ID   HS150_YEAS6             Reviewed;         303 AA.
AC   B5VL26;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   25-MAY-2022, entry version 30.
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=AWRI1631_100500;
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. 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; ABSV01001267; EDZ71368.1; -; Genomic_DNA.
DR   AlphaFoldDB; B5VL26; -.
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   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   InterPro; IPR000420; Yeast_PIR.
DR   Pfam; PF00399; PIR; 4.
DR   PROSITE; PS00929; PIR_REPEAT_1; 5.
DR   PROSITE; PS50256; PIR_REPEAT_2; 5.
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_0000377616"
FT   CHAIN           73..303
FT                   /note="Cell wall mannoprotein HSP150"
FT                   /id="PRO_0000377617"
FT   REPEAT          71..89
FT                   /note="PIR1/2/3 1"
FT   REPEAT          97..113
FT                   /note="PIR1/2/3 2"
FT   REPEAT          114..134
FT                   /note="PIR1/2/3 3; degenerate"
FT   REPEAT          135..153
FT                   /note="PIR1/2/3 4"
FT   REPEAT          154..171
FT                   /note="PIR1/2/3 5"
FT   REPEAT          172..190
FT                   /note="PIR1/2/3 6"
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            145
FT                   /note="Covalent attachment to cell wall glycan"
FT                   /evidence="ECO:0000250"
FT   SITE            164
FT                   /note="Covalent attachment to cell wall glycan"
FT                   /evidence="ECO:0000250"
FT   SITE            182
FT                   /note="Covalent attachment to cell wall glycan"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   303 AA;  30529 MW;  8975D61EC80FCF3C CRC64;
     MQYKKTLVAS ALAATTLAAY APSEPWSTLT PTATYSGGVT DYASTFGIAV QPISTTSSAS
     SAATTASSKA KRAASQIGDG QVQAATTTAS VSTKSSAAAV SQIGDGQIQA TTKTTAAASL
     KLVMVKIQAT TKTTAAAVSQ IGDGQVQATT KTTAAAVSQI TDGQVQATTK TTQAASQVSD
     GQVQATSATS ASAAATSTDP VDAVSCKTSG TLEMNLKGGI LTDGKGRIGS IVANRQFQFD
     GPPPQAGAIY AAGWSITPDG NLAIGDNDVF YQCLSGTFYN LYDEHIGSQC TPVHLEAIDL
     IDC