PIR3_YEAS7
ID PIR3_YEAS7 Reviewed; 415 AA.
AC A6ZZG1;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 25-MAY-2022, entry version 35.
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=SCY_3221;
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 (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; EDN60009.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ZZG1; -.
DR EnsemblFungi; EDN60009; EDN60009; SCY_3221.
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; 12.
DR PROSITE; PS00929; PIR_REPEAT_1; 13.
DR PROSITE; PS50256; PIR_REPEAT_2; 13.
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_0000377608"
FT CHAIN 68..415
FT /note="Cell wall mannoprotein PIR3"
FT /id="PRO_0000377609"
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 REPEAT 200..217
FT /note="PIR1/2/3 8"
FT REPEAT 218..235
FT /note="PIR1/2/3 9"
FT REPEAT 236..253
FT /note="PIR1/2/3 10"
FT REPEAT 254..271
FT /note="PIR1/2/3 11"
FT REPEAT 272..288
FT /note="PIR1/2/3 12"
FT REPEAT 289..307
FT /note="PIR1/2/3 13"
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 192
FT /note="Covalent attachment to cell wall glycan"
FT /evidence="ECO:0000250"
FT SITE 210
FT /note="Covalent attachment to cell wall glycan"
FT /evidence="ECO:0000250"
FT SITE 228
FT /note="Covalent attachment to cell wall glycan"
FT /evidence="ECO:0000250"
FT SITE 246
FT /note="Covalent attachment to cell wall glycan"
FT /evidence="ECO:0000250"
FT SITE 264
FT /note="Covalent attachment to cell wall glycan"
FT /evidence="ECO:0000250"
FT SITE 282
FT /note="Covalent attachment to cell wall glycan"
FT /evidence="ECO:0000250"
FT SITE 299
FT /note="Covalent attachment to cell wall glycan"
FT /evidence="ECO:0000250"
SQ SEQUENCE 415 AA; 41476 MW; 732AA0BC2A2A9E82 CRC64;
MQYKKPLVVS ALAATSLAAY APKDPWSTLT PSATYKGGIT DYSSSFGIAI EAVATSASSV
ASSKAKRAAS QIGDGQVQAA TTTAAVSKKS TAAAVSQITD GQVQAAKSTA AAASQISDGQ
VQAAKSTAAA VSQITDGQVQ AAKSTAAAVS QITDGQVQAA KSTAAAVSQI TDGQVQAAKS
TAAAVSQITD GQVQAAKSTA AAASQISDGQ VQAAKSTAAA ASQISDGQVQ AAKSTAAAAS
QISDGQVQAA KSTAAAASQI SDGQVQATTS TKAAASQITD GQIQASKTTS GASQVSDGQV
QATAEVKDAN DPVDVVSCNN NSTLSMSLSK GILTDRKGRI GSIVANRQFQ FDGPPPQAGA
IYAAGWSITP EGNLALGDQD TFYQCLSGDF YNLYDKHIGS QCHEVYLQAI DLIDC
