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P38138 (GLU2A_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glucosidase 2 subunit alpha

EC=3.2.1.84
Alternative name(s):
Alpha-glucosidase II subunit alpha
Glucosidase II subunit alpha
Reversal of TOR2 lethality protein 2
Gene names
Name:ROT2
Synonyms:GLS2
Ordered Locus Names:YBR229C
ORF Names:YBR1526
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length954 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalytic subunit of glucosidase 2, which cleaves sequentially the 2 innermost alpha-1,3-linked glucose residues from the Glc2Man9GlcNAc2 oligosaccharide precursor of immature glycoproteins. Ref.4 Ref.6

Catalytic activity

Hydrolysis of terminal (1->3)-alpha-D-glucosidic links in (1->3)-alpha-D-glucans.

Enzyme regulation

Inhibited by glucose, maltose and nigerose, and by the antibiotic deoxynojirimycin.

Pathway

Glycan metabolism; N-glycan metabolism.

Subunit structure

Heterodimer of a catalytic subunit alpha (ROT2) and a subunit beta (GTB1).

Subcellular location

Endoplasmic reticulum Ref.6.

Miscellaneous

Present with 238 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the glycosyl hydrolase 31 family.

Biophysicochemical properties

pH dependence:

Optimum pH is 5.8-6.8. Ref.3

Binary interactions

With

Entry

#Exp.

IntAct

Notes

GTB1Q049241EBI-21021,EBI-37493

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 954932Glucosidase 2 subunit alpha
PRO_0000185370

Sites

Active site5371Nucleophile By similarity
Active site5401 By similarity
Active site6141Proton donor By similarity

Amino acid modifications

Glycosylation1141N-linked (GlcNAc...) Potential
Glycosylation1261N-linked (GlcNAc...) Potential
Glycosylation1421N-linked (GlcNAc...) Potential
Glycosylation1731N-linked (GlcNAc...) Potential
Glycosylation3451N-linked (GlcNAc...) Potential
Glycosylation7831N-linked (GlcNAc...) Potential
Glycosylation7911N-linked (GlcNAc...) Potential
Glycosylation8671N-linked (GlcNAc...) Potential
Glycosylation8801N-linked (GlcNAc...) Potential
Glycosylation9071N-linked (GlcNAc...) Potential
Glycosylation9411N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
P38138 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: 92E93572F04FB009

FASTA954110,266
        10         20         30         40         50         60 
MVLLKWLVCQ LVFFTAFSHA FTDYLLKKCA QSGFCHRNRV YAENIAKSHH CYYKVDAESI 

        70         80         90        100        110        120 
AHDPLENVLH ATIIKTIPRL EGDDIAVQFP FSLSFLQDHS VRFTINEKER MPTNSSGLLI 

       130        140        150        160        170        180 
SSQRFNETWK YAFDKKFQEE ANRTSIPQFH FLKQKQTVNS FWSKISSFLS LSNSTADTFH 

       190        200        210        220        230        240 
LRNGDVSVEI FAEPFQLKVY WQNALKLIVN EQNFLNIEHH RTKQENFAHV LPEETTFNMF 

       250        260        270        280        290        300 
KDNFLYSKHD SMPLGPESVA LDFSFMGSTN VYGIPEHATS LRLMDTSGGK EPYRLFNVDV 

       310        320        330        340        350        360 
FEYNIGTSQP MYGSIPFMFS SSSTSIFWVN AADTWVDIKY DTSKNKTMTH WISENGVIDV 

       370        380        390        400        410        420 
VMSLGPDIPT IIDKFTDLTG RPFLPPISSI GYHQCRWNYN DEMDVLTVDS QMDAHMIPYD 

       430        440        450        460        470        480 
FIWLDLEYTN DKKYFTWKQH SFPNPKRLLS KLKKLGRNLV VLIDPHLKKD YEISDRVINE 

       490        500        510        520        530        540 
NVAVKDHNGN DYVGHCWPGN SIWIDTISKY GQKIWKSFFE RFMDLPADLT NLFIWNDMNE 

