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Protein

Cell wall protein ECM33

Gene

ECM33

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Required for proper cell wall integrity and for the correct assembly of the mannoprotein outer layer of the cell wall. Important for apical bud growth.3 Publications

GO - Biological processi

  • fungal-type cell wall organization Source: SGD
Complete GO annotation...

Keywords - Biological processi

Cell wall biogenesis/degradation

Enzyme and pathway databases

BioCyciYEAST:G3O-29046-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Cell wall protein ECM33
Alternative name(s):
Extracellular mutant protein 33
Gene namesi
Name:ECM33
Ordered Locus Names:YBR078W
ORF Names:YBR0727
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:YBR078W.
SGDiS000000282. ECM33.

Subcellular locationi

GO - Cellular componenti

  • anchored component of membrane Source: UniProtKB-KW
  • extracellular region Source: UniProtKB-KW
  • fungal-type cell wall Source: SGD
  • plasma membrane Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell wall, Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence analysisAdd
BLAST
Chaini20 – 406387Cell wall protein ECM33PRO_0000033191Add
BLAST
Propeptidei407 – 42923Removed in mature formSequence analysisPRO_0000033192Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi21 – 211N-linked (GlcNAc...)Sequence analysis
Glycosylationi56 – 561N-linked (GlcNAc...)Sequence analysis
Glycosylationi82 – 821N-linked (GlcNAc...)Sequence analysis
Glycosylationi196 – 1961N-linked (GlcNAc...)Sequence analysis
Glycosylationi209 – 2091N-linked (GlcNAc...)Sequence analysis
Glycosylationi227 – 2271N-linked (GlcNAc...)Sequence analysis
Glycosylationi234 – 2341N-linked (GlcNAc...)Sequence analysis
Glycosylationi241 – 2411N-linked (GlcNAc...)Sequence analysis
Glycosylationi267 – 2671N-linked (GlcNAc...)Sequence analysis
Glycosylationi279 – 2791N-linked (GlcNAc...)Sequence analysis
Glycosylationi304 – 3041N-linked (GlcNAc...)Sequence analysis
Glycosylationi328 – 3281N-linked (GlcNAc...)Sequence analysis
Modified residuei339 – 3391PhosphoserineCombined sources
Glycosylationi389 – 3891N-linked (GlcNAc...)Sequence analysis
Lipidationi406 – 4061GPI-anchor amidated glycineSequence analysis

Post-translational modificationi

The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannoprotein is covalently attached via its lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer cell wall layer.Curated
Extensively N-glycosylated.1 Publication

Keywords - PTMi

Glycoprotein, GPI-anchor, Lipoprotein, Phosphoprotein

Proteomic databases

MaxQBiP38248.
PeptideAtlasiP38248.

PTM databases

iPTMnetiP38248.

Interactioni

Protein-protein interaction databases

BioGridi32780. 238 interactions.
DIPiDIP-6584N.
IntActiP38248. 2 interactions.
MINTiMINT-4805607.

Structurei

3D structure databases

ProteinModelPortaliP38248.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi311 – 40494Ser-richAdd
BLAST

Sequence similaritiesi

Belongs to the SPS2 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

GeneTreeiENSGT00530000065410.
HOGENOMiHOG000093252.
InParanoidiP38248.
OMAiQNTALRS.
OrthoDBiEOG74BK3P.

Family and domain databases

Gene3Di3.80.20.20. 1 hit.
InterProiIPR032675. L_dom-like.
IPR000494. Rcpt_L-dom.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 2 hits.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P38248-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQFKNALTAT AILSASALAA NSTTSIPSSC SIGTSATATA QADLDKISGC
60 70 80 90 100
STIVGNLTIT GDLGSAALAS IQEIDGSLTI FNSSSLSSFS ADSIKKITGD
110 120 130 140 150
LNMQELIILT SASFGSLQEV DSINMVTLPA ISTFSTDLQN ANNIIVSDTT
160 170 180 190 200
LESVEGFSTL KKVNVFNINN NRYLNSFQSS LESVSDSLQF SSNGDNTTLA
210 220 230 240 250
FDNLVWANNI TLRDVNSISF GSLQTVNASL GFINNTLPSL NLTQLSKVGQ
260 270 280 290 300
SLSIVSNDEL SKAAFSNLTT VGGGFIIANN TQLKVIDGFN KVQTVGGAIE
310 320 330 340 350
VTGNFSTLDL SSLKSVRGGA NFDSSSSNFS CNALKKLQSN GAIQGDSFVC
360 370 380 390 400
KNGATSTSVK LSSTSTESSK SSATSSASSS GDASNAQANV SASASSSSSS
410 420
SKKSKGAAPE LVPATSFMGV VAAVGVALL
Length:429
Mass (Da):43,769
Last modified:April 29, 2008 - v3
Checksum:iF57D94E1E53600CF
GO

Sequence cautioni

The sequence CAA53935.1 differs from that shown. Reason: Frameshift at position 428. Curated
The sequence CAA53935.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAA85022.1 differs from that shown. Reason: Frameshift at position 428. Curated
The sequence CAA85023.1 differs from that shown. Reason: Frameshift at position 428. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X76294 Genomic DNA. Translation: CAA53935.1. Sequence problems.
Z35947 Genomic DNA. Translation: CAA85022.1. Frameshift.
Z35948 Genomic DNA. Translation: CAA85023.1. Frameshift.
BK006936 Genomic DNA. Translation: DAA07197.2.
PIRiS70297.
RefSeqiNP_009634.2. NM_001178426.2.

