HS150_YEAS7
ID HS150_YEAS7 Reviewed; 389 AA.
AC A6ZQH3;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 25-MAY-2022, entry version 37.
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=SCY_3134;
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. 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; AAFW02000044; EDN63225.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ZQH3; -.
DR EnsemblFungi; EDN63225; EDN63225; SCY_3134.
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 GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR InterPro; IPR000420; Yeast_PIR.
DR Pfam; PF00399; PIR; 10.
DR PROSITE; PS00929; PIR_REPEAT_1; 10.
DR PROSITE; PS50256; PIR_REPEAT_2; 10.
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_0000377618"
FT CHAIN 73..389
FT /note="Cell wall mannoprotein HSP150"
FT /id="PRO_0000377619"
FT REPEAT 71..89
FT /note="PIR1/2/3 1"
FT REPEAT 97..115
FT /note="PIR1/2/3 2"
FT REPEAT 116..134
FT /note="PIR1/2/3 3"
FT REPEAT 140..158
FT /note="PIR1/2/3 4"
FT REPEAT 164..182
FT /note="PIR1/2/3 5"
FT REPEAT 183..201
FT /note="PIR1/2/3 6"
FT REPEAT 202..220
FT /note="PIR1/2/3 7"
FT REPEAT 221..239
FT /note="PIR1/2/3 8"
FT REPEAT 240..257
FT /note="PIR1/2/3 9"
FT REPEAT 258..276
FT /note="PIR1/2/3 10"
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 126
FT /note="Covalent attachment to cell wall glycan"
FT /evidence="ECO:0000250"
FT SITE 150
FT /note="Covalent attachment to cell wall glycan"
FT /evidence="ECO:0000250"
FT SITE 174
FT /note="Covalent attachment to cell wall glycan"
FT /evidence="ECO:0000250"
FT SITE 193
FT /note="Covalent attachment to cell wall glycan"
FT /evidence="ECO:0000250"
FT SITE 212
FT /note="Covalent attachment to cell wall glycan"
FT /evidence="ECO:0000250"
FT SITE 231
FT /note="Covalent attachment to cell wall glycan"
FT /evidence="ECO:0000250"
FT SITE 250
FT /note="Covalent attachment to cell wall glycan"
FT /evidence="ECO:0000250"
FT SITE 268
FT /note="Covalent attachment to cell wall glycan"
FT /evidence="ECO:0000250"
SQ SEQUENCE 389 AA; 38717 MW; CF25682B9DB34FAE CRC64;
MQYKKTLVAS ALAATTLAAY APSEPWSTLT PTATYSGGVT DYASTFGIAV QPISTTSSAS
SAATTASSKA KRAASQIGDG QVQAATTTAS VSTKSTAAAV SQIGDGQVQA TTKTTAAAVS
QIGDGQIQAT TKTTSAKTTA AAVSQIGDGQ IQATTTTLAP KSTAAAVSQI GDGQVQATTK
TTAAAVSQIG DGQVQATTKT TAAAVSQIGD GQVQATTKTT AAAVSQIGDG QVQATTKTTA
AAVSQITDGQ VQATTKTTQA ASQVSDGQVQ ATTATSASAA ATSTDPVDAV SCKTSGTLEM
NLKGGILTDG KGRIGSIVAN RQFQFDGPPP QAGAIYAAGW SITPDGNLAI GDNDVFYQCL
SGTFYNLYDE HIGSQCTPVH LEAIDLIDC
