ECM33_YEAS2
ID ECM33_YEAS2 Reviewed; 430 AA.
AC C7GQJ1;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-OCT-2009, sequence version 1.
DT 25-MAY-2022, entry version 38.
DE RecName: Full=Cell wall protein ECM33;
DE AltName: Full=Extracellular mutant protein 33;
DE Flags: Precursor;
GN Name=ECM33; ORFNames=C1Q_02579;
OS Saccharomyces cerevisiae (strain JAY291) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=574961;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JAY291;
RX PubMed=19812109; DOI=10.1101/gr.091777.109;
RA Argueso J.L., Carazzolle M.F., Mieczkowski P.A., Duarte F.M., Netto O.V.C.,
RA Missawa S.K., Galzerani F., Costa G.G.L., Vidal R.O., Noronha M.F.,
RA Dominska M., Andrietta M.G.S., Andrietta S.R., Cunha A.F., Gomes L.H.,
RA Tavares F.C.A., Alcarde A.R., Dietrich F.S., McCusker J.H., Petes T.D.,
RA Pereira G.A.G.;
RT "Genome structure of a Saccharomyces cerevisiae strain widely used in
RT bioethanol production.";
RL Genome Res. 19:2258-2270(2009).
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}.
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DR EMBL; ACFL01000124; EEU06930.1; -; Genomic_DNA.
DR AlphaFoldDB; C7GQJ1; -.
DR SMR; C7GQJ1; -.
DR Proteomes; UP000008073; 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..407
FT /note="Cell wall protein ECM33"
FT /id="PRO_0000392090"
FT PROPEP 408..430
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000392091"
FT REGION 362..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 340
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38248"
FT LIPID 407
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT CARBOHYD 22
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 57
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 197
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 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 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 430 AA; 43843 MW; 078F3141E8CF21D6 CRC64;
MQFKNALTAT AILSASALAG TNSTTSIPSS CSIGTSATAT AQADLDKISG CSTIVGNLTI
TGDLGSAALA SIQEIDGSLT IFNSSSLSSF SADSIKKITG DLNMQELIIL TSASFGSLQE
VDSINMVTLP AISTFSTDLQ NANNIIVSDT TLESVEGFST LKKVNVFNIN NNRYLNSFQS
SLESVSDSLQ FSSNGDNTTL AFDNLVWANN ITLRDVNSIS FGSLQTVNAS LGFINNTLPS
LNLTQLSKVG QSLSIVSNDE LSKAAFSNLT TVGGGFIIAN NTQLKVIDGF NKVQTVGGAI
EVTGNFSTLD LSSLKSVRGG ANFDSSSSNF SCNALKKLQS NGAIQGDSFV CKNGATSTSV
KLSSTSTESS KSSATSSASS SGDASNAQAS VSASASSSSS SSKKSKGAAP ELVPATSFMG
VVAAVAVALL
