Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Probable family 17 glucosidase SCW4

Gene

SCW4

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

Glucanases possibly play a role in cell expansion during growth, in cell-cell fusion during mating, and in spore release during sporulation.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei323 – 3231NucleophileBy similarity
Active sitei377 – 3771Proton donorBy similarity

GO - Molecular functioni

  • glucosidase activity Source: SGD

GO - Biological processi

  • carbohydrate metabolic process Source: InterPro
  • cell wall organization Source: UniProtKB-KW
  • conjugation with cellular fusion Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Cell wall biogenesis/degradation

Enzyme and pathway databases

BioCyciYEAST:YGR279C-MONOMER.

Protein family/group databases

CAZyiGH17. Glycoside Hydrolase Family 17.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable family 17 glucosidase SCW4 (EC:3.2.1.-)
Alternative name(s):
Soluble cell wall protein 4
Gene namesi
Name:SCW4
Ordered Locus Names:YGR279C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGR279C.
SGDiS000003511. SCW4.

Subcellular locationi

  • Secretedcell wall 1 Publication

GO - Cellular componenti

  • extracellular region Source: SGD
  • fungal-type cell wall Source: SGD
  • vacuole Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cell wall, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence analysisAdd
BLAST
Propeptidei20 – 30111 PublicationPRO_0000011899Add
BLAST
Chaini31 – 386356Probable family 17 glucosidase SCW4PRO_0000011900Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi89 – 891N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Cleavage on pair of basic residues, Glycoprotein

Proteomic databases

MaxQBiP53334.
PeptideAtlasiP53334.

Interactioni

Protein-protein interaction databases

BioGridi33529. 41 interactions.
DIPiDIP-6513N.
IntActiP53334. 5 interactions.
MINTiMINT-685889.

Structurei

3D structure databases

ProteinModelPortaliP53334.
SMRiP53334. Positions 135-386.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi71 – 15585Ser-richAdd
BLAST

Sequence similaritiesi

Belongs to the glycosyl hydrolase 17 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

GeneTreeiENSGT00390000008245.
HOGENOMiHOG000216601.
InParanoidiP53334.
OMAiESGWPHA.
OrthoDBiEOG73FQWG.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR000490. Glyco_hydro_17.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00332. Glyco_hydro_17. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00587. GLYCOSYL_HYDROL_F17. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P53334-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLSNLIASA SLLSAATLAA PANHEHKDKR AVVTTTVQKQ TTIIVNGAAS
60 70 80 90 100
TPVAALEENA VVNSAPAAAT STTSSAASVA TAAASSSENN SQVSAAASPA
110 120 130 140 150
SSSAATSTQS SSSSQASSSS SSGEDVSSFA SGVRGITYTP YESSGACKSA
160 170 180 190 200
SEVASDLAQL TDFPVIRLYG TDCNQVENVF KAKASNQKVF LGIYYVDQIQ
210 220 230 240 250
DGVNTIKSAV ESYGSWDDVT TVSIGNELVN GNQATPSQVG QYIDSGRSAL
260 270 280 290 300
KAAGYTGPVV SVDTFIAVIN NPELCDYSDY MAVNAHAYFD KNTVAQDSGK
310 320 330 340 350
WLLEQIQRVW TACDGKKNVV ITESGWPSKG ETYGVAVPSK ENQKDAVSAI
360 370 380
TSSCGADTFL FTAFNDYWKA DGAYGVEKYW GILSNE
Length:386
Mass (Da):40,173
Last modified:October 1, 1996 - v1
Checksum:i86CE93AEC12E7612
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti35 – 351T → A AA sequence (PubMed:9748433).Curated
Sequence conflicti40 – 401Q → K AA sequence (PubMed:9748433).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z73064 Genomic DNA. Translation: CAA97310.1.
BK006941 Genomic DNA. Translation: DAA08367.1.
PIRiS64614.
RefSeqiNP_011795.1. NM_001181408.1.

Genome annotation databases

EnsemblFungiiYGR279C; YGR279C; YGR279C.
GeneIDi853196.
KEGGisce:YGR279C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z73064 Genomic DNA. Translation: CAA97310.1.
BK006941 Genomic DNA. Translation: DAA08367.1.
PIRiS64614.
RefSeqiNP_011795.1. NM_001181408.1.

3D structure databases

ProteinModelPortaliP53334.
SMRiP53334. Positions 135-386.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33529. 41 interactions.
DIPiDIP-6513N.
IntActiP53334. 5 interactions.
MINTiMINT-685889.

Protein family/group databases

CAZyiGH17. Glycoside Hydrolase Family 17.

Proteomic databases

MaxQBiP53334.
PeptideAtlasiP53334.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGR279C; YGR279C; YGR279C.
GeneIDi853196.
KEGGisce:YGR279C.

Organism-specific databases

EuPathDBiFungiDB:YGR279C.
SGDiS000003511. SCW4.

Phylogenomic databases

GeneTreeiENSGT00390000008245.
HOGENOMiHOG000216601.
InParanoidiP53334.
OMAiESGWPHA.
OrthoDBiEOG73FQWG.

Enzyme and pathway databases

BioCyciYEAST:YGR279C-MONOMER.

Miscellaneous databases

PROiP53334.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR000490. Glyco_hydro_17.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00332. Glyco_hydro_17. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00587. GLYCOSYL_HYDROL_F17. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence analysis of a near-subtelomeric 35.4 kb DNA segment on the right arm of chromosome VII from Saccharomyces cerevisiae carrying the MAL1 locus reveals 15 complete open reading frames, including ZUO1, BGL2 and BIO2 genes and an ABC transporter gene."
    Volckaert G., Voet M., Robben J.
    Yeast 13:251-259(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "New potential cell wall glucanases of Saccharomyces cerevisiae and their involvement in mating."
    Cappellaro C., Mrsa V., Tanner W.
    J. Bacteriol. 180:5030-5037(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 31-40, SUBCELLULAR LOCATION.
    Strain: ATCC 96099 / S288c / SEY6210.
  5. "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.
  6. "Global analysis of the glycoproteome in Saccharomyces cerevisiae reveals new roles for protein glycosylation in eukaryotes."
    Kung L.A., Tao S.-C., Qian J., Smith M.G., Snyder M., Zhu H.
    Mol. Syst. Biol. 5:308-308(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSCW4_YEAST
AccessioniPrimary (citable) accession number: P53334
Secondary accession number(s): D6VV56
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 8, 2016
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 38000 wall-bound molecules/cell in log phase YPD medium.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: 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.