PIR1_YEAST
ID PIR1_YEAST Reviewed; 341 AA.
AC Q03178; D6VX35;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Cell wall mannoprotein PIR1;
DE AltName: Full=Covalently-linked cell wall protein 6;
DE AltName: Full=Protein with internal repeats 1;
DE Flags: Precursor;
GN Name=PIR1; Synonyms=CCW6; OrderedLocusNames=YKL164C; ORFNames=YKL618;
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=RAY-3AD;
RX PubMed=8322511; DOI=10.1002/yea.320090504;
RA Toh-e A., Yasunaga S., Nisogi H., Tanaka K., Oguchi T., Matsui Y.;
RT "Three yeast genes, PIR1, PIR2 and PIR3, containing internal tandem
RT repeats, are related to each other, and PIR1 and PIR2 are required for
RT tolerance to heat shock.";
RL Yeast 9:481-494(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091859; DOI=10.1002/yea.320100005;
RA Vandenbol M., Bolle P.-A., Dion C., Portetelle D., Hilger F.;
RT "DNA sequencing of a 36.2 kb fragment located between the FAS1 and LAP loci
RT of chromosome XI of Saccharomyces cerevisiae.";
RL Yeast 10:S35-S40(1994).
RN [3]
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 [4]
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 [5]
RP PROTEIN SEQUENCE OF 19-25 AND 64-84, CLEAVAGE BY KEX2, GLYCOSYLATION, AND
RP SUBCELLULAR LOCATION.
RX PubMed=9301021;
RX DOI=10.1002/(sici)1097-0061(19970930)13:12<1145::aid-yea163>3.0.co;2-y;
RA Mrsa V., Seidl T., Gentzsch M., Tanner W.;
RT "Specific labelling of cell wall proteins by biotinylation. Identification
RT of four covalently linked O-mannosylated proteins of Saccharomyces
RT cerevisiae.";
RL Yeast 13:1145-1154(1997).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9192695; DOI=10.1073/pnas.94.13.7082;
RA Yun D.-J., Zhao Y., Pardo J.M., Narasimhan M.L., Damsz B., Lee H.,
RA Abad L.R., D'Urzo M.P., Hasegawa P.M., Bressan R.A.;
RT "Stress proteins on the yeast cell surface determine resistance to osmotin,
RT a plant antifungal protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:7082-7087(1997).
RN [7]
RP INDUCTION.
RX PubMed=10594829; DOI=10.1046/j.1365-2958.1999.01667.x;
RA Jung U.S., Levin D.E.;
RT "Genome-wide analysis of gene expression regulated by the yeast cell wall
RT integrity signalling pathway.";
RL Mol. Microbiol. 34:1049-1057(1999).
RN [8]
RP FUNCTION.
RX PubMed=10407261;
RX DOI=10.1002/(sici)1097-0061(199907)15:10a<813::aid-yea421>3.0.co;2-y;
RA Mrsa V., Tanner W.;
RT "Role of NaOH-extractable cell wall proteins Ccw5p, Ccw6p, Ccw7p and Ccw8p
RT (members of the Pir protein family) in stability of the Saccharomyces
RT cerevisiae cell wall.";
RL Yeast 15:813-820(1999).
RN [9]
RP INDUCTION.
RX PubMed=11309124; DOI=10.1046/j.1365-2958.2001.02388.x;
RA Doolin M.-T., Johnson A.L., Johnston L.H., Butler G.;
RT "Overlapping and distinct roles of the duplicated yeast transcription
RT factors Ace2p and Swi5p.";
RL Mol. Microbiol. 40:422-432(2001).
RN [10]
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 [11]
RP FUNCTION.
RX PubMed=15470095; DOI=10.1099/mic.0.27296-0;
RA Teparic R., Stuparevic I., Mrsa V.;
RT "Increased mortality of Saccharomyces cerevisiae cell wall protein
RT mutants.";
RL Microbiology 150:3145-3150(2004).
