ECM33_YEAST
ID ECM33_YEAST Reviewed; 429 AA.
AC P38248; D6VQ77; P89498;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 3.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Cell wall protein ECM33;
DE AltName: Full=Extracellular mutant protein 33;
DE Flags: Precursor;
GN Name=ECM33; OrderedLocusNames=YBR078W; ORFNames=YBR0727;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7985423; DOI=10.1002/yea.320100711;
RA van der Aart Q.J.M., Barthe C., Doignon F., Aigle M., Crouzet M.,
RA Steensma H.Y.;
RT "Sequence analysis of a 31 kb DNA fragment from the right arm of
RT Saccharomyces cerevisiae chromosome II.";
RL Yeast 10:959-964(1994).
RN [2]
RP SEQUENCE REVISION.
RA van der Aart Q.J.M.;
RL Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [4]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 428.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP IDENTIFICATION.
RX PubMed=9335584; DOI=10.1093/genetics/147.2.435;
RA Lussier M., White A.-M., Sheraton J., di Paolo T., Treadwell J.,
RA Southard S.B., Horenstein C.I., Chen-Weiner J., Ram A.F.J., Kapteyn J.C.,
RA Roemer T.W., Vo D.H., Bondoc D.C., Hall J., Zhong W.-W., Sdicu A.-M.,
RA Davies J., Klis F.M., Robbins P.W., Bussey H.;
RT "Large scale identification of genes involved in cell surface biosynthesis
RT and architecture in Saccharomyces cerevisiae.";
RL Genetics 147:435-450(1997).
RN [6]
RP GPI-ANCHOR, AND SUBCELLULAR LOCATION.
RX PubMed=10383953; DOI=10.1128/jb.181.13.3886-3889.1999;
RA Hamada K., Terashima H., Arisawa M., Yabuki N., Kitada K.;
RT "Amino acid residues in the omega-minus region participate in cellular
RT localization of yeast glycosylphosphatidylinositol-attached proteins.";
RL J. Bacteriol. 181:3886-3889(1999).
RN [7]
RP IDENTIFICATION OF INTRON.
RX PubMed=10734188; DOI=10.1093/nar/28.8.1700;
RA Davis C.A., Grate L., Spingola M., Ares M. Jr.;
RT "Test of intron predictions reveals novel splice sites, alternatively
RT spliced mRNAs and new introns in meiotically regulated genes of yeast.";
RL Nucleic Acids Res. 28:1700-1706(2000).
RN [8]
RP FUNCTION.
RX PubMed=11957109; DOI=10.1007/s10142-001-0043-1;
RA Bidlingmaier S., Snyder M.A.;
RT "Large-scale identification of genes important for apical growth in
RT Saccharomyces cerevisiae by directed allele replacement technology (DART)
RT screening.";
RL Funct. Integr. Genomics 1:345-356(2002).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12583915; DOI=10.1111/j.1574-6968.2003.tb11515.x;
RA Terashima H., Hamada K., Kitada K.;
RT "The localization change of Ybr078w/Ecm33, a yeast GPI-associated protein,
RT from the plasma membrane to the cell wall, affecting the cellular
RT function.";
RL FEMS Microbiol. Lett. 218:175-180(2003).
RN [10]
RP FUNCTION.
RX PubMed=15583168; DOI=10.1099/mic.0.26924-0;
RA Pardo M., Monteoliva L., Vazquez P., Martinez R., Molero G., Nombela C.,
RA Gil C.;
RT "PST1 and ECM33 encode two yeast cell surface GPI proteins important for
RT cell wall integrity.";
RL Microbiology 150:4157-4170(2004).
RN [11]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15781460; DOI=10.1074/jbc.m500334200;
RA Yin Q.Y., de Groot P.W.J., Dekker H.L., de Jong L., Klis F.M.,
RA de Koster C.G.;
RT "Comprehensive proteomic analysis of Saccharomyces cerevisiae cell walls:
RT identification of proteins covalently attached via
RT glycosylphosphatidylinositol remnants or mild alkali-sensitive linkages.";
RL J. Biol. Chem. 280:20894-20901(2005).
RN [12]
RP LEVEL OF PROTEIN EXPRESSION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17617218; DOI=10.1111/j.1567-1364.2007.00272.x;
RA Yin Q.Y., de Groot P.W.J., de Jong L., Klis F.M., de Koster C.G.;
RT "Mass spectrometric quantitation of covalently bound cell wall proteins in
RT Saccharomyces cerevisiae.";
RL FEMS Yeast Res. 7:887-896(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-339, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=17761666; DOI=10.1074/mcp.m700098-mcp200;
RA Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B.,
RA van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.;
RT "Profiling phosphoproteins of yeast mitochondria reveals a role of
RT phosphorylation in assembly of the ATP synthase.";
RL Mol. Cell. Proteomics 6:1896-1906(2007).
