PIR3_YEAST
ID PIR3_YEAST Reviewed; 325 AA.
AC Q03180; D6VX36;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 3.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Cell wall mannoprotein PIR3;
DE AltName: Full=Covalently-linked cell wall protein 8;
DE AltName: Full=Protein with internal repeats 3;
DE Flags: Precursor;
GN Name=PIR3; Synonyms=CCW8; OrderedLocusNames=YKL163W; ORFNames=YKL617;
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 19-22, CLEAVAGE BY KEX2, AND GLYCOSYLATION.
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 PROTEIN SEQUENCE OF 68-77.
RC STRAIN=RH732;
RX PubMed=8314797; DOI=10.1016/s0021-9258(19)85250-x;
RA Singer-Krueger B., Frank R., Crausaz F., Riezman H.;
RT "Partial purification and characterization of early and late endosomes from
RT yeast. Identification of four novel proteins.";
RL J. Biol. Chem. 268:14376-14386(1993).
RN [7]
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 [8]
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 [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
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 [10]
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 [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).
RN [15]
RP INDUCTION.
RX PubMed=17617218; DOI=10.1111/j.1567-1364.2007.00272.x;
RA Yin Q.Y., de Groot P.W.J., de Jong L., Klis F.M., de Koster C.G.;
RT "Mass spectrometric quantitation of covalently bound cell wall proteins in
RT Saccharomyces cerevisiae.";
RL FEMS Yeast Res. 7:887-896(2007).
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 {ECO:0000269|PubMed:10407261, ECO:0000269|PubMed:15470095,
CC ECO:0000269|PubMed:9192695}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:10407261,
CC ECO:0000269|PubMed:15781460, ECO:0000269|PubMed:9192695}.
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 regulated by the ACE2 and SWI5
CC transcription factors. {ECO:0000269|PubMed:10594829,
CC ECO:0000269|PubMed:11309124, ECO:0000269|PubMed:15116342,
CC ECO:0000269|PubMed:17617218}.
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 -!- SIMILARITY: Belongs to the PIR protein family. {ECO:0000305}.
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DR EMBL; D13742; BAA02887.1; -; Genomic_DNA.
DR EMBL; Z26877; CAA81491.1; -; Genomic_DNA.
DR EMBL; Z28163; CAA82005.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09002.1; -; Genomic_DNA.
DR PIR; S37788; S37788.
DR RefSeq; NP_012758.1; NM_001179729.1.
DR AlphaFoldDB; Q03180; -.
DR BioGRID; 33975; 41.
DR DIP; DIP-4752N; -.
DR IntAct; Q03180; 1.
DR STRING; 4932.YKL163W; -.
DR PaxDb; Q03180; -.
DR PRIDE; Q03180; -.
DR EnsemblFungi; YKL163W_mRNA; YKL163W; YKL163W.
DR GeneID; 853693; -.
DR KEGG; sce:YKL163W; -.
DR SGD; S000001646; PIR3.
DR VEuPathDB; FungiDB:YKL163W; -.
DR eggNOG; ENOG502QQD8; Eukaryota.
DR GeneTree; ENSGT00940000176350; -.
DR HOGENOM; CLU_039662_0_0_1; -.
DR InParanoid; Q03180; -.
DR OMA; MQYKKPL; -.
DR BioCyc; YEAST:G3O-31931-MON; -.
DR PRO; PR:Q03180; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; Q03180; protein.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0009277; C:fungal-type cell wall; 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 InterPro; IPR000420; Yeast_PIR.
DR Pfam; PF00399; PIR; 7.
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..67
FT /evidence="ECO:0000269|PubMed:8314797"
FT /id="PRO_0000033256"
FT CHAIN 68..325
FT /note="Cell wall mannoprotein PIR3"
FT /id="PRO_0000033257"
FT REPEAT 68..91
FT /note="PIR1/2/3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00149,
FT ECO:0000269|PubMed:16086015"
FT REPEAT 92..109
FT /note="PIR1/2/3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00149,
FT ECO:0000269|PubMed:16086015"
FT REPEAT 110..127
FT /note="PIR1/2/3 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00149,
FT ECO:0000269|PubMed:16086015"
FT REPEAT 128..145
FT /note="PIR1/2/3 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00149,
FT ECO:0000269|PubMed:16086015"
FT REPEAT 146..163
FT /note="PIR1/2/3 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00149,
FT ECO:0000269|PubMed:16086015"
FT REPEAT 164..181
FT /note="PIR1/2/3 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00149,
FT ECO:0000269|PubMed:16086015"
FT REPEAT 182..199
FT /note="PIR1/2/3 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00149,
FT ECO:0000269|PubMed:16086015"
FT REPEAT 200..217
FT /note="PIR1/2/3 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00149,
FT ECO:0000269|PubMed:16086015"
FT SITE 67..68
FT /note="Cleavage; by KEX2"
FT SITE 76
FT /note="Covalent attachment to cell wall glycan"
FT /evidence="ECO:0000250"
FT SITE 102
FT /note="Covalent attachment to cell wall glycan"
FT /evidence="ECO:0000250"
FT SITE 120
FT /note="Covalent attachment to cell wall glycan"
FT /evidence="ECO:0000250"
FT SITE 138
FT /note="Covalent attachment to cell wall glycan"
FT /evidence="ECO:0000250"
FT SITE 156
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 192
FT /note="Covalent attachment to cell wall glycan"
FT /evidence="ECO:0000250"
FT SITE 209
FT /note="Covalent attachment to cell wall glycan"
FT /evidence="ECO:0000250"
FT VARIANT 113
FT /note="V -> A (in strain: RAY-3AD)"
FT VARIANT 117
FT /note="T -> S (in strain: RAY-3AD)"
FT VARIANT 144
FT /note="S -> STAAAVSQITDGQVQAAKSTAAAASQISDGQVQAAKS (in
FT strain: RAY-3AD)"
SQ SEQUENCE 325 AA; 33004 MW; 7B5670510F8FD1A1 CRC64;
MQYKKPLVVS ALAATSLAAY APKDPWSTLT PSATYKGGIT DYSSSFGIAI EAVATSASSV
ASSKAKRAAS QIGDGQVQAA TTTAAVSKKS TAAAVSQITD GQVQAAKSTA AAVSQITDGQ
VQAAKSTAAA VSQITDGQVQ AAKSTAAAVS QITDGQVQAA KSTAAAASQI SDGQVQATTS
TKAAASQITD GQIQASKTTS GASQVSDGQV QATAEVKDAN DPVDVVSCNN NSTLSMSLSK
GILTDRKGRI GSIVANRQFQ FDGPPPQAGA IYAAGWSITP EGNLALGDQD TFYQCLSGDF
YNLYDKHIGS QCHEVYLQAI DLIDC