Genome annotation databases

EnsemblFungiiYBR078W; YBR078W; YBR078W.
GeneIDi852370.
KEGGisce:YBR078W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X76294 Genomic DNA. Translation: CAA53935.1. Sequence problems.
Z35947 Genomic DNA. Translation: CAA85022.1. Frameshift.
Z35948 Genomic DNA. Translation: CAA85023.1. Frameshift.
BK006936 Genomic DNA. Translation: DAA07197.2.
PIRiS70297.
RefSeqiNP_009634.2. NM_001178426.2.

3D structure databases

ProteinModelPortaliP38248.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32780. 238 interactions.
DIPiDIP-6584N.
IntActiP38248. 2 interactions.
MINTiMINT-4805607.

PTM databases

iPTMnetiP38248.

Proteomic databases

MaxQBiP38248.
PeptideAtlasiP38248.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYBR078W; YBR078W; YBR078W.
GeneIDi852370.
KEGGisce:YBR078W.

Organism-specific databases

EuPathDBiFungiDB:YBR078W.
SGDiS000000282. ECM33.

Phylogenomic databases

GeneTreeiENSGT00530000065410.
HOGENOMiHOG000093252.
InParanoidiP38248.
OMAiQNTALRS.
OrthoDBiEOG74BK3P.

Enzyme and pathway databases

BioCyciYEAST:G3O-29046-MONOMER.

Miscellaneous databases

PROiP38248.

Family and domain databases

Gene3Di3.80.20.20. 1 hit.
InterProiIPR032675. L_dom-like.
IPR000494. Rcpt_L-dom.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence analysis of a 31 kb DNA fragment from the right arm of Saccharomyces cerevisiae chromosome II."
    van der Aart Q.J.M., Barthe C., Doignon F., Aigle M., Crouzet M., Steensma H.Y.
    Yeast 10:959-964(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. van der Aart Q.J.M.
    Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. "Complete DNA sequence of yeast chromosome II."
    Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C.
    , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
    EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 428.
    Strain: ATCC 204508 / S288c.
  5. "Large scale identification of genes involved in cell surface biosynthesis and architecture in Saccharomyces cerevisiae."
    Lussier M., White A.-M., Sheraton J., di Paolo T., Treadwell J., Southard S.B., Horenstein C.I., Chen-Weiner J., Ram A.F.J., Kapteyn J.C., Roemer T.W., Vo D.H., Bondoc D.C., Hall J., Zhong W.-W., Sdicu A.-M., Davies J., Klis F.M., Robbins P.W., Bussey H.
    Genetics 147:435-450(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
  6. "Amino acid residues in the omega-minus region participate in cellular localization of yeast glycosylphosphatidylinositol-attached proteins."
    Hamada K., Terashima H., Arisawa M., Yabuki N., Kitada K.
    J. Bacteriol. 181:3886-3889(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: GPI-ANCHOR, SUBCELLULAR LOCATION.
  7. "Test of intron predictions reveals novel splice sites, alternatively spliced mRNAs and new introns in meiotically regulated genes of yeast."
    Davis C.A., Grate L., Spingola M., Ares M. Jr.
    Nucleic Acids Res. 28:1700-1706(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF INTRON.
  8. "Large-scale identification of genes important for apical growth in Saccharomyces cerevisiae by directed allele replacement technology (DART) screening."
    Bidlingmaier S., Snyder M.A.
    Funct. Integr. Genomics 1:345-356(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "The localization change of Ybr078w/Ecm33, a yeast GPI-associated protein, from the plasma membrane to the cell wall, affecting the cellular function."
    Terashima H., Hamada K., Kitada K.
    FEMS Microbiol. Lett. 218:175-180(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  10. "PST1 and ECM33 encode two yeast cell surface GPI proteins important for cell wall integrity."
    Pardo M., Monteoliva L., Vazquez P., Martinez R., Molero G., Nombela C., Gil C.
    Microbiology 150:4157-4170(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Comprehensive proteomic analysis of Saccharomyces cerevisiae cell walls: identification of proteins covalently attached via glycosylphosphatidylinositol remnants or mild alkali-sensitive linkages."
    Yin Q.Y., de Groot P.W.J., Dekker H.L., de Jong L., Klis F.M., de Koster C.G.
    J. Biol. Chem. 280:20894-20901(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
  12. "Mass spectrometric quantitation of covalently bound cell wall proteins in Saccharomyces cerevisiae."
    Yin Q.Y., de Groot P.W.J., de Jong L., Klis F.M., de Koster C.G.
    FEMS Yeast Res. 7:887-896(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: LEVEL OF PROTEIN EXPRESSION, IDENTIFICATION BY MASS SPECTROMETRY.
  13. "Profiling phosphoproteins of yeast mitochondria reveals a role of phosphorylation in assembly of the ATP synthase."
    Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B., van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.
    Mol. Cell. Proteomics 6:1896-1906(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-339, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ATCC 76625 / YPH499.
  14. "An engineered Saccharomyces cerevisiae strain binds the broadly neutralizing human immunodeficiency virus type 1 antibody 2G12 and elicits mannose-specific gp120-binding antibodies."
    Luallen R.J., Lin J., Fu H., Cai K.K., Agrawal C., Mboudjeka I., Lee F.-H., Montefiori D., Smith D.F., Doms R.W., Geng Y.
    J. Virol. 82:6447-6457(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, GLYCOSYLATION, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiECM33_YEAST
AccessioniPrimary (citable) accession number: P38248
Secondary accession number(s): D6VQ77, P89498
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: April 29, 2008
Last modified: June 8, 2016
This is version 138 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 6500 wall-bound molecules/cell in log phase YPD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome II
    Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.