RN [14]
RP SUBCELLULAR LOCATION, GLYCOSYLATION, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=18434410; DOI=10.1128/jvi.00412-08;
RA Luallen R.J., Lin J., Fu H., Cai K.K., Agrawal C., Mboudjeka I., Lee F.-H.,
RA Montefiori D., Smith D.F., Doms R.W., Geng Y.;
RT "An engineered Saccharomyces cerevisiae strain binds the broadly
RT neutralizing human immunodeficiency virus type 1 antibody 2G12 and elicits
RT mannose-specific gp120-binding antibodies.";
RL J. Virol. 82:6447-6457(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. {ECO:0000269|PubMed:11957109,
CC ECO:0000269|PubMed:12583915, ECO:0000269|PubMed:15583168}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10383953,
CC ECO:0000269|PubMed:12583915, ECO:0000269|PubMed:18434410}; Lipid-
CC anchor, GPI-anchor {ECO:0000269|PubMed:10383953}. Secreted, cell wall
CC {ECO:0000269|PubMed:12583915, ECO:0000269|PubMed:15781460}.
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:0000269|PubMed:12583915,
CC ECO:0000269|PubMed:15781460}.
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.
CC {ECO:0000305}.
CC -!- PTM: Extensively N-glycosylated. {ECO:0000269|PubMed:18434410}.
CC -!- MISCELLANEOUS: Present with 6500 wall-bound molecules/cell in log phase
CC YPD medium. {ECO:0000269|PubMed:17617218}.
CC -!- SIMILARITY: Belongs to the SPS2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA53935.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA53935.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA85022.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA85023.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X76294; CAA53935.1; ALT_SEQ; Genomic_DNA.
DR EMBL; Z35947; CAA85022.1; ALT_FRAME; Genomic_DNA.
DR EMBL; Z35948; CAA85023.1; ALT_FRAME; Genomic_DNA.
DR EMBL; BK006936; DAA07197.2; -; Genomic_DNA.
DR PIR; S70297; S70297.
DR RefSeq; NP_009634.2; NM_001178426.2.
DR AlphaFoldDB; P38248; -.
DR SMR; P38248; -.
DR BioGRID; 32780; 354.
DR DIP; DIP-6584N; -.
DR IntAct; P38248; 4.
DR MINT; P38248; -.
DR STRING; 4932.YBR078W; -.
DR iPTMnet; P38248; -.
DR MaxQB; P38248; -.
DR PaxDb; P38248; -.
DR PRIDE; P38248; -.
DR EnsemblFungi; YBR078W_mRNA; YBR078W; YBR078W.
DR GeneID; 852370; -.
DR KEGG; sce:YBR078W; -.
DR SGD; S000000282; ECM33.
DR VEuPathDB; FungiDB:YBR078W; -.
DR eggNOG; ENOG502QUZC; Eukaryota.
DR GeneTree; ENSGT00940000176339; -.
DR HOGENOM; CLU_035846_0_0_1; -.
DR InParanoid; P38248; -.
DR OMA; GHNYECT; -.
DR BioCyc; YEAST:G3O-29046-MON; -.
DR PRO; PR:P38248; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38248; protein.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0031505; P:fungal-type cell wall organization; IMP:SGD.
DR Gene3D; 3.80.20.20; -; 1.
DR InterPro; IPR036941; Rcpt_L-dom_sf.
PE 1: Evidence at protein level;
KW Cell membrane; Cell wall; Cell wall biogenesis/degradation; Glycoprotein;
KW GPI-anchor; Lipoprotein; Membrane; Phosphoprotein; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..406
FT /note="Cell wall protein ECM33"
FT /id="PRO_0000033191"
FT PROPEP 407..429
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000033192"
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:0007744|PubMed:17761666"
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; 43769 MW; F57D94E1E53600CF CRC64;
MQFKNALTAT AILSASALAA NSTTSIPSSC 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
VTGNFSTLDL SSLKSVRGGA NFDSSSSNFS CNALKKLQSN GAIQGDSFVC KNGATSTSVK
LSSTSTESSK SSATSSASSS GDASNAQANV SASASSSSSS SKKSKGAAPE LVPATSFMGV
VAAVGVALL
