ID   PIR3_YEAS1              Reviewed;         307 AA.
AC   B3LQU1;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 33.
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; ORFNames=SCRG_03864;
OS   Saccharomyces cerevisiae (strain RM11-1a) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=285006;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RM11-1a;
RG   The Broad Institute Genome Sequencing Platform;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Cuomo C.,
RA   Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M.,
RA   Mauceli E.W., Brockman W., MacCallum I.A., Rounsley S., Young S.K.,
RA   LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   O'Leary S., Kodira C.D., Zeng Q., Yandava C., Alvarado L., Pratt S.,
RA   Kruglyak L.;
RT   "Annotation of the Saccharomyces cerevisiae RM11-1a genome.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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       (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; CH408051; EDV12944.1; -; Genomic_DNA.
DR   AlphaFoldDB; B3LQU1; -.
DR   EnsemblFungi; EDV12944; EDV12944; SCRG_03864.
DR   HOGENOM; CLU_039662_0_0_1; -.
DR   Proteomes; UP000008335; 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; 6.
DR   PROSITE; PS00929; PIR_REPEAT_1; 7.
DR   PROSITE; PS50256; PIR_REPEAT_2; 7.
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..67
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000377606"
FT   CHAIN           68..307
FT                   /note="Cell wall mannoprotein PIR3"
FT                   /id="PRO_0000377607"
FT   REPEAT          66..84
FT                   /note="PIR1/2/3 1"
FT   REPEAT          92..109
FT                   /note="PIR1/2/3 2"
FT   REPEAT          110..127
FT                   /note="PIR1/2/3 3"
FT   REPEAT          128..145
FT                   /note="PIR1/2/3 4"
FT   REPEAT          146..163
FT                   /note="PIR1/2/3 5"
FT   REPEAT          164..181
FT                   /note="PIR1/2/3 6"
FT   REPEAT          182..199
FT                   /note="PIR1/2/3 7"
FT   SITE            67..68
FT                   /note="Cleavage; by KEX2"
FT                   /evidence="ECO:0000250"
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            191
FT                   /note="Covalent attachment to cell wall glycan"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   307 AA;  31234 MW;  1623387CBA736641 CRC64;
     MQYKKPLVVS ALAATSLAAY APKDPWSTLT PSATYKGGIT DYSSSFGIAI EAVATSASSV
     ASSKAKRAAS QIGDGQVQAA TTTAAVSKKS TAAAVSQITD GQVQAAKSTA AAASQISDGQ
     VQAAKSTAAA VSQITDGQVQ AAKSTAAAAS QISDGQVQAT TSTKAAASQI TDGQIQASKT
     TSGASQVSDG QVQATAEVKD ANDPVDVVSC NNNSTLSMSL SKGILTDRKG RIGSIVANRQ
     FQFDGPPPQA GAIYAAGWSI TPEGNLALGD QDTFYQCLSG DFYNLYDKHI GSQCHEVYLQ
     AIDLIDC