PST1_YEAS7
ID PST1_YEAS7 Reviewed; 444 AA.
AC A6ZY20;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 25-MAY-2022, entry version 51.
DE RecName: Full=Cell wall mannoprotein PST1;
DE AltName: Full=Haze protective factor 2;
DE AltName: Full=Protoplast secreted protein 1;
DE Flags: Precursor;
GN Name=PST1; Synonyms=HPF2; ORFNames=SCY_0958;
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: Has a partially redundant function to ECM33 in cell wall
CC integrity. May be involved in a repair mechanism activated in response
CC to cell wall damage (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC anchor {ECO:0000250}. Secreted, cell wall {ECO:0000250}.
CC Note=Identified as GPI-anchored plasma membrane protein (GPI-PMP) as
CC well as non-covalently-linked, soluble protein of the cell wall.
CC Secreted by regenerating protoplasts. In budded cells, concentrates at
CC the surface of the buds (By similarity). {ECO:0000250}.
CC -!- INDUCTION: Positively regulated by cell integrity signaling through
CC MPK1 in response to cell wall perturbation. Induction is dependent on
CC transcription factor RLM1 (By similarity). {ECO:0000250}.
CC -!- PTM: Extensively N- and O-mannosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SPS2 family. {ECO:0000305}.
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DR EMBL; AAFW02000145; EDN60400.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ZY20; -.
DR SMR; A6ZY20; -.
DR EnsemblFungi; EDN60400; EDN60400; SCY_0958.
DR HOGENOM; CLU_035846_0_0_1; -.
DR Proteomes; UP000007060; Unassembled WGS sequence.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR Gene3D; 3.80.20.20; -; 2.
DR InterPro; IPR036941; Rcpt_L-dom_sf.
PE 3: Inferred from homology;
KW Cell membrane; Cell wall; Glycoprotein; GPI-anchor; Lipoprotein; Membrane;
KW Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..419
FT /note="Cell wall mannoprotein PST1"
FT /id="PRO_0000330255"
FT PROPEP 420..444
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000330256"
FT REGION 359..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..379
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 419
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 76
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 235
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 268
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 305
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 329
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 444 AA; 45807 MW; 970F60CACA453C65 CRC64;
MQLHSLIAST ALLITSALAA TSSSSSIPSS CTISSHATAT AQSDLDKYSR CDTLVGNLTI
GGGLKTGALA NVKEINGSLT IFNATNLTSF AADSLESITD SLNLQSLTIL TSASFGSLQS
VDSIKLITLP AISSFTSNIK SANNIYISDT SLQSVDGFSA LKKVNVFNVN NNKKLTSIKS
PVETVSDSLQ FSFNGNQTKI TFDDLVWANN ISLTDVHSVS FANLQKINSS LGFINNSISS
LNFTKLNTIG QTFSIVSNDY LKNLSFSNLS TIGGALVVAN NTGLQKIGGL DNLTTIGGTL
EVVGNFTSLN LDSLKSVKGG ADVESKSSNF SCNALKALQK KGGIKGESFV CKNGASSTSV
KLSSTSKSQS SQTTAKVSKS SSKAEEKKFT SGDIKAAASA SSVSSSSASS SSSKSSKGNA
AIMAPIGQTT PLVGLLTAII MSIM
