ID   PIR1_YEAS7              Reviewed;         341 AA.
AC   A6ZZG0;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 35.
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; ORFNames=SCY_3220;
OS   Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=307796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJM789;
RX   PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA   Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA   Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA   Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA   Steinmetz L.M.;
RT   "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT   strain YJM789.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(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       and for tolerance to heat shock (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000250}.
CC       Note=Covalently attached to the cell wall. {ECO:0000250}.
CC   -!- DOMAIN: The PIR1/2/3 repeats are required for the covalent linkage to
CC       the cell wall (By similarity). Their number varies among different
CC       strains 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 (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PIR protein family. {ECO:0000305}.
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DR   EMBL; AAFW02000151; EDN60008.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6ZZG0; -.
DR   PRIDE; A6ZZG0; -.
DR   EnsemblFungi; EDN60008; EDN60008; SCY_3220.
DR   HOGENOM; CLU_039662_0_0_1; -.
DR   Proteomes; UP000007060; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0005199; F:structural constituent of cell wall; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   Cell wall; Cell wall biogenesis/degradation;
KW   Cleavage on pair of basic residues; Glycoprotein; Repeat; Secreted; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000250"
FT   PROPEP          19..63
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000377604"
FT   CHAIN           64..341
FT                   /note="Cell wall mannoprotein PIR1"
FT                   /id="PRO_0000377605"
FT   REPEAT          64..82
FT                   /note="PIR1/2/3 1"
FT   REPEAT          83..101
FT                   /note="PIR1/2/3 2"
FT   REPEAT          102..120
FT                   /note="PIR1/2/3 3"
FT   REPEAT          126..144
FT                   /note="PIR1/2/3 4"
FT   REPEAT          145..163
FT                   /note="PIR1/2/3 5"
FT   REPEAT          164..182
FT                   /note="PIR1/2/3 6"
FT   REPEAT          183..201
FT                   /note="PIR1/2/3 7"
FT   REPEAT          202..220
FT                   /note="PIR1/2/3 8"
FT   SITE            63..64
FT                   /note="Cleavage; by KEX2"
FT                   /evidence="ECO:0000250"
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;  34608 MW;  15F0668244769C12 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 VHLQAIDLVN C