       550        560        570        580        590        600 
PSIFDGPETT APKDLIHDNY IEERSVHNIY GLSVHEATYD AIKSIYSPSD KRPFLLTRAF 

       610        620        630        640        650        660 
FAGSQRTAAT WTGDNVANWD YLKISIPMVL SNNIAGMPFI GADIAGFAED PTPELIARWY 

       670        680        690        700        710        720 
QAGLWYPFFR AHAHIDTKRR EPYLFNEPLK SIVRDIIQLR YFLLPTLYTM FHKSSVTGFP 

       730        740        750        760        770        780 
IMNPMFIEHP EFAELYHIDN QFYWSNSGLL VKPVTEPGQS ETEMVFPPGI FYEFASLHSF 

       790        800        810        820        830        840 
INNGTDLIEK NISAPLDKIP LFIEGGHIIT MKDKYRRSSM LMKNDPYVIV IAPDTEGRAV 

       850        860        870        880        890        900 
GDLYVDDGET FGYQRGEYVE TQFIFENNTL KNVRSHIPEN LTGIHHNTLR NTNIEKIIIA 

       910        920        930        940        950 
KNNLQHNITL KDSIKVKKNG EESSLPTRSS YENDNKITIL NLSLDITEDW EVIF 

« Hide

References

« Hide 'large scale' references
[1]"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. expand/collapse author list , 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.
[2]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"Inhibition of N-linked complex oligosaccharide formation by 1-deoxynojirimycin, an inhibitor of processing glucosidases."
Saunier B., Kilker R.D. Jr., Tkacz J.S., Quaroni A., Herscovics A.
J. Biol. Chem. 257:14155-14161(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
[4]"Endoplasmic reticulum glucosidase II is composed of a catalytic subunit, conserved from yeast to mammals, and a tightly bound noncatalytic HDEL-containing subunit."
Trombetta E.S., Simons J.F., Helenius A.
J. Biol. Chem. 271:27509-27516(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[5]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]"Yeast GTB1 encodes a subunit of glucosidase II required for glycoprotein processing in the endoplasmic reticulum."
Wilkinson B.M., Purswani J., Stirling C.J.
J. Biol. Chem. 281:6325-6333(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH GTB1, SUBCELLULAR LOCATION, GLYCOSYLATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z36098 Genomic DNA. Translation: CAA85192.1.
BK006936 Genomic DNA. Translation: DAA07344.1.
PIRS46105.
RefSeqNP_009788.3. NM_001178577.3.

3D structure databases

ProteinModelPortalP38138.
SMRP38138. Positions 27-954.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32924. 114 interactions.
DIPDIP-5754N.
IntActP38138. 3 interactions.
MINTMINT-1364745.
STRING4932.YBR229C.

Protein family/group databases

CAZyGH31. Glycoside Hydrolase Family 31.

Proteomic databases

PaxDbP38138.
PeptideAtlasP38138.
PRIDEP38138.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYBR229C; YBR229C; YBR229C.
GeneID852530.
KEGGsce:YBR229C.

Organism-specific databases

CYGDYBR229c.
SGDS000000433. ROT2.

Phylogenomic databases

eggNOGCOG1501.
GeneTreeENSGT00740000115152.
HOGENOMHOG000115864.
KOK05546.
OMAAIDDQLY.
OrthoDBEOG7G7KXG.

Enzyme and pathway databases

BioCycYEAST:YBR229C-MONOMER.
UniPathwayUPA00957.

Gene expression databases

GenevestigatorP38138.

Family and domain databases

InterProIPR011013. Gal_mutarotase_SF_dom.
IPR000322. Glyco_hydro_31.
IPR025887. Glyco_hydro_31_N_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF13802. Gal_mutarotas_2. 1 hit.
PF01055. Glyco_hydro_31. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
SSF74650. SSF74650. 3 hits.
PROSITEPS00129. GLYCOSYL_HYDROL_F31_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio971580.

Entry information

Entry nameGLU2A_YEAST
AccessionPrimary (citable) accession number: P38138
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: April 16, 2014
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome II

Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries