ECM33_YEAS6
ID ECM33_YEAS6 Reviewed; 429 AA.
AC B5VE42;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-MAR-2010, sequence version 2.
DT 25-MAY-2022, entry version 37.
DE RecName: Full=Cell wall protein ECM33;
DE AltName: Full=Extracellular mutant protein 33;
DE Flags: Precursor;
GN Name=ECM33; ORFNames=AWRI1631_21650;
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: Required for proper cell wall integrity and for the correct
CC assembly of the mannoprotein outer layer of the cell wall. Important
CC for apical bud growth (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 covalently-linked GPI-modified cell wall protein (GPI-CWP) in
CC the outer cell wall layer. {ECO:0000250}.
CC -!- PTM: The GPI-anchor is attached to the protein in the endoplasmic
CC reticulum and serves to target the protein to the cell surface. There,
CC the glucosamine-inositol phospholipid moiety is cleaved off and the
CC GPI-modified mannoprotein is covalently attached via its lipidless GPI
CC glycan remnant to the 1,6-beta-glucan of the outer cell wall layer (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SPS2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDZ73806.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; ABSV01000113; EDZ73806.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; B5VE42; -.
DR SMR; B5VE42; -.
DR Proteomes; UP000008988; 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 GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR Gene3D; 3.80.20.20; -; 1.
DR InterPro; IPR036941; Rcpt_L-dom_sf.
PE 3: Inferred from homology;
KW Cell membrane; Cell wall; Cell wall biogenesis/degradation; Glycoprotein;
KW GPI-anchor; Lipoprotein; Membrane; Phosphoprotein; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..406
FT /note="Cell wall protein ECM33"
FT /id="PRO_0000392092"
FT PROPEP 407..429
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000392093"
FT REGION 361..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..405
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 339
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38248"
FT LIPID 406
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT CARBOHYD 21
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 82
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 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 227
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 234
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 279
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 304
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 328
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 389
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 429 AA; 43831 MW; 76A9875AFA0AC037 CRC64;
MQFKNALTAT AILSASALAA NSSTSIPSSC SIGTSATATA QADLDKISGC STIVGNLTIT
GDLGSAALAS IQEIDGSLTI FNSSSLSSFS ADSIKKITGD LNMQELIILT SASFGSLQEV
DSINMVTLPA ISTFSTDLQN ANNIIVSDTT LESVEGFSTL KKVNVFNINN NRYLNSFQSS
LESVSDSLQF SSNGDNTTLA FDNLVWANNI TLRDVNSISF GSLQTVNASL GFINNTLPSL
NLTQLSKVGQ SLSIVSNDEL SKAAFSNLTT VGGGFIIANN TQLKVIDGFN KVQTVGGAIE
FTGNFSTLDL SSLKSVRGGA KFDSSSSNFS CNALKKLQSN GAIQGDSFVC KNGATSTSVK
LSSTSTESSK SSATSSASSS GDASNAQANV SASASSSSSS SKKSKGAAPE LVPATSFMGV
VAAVAVALL
