PIR5_YEAS7
ID PIR5_YEAS7 Reviewed; 287 AA.
AC A6ZQH2;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 25-MAY-2022, entry version 33.
DE RecName: Full=Cell wall protein PIR5;
DE AltName: Full=Protein with internal repeats 5;
DE Flags: Precursor;
GN Name=PIR5; ORFNames=SCY_3133;
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. 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; AAFW02000044; EDN63224.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ZQH2; -.
DR EnsemblFungi; EDN63224; EDN63224; SCY_3133.
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 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_0000377622"
FT CHAIN 63..287
FT /note="Cell wall protein PIR5"
FT /id="PRO_0000377744"
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; 30287 MW; BE20867CA0DECA65 CRC64;
MHYKKAFLAS LLSSIALTAY APPEPWATLT PSSKMDGGTT EYRTSFGLAV IPFTVTESKV
KRNVISQIND GQVQVTTQKL PHPVSQIGDG QIQVTTQKVP PVVSHIVSQI GDGQLQITTA
KNVVTKSTIA VPSKTVTATA TSTATAVSQI HDGQVQVTIS SASSSSVLSK SKLEPTKKPN
NEKVIKVQAC KSSGTLAITL QEGVLIDSSG RIGSIVANRQ FQFDGPPPQA GAIYAGGWSI
TKHGTLAIGD NDVFYQCLSG TFYNLYDQSI GGQCNPVHLQ TVGLVDC