide and might
CC have an alternate localization.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage; Named isoforms=2;
CC Name=Long;
CC IsoId=P47033-1; Sequence=Displayed;
CC Name=Short; Synonyms=+452 PRY3;
CC IsoId=P47033-2; Sequence=Not described;
CC -!- INDUCTION: Expressed specifically in daughter cells through activation
CC by the transcription factor ACE2. STE12 represses expression of the
CC full-length transcript and induces expression of the short form. STE12-
CC binding to pheromone response elements (PREs) at positions -175 and
CC -161 prevents SPT15 from binding TATA-box 1 and thus it binds TATA-box
CC 2 at position +385 and directs internal transcription initiation at
CC position +452. {ECO:0000269|PubMed:11747810,
CC ECO:0000269|PubMed:16940175}.
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 -!- MISCELLANEOUS: [Isoform Short]: Produced by alternative promoter usage.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the CRISP family. {ECO:0000305}.
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DR EMBL; X83502; CAA58492.1; -; Genomic_DNA.
DR EMBL; X88851; CAA61314.1; -; Genomic_DNA.
DR EMBL; Z49353; CAA89370.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08721.1; -; Genomic_DNA.
DR PIR; S56032; S56032.
DR RefSeq; NP_012457.1; NM_001181511.1. [P47033-1]
DR AlphaFoldDB; P47033; -.
DR SMR; P47033; -.
DR BioGRID; 33678; 121.
DR DIP; DIP-3925N; -.
DR STRING; 4932.YJL078C; -.
DR iPTMnet; P47033; -.
DR MaxQB; P47033; -.
DR PaxDb; P47033; -.
DR PRIDE; P47033; -.
DR EnsemblFungi; YJL078C_mRNA; YJL078C; YJL078C. [P47033-1]
DR GeneID; 853367; -.
DR KEGG; sce:YJL078C; -.
DR SGD; S000003614; PRY3.
DR VEuPathDB; FungiDB:YJL078C; -.
DR eggNOG; KOG3017; Eukaryota.
DR GeneTree; ENSGT00980000198854; -.
DR HOGENOM; CLU_015197_0_0_1; -.
DR InParanoid; P47033; -.
DR OMA; IYTEVNA; -.
DR BioCyc; YEAST:G3O-31535-MON; -.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR PRO; PR:P47033; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P47033; protein.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0009277; C:fungal-type cell wall; 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 Alternative promoter usage; Cell wall; Glycoprotein; GPI-anchor;
KW Lipid transport; Lipoprotein; Membrane; Reference proteome; Secreted;
KW Signal; Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..853
FT /note="Cell wall protein PRY3"
FT /id="PRO_0000211549"
FT PROPEP 854..881
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000372447"
FT DOMAIN 30..144
FT /note="SCP"
FT REGION 262..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 453..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 758..788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 800..830
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 853
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:23038983"
FT CARBOHYD 360
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 488
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 535
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 547
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 569
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 625
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 881 AA; 89153 MW; 37DBAC660CA9D12A CRC64;
MLEFPISVLL GCLVAVKAQT TFPNFESDVL NEHNKFRALH VDTAPLTWSD TLATYAQNYA
DQYDCSGVLT HSDGPYGENL ALGYTDTGAV DAWYGEISKY NYSNPGFSES TGHFTQVVWK
STAEIGCGYK YCGTTWNNYI VCSYNPPGNY LGEFAEEVEP LISTVSSSSS SSSSTSTTSD
TVSTISSSIM PAVAQGYTTT VSSAASSSSL KSTTINPAKT ATLTASSSTV ITSSTESVGS
STVSSASSSS VTTSYATSSS TVVSSDATSS TTTTSSVATS SSTTSSDPTS STAAASSSDP
ASSSAAASSS ASTENAASSS SAISSSSSMV SAPLSSTLTT STASSRSVTS NSVNSVKFAN
TTVFSAQTTS SVSASLSSSV AADDIQGSTS KEATSSVSEH TSIVTSATNA AQYATRLGSS
SRSSSGAVSS SAVSQSVLNS VIAVNTDVSV TSVSSTAHTT KDTATTSVTA SESITSETAQ
ASSSTEKNIS NSAATSSSIY SNSASVSGHG VTYAAEYAIT SEQSSALATS VPATNCSSIV
KTTTLENSST TTITAITKST TTLATTANNS TRAATAVTID PTLDPTDNSA SPTDNAKHTS
TYGSSSTGAS LDSLRTTTSI SVSSNTTQLV STCTSESDYS DSPSFAISTA TTTESNLITN
TITASCSTDS NFPTSAASST DETAFTRTIS TSCSTLNGAS TQTSELTTSP MKTNTVVPAS
SFPSTTTTCL ENDDTAFSSI YTEVNAATII NPGETSSLAS DFATSEKPNE PTSVKSTSNE
GTSSTTTTYQ QTVATLYAKP SSTSLGARTT TGSNGRSTTS QQDGSAMHQP TSSIYTQLKE
GTSTTAKLSA YEGAATPLSI FQCNSLAGTI AAFVVAVLFA F