RN [12]
RP INDUCTION.
RX PubMed=15116342; DOI=10.1002/yea.1109;
RA Boorsma A., de Nobel H., ter Riet B., Bargmann B., Brul S.,
RA Hellingwerf K.J., Klis F.M.;
RT "Characterization of the transcriptional response to cell wall stress in
RT Saccharomyces cerevisiae.";
RL Yeast 21:413-427(2004).
RN [13]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
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 [14]
RP REPEATS.
RX PubMed=16086015; DOI=10.1038/ng1618;
RA Verstrepen K.J., Jansen A., Lewitter F., Fink G.R.;
RT "Intragenic tandem repeats generate functional variability.";
RL Nat. Genet. 37:986-990(2005).
CC -!- FUNCTION: Component of the outer cell wall layer. Required for
CC stability of the cell wall and for optimal growth. Required for
CC resistance against several antifungal and cell wall-perturbing agents
CC and for tolerance to heat shock. {ECO:0000269|PubMed:10407261,
CC ECO:0000269|PubMed:15470095, ECO:0000269|PubMed:9192695}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:15781460,
CC ECO:0000269|PubMed:9192695, ECO:0000269|PubMed:9301021}.
CC Note=Covalently attached to the cell wall.
CC -!- INDUCTION: Positively regulated by signaling through MPK1 in response
CC to cell wall perturbation. Expression is also regulated by the SWI5
CC transcription factor. {ECO:0000269|PubMed:10594829,
CC ECO:0000269|PubMed:11309124, ECO:0000269|PubMed:15116342}.
CC -!- DOMAIN: The PIR1/2/3 repeats are required for covalent linkage to the
CC cell wall (By similarity). Their number varies among different strains
CC of S.cerevisiae. {ECO:0000250}.
CC -!- PTM: Covalently linked to beta-1,3-glucan of the inner cell wall layer
CC via an alkali-sensitive ester linkage between the gamma-carboxyl group
CC of glutamic acids, arising from specific glutamines within the PIR1/2/3
CC repeats, and hydroxyl groups of glucoses of beta-1,3-glucan chains.
CC {ECO:0000250}.
CC -!- PTM: O-glycosylated. Extensively O-mannosylated.
CC {ECO:0000269|PubMed:9301021}.
CC -!- MISCELLANEOUS: Present with 1170 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the PIR protein family. {ECO:0000305}.
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DR EMBL; D13740; BAA02885.1; -; Genomic_DNA.
DR EMBL; Z26877; CAA81490.1; -; Genomic_DNA.
DR EMBL; Z28164; CAA82006.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09001.1; -; Genomic_DNA.
DR PIR; S33650; S33650.
DR RefSeq; NP_012757.1; NM_001179730.1.
DR AlphaFoldDB; Q03178; -.
DR BioGRID; 33974; 69.
DR DIP; DIP-4607N; -.
DR IntAct; Q03178; 11.
DR MINT; Q03178; -.
DR STRING; 4932.YKL164C; -.
DR MaxQB; Q03178; -.
DR PaxDb; Q03178; -.
DR PRIDE; Q03178; -.
DR EnsemblFungi; YKL164C_mRNA; YKL164C; YKL164C.
DR GeneID; 853692; -.
DR KEGG; sce:YKL164C; -.
DR SGD; S000001647; PIR1.
DR VEuPathDB; FungiDB:YKL164C; -.
DR eggNOG; ENOG502QQD8; Eukaryota.
DR GeneTree; ENSGT00940000176350; -.
DR HOGENOM; CLU_039662_0_0_1; -.
DR InParanoid; Q03178; -.
DR OMA; AETCKSS; -.
DR BioCyc; YEAST:G3O-31932-MON; -.
DR PRO; PR:Q03178; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; Q03178; protein.
DR GO; GO:0005621; C:cellular bud scar; IDA:SGD.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:SGD.
DR GO; GO:0034399; C:nuclear periphery; IDA:SGD.
