HS150_YEAS1
ID HS150_YEAS1 Reviewed; 368 AA.
AC B3LPW4;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 32.
DE RecName: Full=Cell wall mannoprotein HSP150;
DE AltName: Full=150 kDa heat shock glycoprotein;
DE AltName: Full=Covalently-linked cell wall protein 7;
DE AltName: Full=Protein with internal repeats 2;
DE Flags: Precursor;
GN Name=HSP150; ORFNames=SCRG_03517;
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 and for tolerance to heat shock (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: The propeptide is cleaved off in the late Golgi. While both
CC peptides are secreted, only a fraction of the mature glycoprotein is
CC incorporated into the cell wall (By similarity). {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; CH408050; EDV12617.1; -; Genomic_DNA.
DR AlphaFoldDB; B3LPW4; -.
DR PRIDE; B3LPW4; -.
DR EnsemblFungi; EDV12617; EDV12617; SCRG_03517.
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; 7.
DR PROSITE; PS00929; PIR_REPEAT_1; 7.
DR PROSITE; PS50256; PIR_REPEAT_2; 9.
PE 3: Inferred from homology;
KW Cell wall; Cell wall biogenesis/degradation;
KW Cleavage on pair of basic residues; Glycoprotein; Repeat; Secreted; Signal;
KW Stress response.
FT SIGNAL 1..18
FT /evidence="ECO:0000250"
FT PROPEP 19..72
FT /evidence="ECO:0000250"
FT /id="PRO_0000377614"
FT CHAIN 73..368
FT /note="Cell wall mannoprotein HSP150"
FT /id="PRO_0000377615"
FT REPEAT 71..89
FT /note="PIR1/2/3 1"
FT REPEAT 97..113
FT /note="PIR1/2/3 2"
FT REPEAT 114..132
FT /note="PIR1/2/3 3"
FT REPEAT 138..156
FT /note="PIR1/2/3 4"
FT REPEAT 162..180
FT /note="PIR1/2/3 5"
FT REPEAT 181..199
FT /note="PIR1/2/3 6"
FT REPEAT 200..218
FT /note="PIR1/2/3 7"
FT REPEAT 219..236
FT /note="PIR1/2/3 8"
FT REPEAT 237..255
FT /note="PIR1/2/3 9"
FT SITE 72..73
FT /note="Cleavage; by KEX2"
FT /evidence="ECO:0000250"
FT SITE 81
FT /note="Covalent attachment to cell wall glycan"
FT /evidence="ECO:0000250"
FT SITE 107
FT /note="Covalent attachment to cell wall glycan"
FT /evidence="ECO:0000250"
FT SITE 124
FT /note="Covalent attachment to cell wall glycan"
FT /evidence="ECO:0000250"
FT SITE 148
FT /note="Covalent attachment to cell wall glycan"
FT /evidence="ECO:0000250"
FT SITE 172
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"
FT SITE 210
FT /note="Covalent attachment to cell wall glycan"
FT /evidence="ECO:0000250"
FT SITE 229
FT /note="Covalent attachment to cell wall glycan"
FT /evidence="ECO:0000250"
FT SITE 247
FT /note="Covalent attachment to cell wall glycan"
FT /evidence="ECO:0000250"
SQ SEQUENCE 368 AA; 36763 MW; C105CE824197D8A8 CRC64;
MQYKKTLVAS ALAATTLAAY APSEPWSTLT PTATYSGGVT DYASTFGIAV QPISTTSSAS
SAATTASSKA KRAASQIGDG QVQAATTTAS VSTKSSAAAV SQIGDGQIQA TTKTTAAAVS
RDGQIQATTK TTSAKTTAAA VSQIGDGQIQ ATTTTLAPKS TAAAVSQMGD GQIQATTKTT
AAAVSQIGDG QVQATTKTTA AAVSQIGDGQ VQATTKTTAA AVSQITDGQV QATTKTTQAA
SQVSDGQVQA TSATSASAAA TSTDPVDAVS CKTSGTLEMN LKGGILTDGK GRIGSIVANR
QFQFDGPPPQ AGAIYAAGWS ITPDGNLAIG DNDVFYQCLS GTFYNLYDEH IGSQCTPVHL
EAIDLIDC
