PIR5_YEAS1
ID PIR5_YEAS1 Reviewed; 287 AA.
AC B3LPW3;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 28.
DE RecName: Full=Cell wall protein PIR5;
DE AltName: Full=Protein with internal repeats 5;
DE Flags: Precursor;
GN Name=PIR5; ORFNames=SCRG_03516;
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. 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; CH408050; EDV12616.1; -; Genomic_DNA.
DR AlphaFoldDB; B3LPW3; -.
DR PRIDE; B3LPW3; -.
DR EnsemblFungi; EDV12616; EDV12616; SCRG_03516.
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 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_0000377620"
FT CHAIN 63..287
FT /note="Cell wall protein PIR5"
FT /id="PRO_0000377742"
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