DR GO; GO:0005199; F:structural constituent of cell wall; IDA:SGD.
DR GO; GO:0031505; P:fungal-type cell wall organization; IMP:SGD.
DR GO; GO:0006886; P:intracellular protein transport; IMP:SGD.
DR InterPro; IPR000420; Yeast_PIR.
DR Pfam; PF00399; PIR; 8.
DR PROSITE; PS00929; PIR_REPEAT_1; 8.
DR PROSITE; PS50256; PIR_REPEAT_2; 8.
PE 1: Evidence at protein level;
KW Cell wall; Cell wall biogenesis/degradation;
KW Cleavage on pair of basic residues; Direct protein sequencing;
KW Glycoprotein; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:9301021"
FT PROPEP 19..63
FT /evidence="ECO:0000269|PubMed:9301021"
FT /id="PRO_0000033254"
FT CHAIN 64..341
FT /note="Cell wall mannoprotein PIR1"
FT /id="PRO_0000033255"
FT REPEAT 64..82
FT /note="PIR1/2/3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00149,
FT ECO:0000269|PubMed:16086015"
FT REPEAT 83..101
FT /note="PIR1/2/3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00149,
FT ECO:0000269|PubMed:16086015"
FT REPEAT 102..125
FT /note="PIR1/2/3 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00149,
FT ECO:0000269|PubMed:16086015"
FT REPEAT 126..144
FT /note="PIR1/2/3 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00149,
FT ECO:0000269|PubMed:16086015"
FT REPEAT 145..163
FT /note="PIR1/2/3 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00149,
FT ECO:0000269|PubMed:16086015"
FT REPEAT 164..182
FT /note="PIR1/2/3 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00149,
FT ECO:0000269|PubMed:16086015"
FT REPEAT 183..201
FT /note="PIR1/2/3 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00149,
FT ECO:0000269|PubMed:16086015"
FT REPEAT 202..220
FT /note="PIR1/2/3 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00149,
FT ECO:0000269|PubMed:16086015"
FT SITE 63..64
FT /note="Cleavage; by KEX2"
FT SITE 74
FT /note="Covalent attachment to cell wall glycan"
FT /evidence="ECO:0000250"
FT SITE 93
FT /note="Covalent attachment to cell wall glycan"
FT /evidence="ECO:0000250"
FT SITE 112
FT /note="Covalent attachment to cell wall glycan"
FT /evidence="ECO:0000250"
FT SITE 136
FT /note="Covalent attachment to cell wall glycan"
FT /evidence="ECO:0000250"
FT SITE 155
FT /note="Covalent attachment to cell wall glycan"
FT /evidence="ECO:0000250"
FT SITE 174
FT /note="Covalent attachment to cell wall glycan"
FT /evidence="ECO:0000250"
FT SITE 193
FT /note="Covalent attachment to cell wall glycan"
FT /evidence="ECO:0000250"
FT SITE 212
FT /note="Covalent attachment to cell wall glycan"
FT /evidence="ECO:0000250"
SQ SEQUENCE 341 AA; 34622 MW; 15F0736244769C12 CRC64;
MQYKKSLVAS ALVATSLAAY APKDPWSTLT PSATYKGGIT DYSSTFGIAV EPIATTASSK
AKRAAAISQI GDGQIQATTK TTAAAVSQIG DGQIQATTKT KAAAVSQIGD GQIQATTKTT
SAKTTAAAVS QIGDGQIQAT TKTKAAAVSQ IGDGQIQATT KTTAAAVSQI GDGQIQATTK
TTAAAVSQIG DGQIQATTNT TVAPVSQITD GQIQATTLTS ATIIPSPAPA PITNGTDPVT
AETCKSSGTL EMNLKGGILT DGKGRIGSIV ANRQFQFDGP PPQAGAIYAA GWSITPEGNL
AIGDQDTFYQ CLSGNFYNLY DEHIGTQCNA VHLQAIDLLN C
