ID   PIR5_YEAS6              Reviewed;         287 AA.
AC   B5VL25;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   25-MAY-2022, entry version 25.
DE   RecName: Full=Cell wall protein PIR5;
DE   AltName: Full=Protein with internal repeats 5;
DE   Flags: Precursor;
GN   Name=PIR5; ORFNames=AWRI1631_100490;
OS   Saccharomyces cerevisiae (strain AWRI1631) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=545124;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AWRI1631;
RX   PubMed=18778279; DOI=10.1111/j.1567-1364.2008.00434.x;
RA   Borneman A.R., Forgan A.H., Pretorius I.S., Chambers P.J.;
RT   "Comparative genome analysis of a Saccharomyces cerevisiae wine strain.";
RL   FEMS Yeast Res. 8:1185-1195(2008).
CC   -!- FUNCTION: Component of the outer cell wall layer. May be involved in
CC       meiosis and sporulation (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   -!- SIMILARITY: Belongs to the PIR protein family. {ECO:0000305}.
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DR   EMBL; ABSV01001266; EDZ71370.1; -; Genomic_DNA.
DR   AlphaFoldDB; B5VL25; -.
DR   Proteomes; UP000008988; 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   InterPro; IPR000420; Yeast_PIR.
DR   Pfam; PF00399; PIR; 3.
DR   PROSITE; PS00929; PIR_REPEAT_1; 4.
DR   PROSITE; PS50256; PIR_REPEAT_2; 4.
PE   3: Inferred from homology;
KW   Cell wall; Cleavage on pair of basic residues; Repeat; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..62
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000377621"
FT   CHAIN           63..287
FT                   /note="Cell wall protein PIR5"
FT                   /id="PRO_0000377743"
FT   REPEAT          62..80
FT                   /note="PIR1/2/3 1"
FT   REPEAT          81..99
FT                   /note="PIR1/2/3 2"
FT   REPEAT          104..122
FT                   /note="PIR1/2/3 3"
FT   REPEAT          144..162
FT                   /note="PIR1/2/3 4"
FT   SITE            62..63
FT                   /note="Cleavage; by KEX2"
FT                   /evidence="ECO:0000255"
FT   SITE            72
FT                   /note="Covalent attachment to cell wall glycan"
FT                   /evidence="ECO:0000250"
FT   SITE            91
FT                   /note="Covalent attachment to cell wall glycan"
FT                   /evidence="ECO:0000250"
FT   SITE            114
FT                   /note="Covalent attachment to cell wall glycan"
FT                   /evidence="ECO:0000250"
FT   SITE            154
FT                   /note="Covalent attachment to cell wall glycan"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   287 AA;  30200 MW;  B1A86FC7C18E0428 CRC64;
     MHYKKAFLAS LLSSIALTAY APPEPWATLT PSSKMDGGTT EYRTSFGLAV IPFTVTESKV
     KRNVISQIND GQVQVTTQKL PHPVSQIGDG QIQVTTQKVP PVVSHIVSQI GDGQLQITTA
     KNVVTKSTIA VPSKTATATA TSTATAVSQI HDGQVQVTIS SASSSSVLSK SKLEPTKKPN
     NENVIKVQAC KSSGTLAITL QGGVLIDSNG RIGSIVANRQ FQFDGPPPQA GAIYAGGWSI
     TKHGTLAIGD NDVFYQCLSG TFYNLYDQSI GGQCNPVHLQ TVGLVDC