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Protein

Glucosidase 2 subunit alpha

Gene

ROT2

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

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.2 Publications

Catalytic activityi

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

Enzyme regulationi

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

pH dependencei

Optimum pH is 5.8-6.8.1 Publication

Pathway:iN-glycan metabolism

This protein is involved in the pathway N-glycan metabolism, which is part of Glycan metabolism.
View all proteins of this organism that are known to be involved in the pathway N-glycan metabolism and in Glycan metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei537 – 5371NucleophilePROSITE-ProRule annotation
Active sitei540 – 5401By similarity
Active sitei614 – 6141Proton donorBy similarity

GO - Molecular functioni

  • carbohydrate binding Source: InterPro
  • glucan 1,3-alpha-glucosidase activity Source: SGD

GO - Biological processi

  • fungal-type cell wall beta-glucan biosynthetic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

BioCyciYEAST:YBR229C-MONOMER.
UniPathwayiUPA00957.

Protein family/group databases

CAZyiGH31. Glycoside Hydrolase Family 31.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:ROT2
Synonyms:GLS2
Ordered Locus Names:YBR229C
ORF Names:YBR1526
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome II

Organism-specific databases

CYGDiYBR229c.
EuPathDBiFungiDB:YBR229C.
SGDiS000000433. ROT2.

Subcellular locationi

GO - Cellular componenti

  • endoplasmic reticulum lumen Source: SGD
  • glucosidase II complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence AnalysisAdd
BLAST
Chaini23 – 954932Glucosidase 2 subunit alphaPRO_0000185370Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi114 – 1141N-linked (GlcNAc...)Sequence Analysis
Glycosylationi126 – 1261N-linked (GlcNAc...)Sequence Analysis
Glycosylationi142 – 1421N-linked (GlcNAc...)Sequence Analysis
Glycosylationi173 – 1731N-linked (GlcNAc...)Sequence Analysis
Glycosylationi345 – 3451N-linked (GlcNAc...)Sequence Analysis
Glycosylationi783 – 7831N-linked (GlcNAc...)Sequence Analysis
Glycosylationi791 – 7911N-linked (GlcNAc...)Sequence Analysis
Glycosylationi867 – 8671N-linked (GlcNAc...)Sequence Analysis
Glycosylationi880 – 8801N-linked (GlcNAc...)Sequence Analysis
Glycosylationi907 – 9071N-linked (GlcNAc...)Sequence Analysis
Glycosylationi941 – 9411N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiP38138.
PaxDbiP38138.
PeptideAtlasiP38138.
PRIDEiP38138.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
GTB1Q049241EBI-21021,EBI-37493

Protein-protein interaction databases

BioGridi32924. 114 interactions.
DIPiDIP-5754N.
IntActiP38138. 3 interactions.
MINTiMINT-1364745.

Structurei

3D structure databases

ProteinModelPortaliP38138.
SMRiP38138. Positions 290-897.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 31 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG1501.
GeneTreeiENSGT00760000119229.
HOGENOMiHOG000115864.
InParanoidiP38138.
KOiK05546.
OMAiSHKLEVS.
OrthoDBiEOG7G7KXG.

Family and domain databases

InterProiIPR011013. Gal_mutarotase_SF_dom.
IPR000322. Glyco_hydro_31.
IPR030458. Glyco_hydro_31_AS.
IPR025887. Glyco_hydro_31_N_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF13802. Gal_mutarotas_2. 1 hit.
PF01055. Glyco_hydro_31. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF74650. SSF74650. 3 hits.
PROSITEiPS00129. GLYCOSYL_HYDROL_F31_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P38138-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVLLKWLVCQ LVFFTAFSHA FTDYLLKKCA QSGFCHRNRV YAENIAKSHH
60 70 80 90 100
CYYKVDAESI AHDPLENVLH ATIIKTIPRL EGDDIAVQFP FSLSFLQDHS
110 120 130 140 150
VRFTINEKER MPTNSSGLLI SSQRFNETWK YAFDKKFQEE ANRTSIPQFH
160 170 180 190 200
FLKQKQTVNS FWSKISSFLS LSNSTADTFH LRNGDVSVEI FAEPFQLKVY
210 220 230 240 250
WQNALKLIVN EQNFLNIEHH RTKQENFAHV LPEETTFNMF KDNFLYSKHD
260 270 280 290 300
SMPLGPESVA LDFSFMGSTN VYGIPEHATS LRLMDTSGGK EPYRLFNVDV
310 320 330 340 350
FEYNIGTSQP MYGSIPFMFS SSSTSIFWVN AADTWVDIKY DTSKNKTMTH
360 370 380 390 400
WISENGVIDV VMSLGPDIPT IIDKFTDLTG RPFLPPISSI GYHQCRWNYN
410 420 430 440 450
DEMDVLTVDS QMDAHMIPYD FIWLDLEYTN DKKYFTWKQH SFPNPKRLLS
460 470 480 490 500
KLKKLGRNLV VLIDPHLKKD YEISDRVINE NVAVKDHNGN DYVGHCWPGN
510 520 530 540 550
SIWIDTISKY GQKIWKSFFE RFMDLPADLT NLFIWNDMNE PSIFDGPETT
560 570 580 590 600
APKDLIHDNY IEERSVHNIY GLSVHEATYD AIKSIYSPSD KRPFLLTRAF
610 620 630 640 650
FAGSQRTAAT WTGDNVANWD YLKISIPMVL SNNIAGMPFI GADIAGFAED
660 670 680 690 700
PTPELIARWY QAGLWYPFFR AHAHIDTKRR EPYLFNEPLK SIVRDIIQLR
710 720 730 740 750
YFLLPTLYTM FHKSSVTGFP IMNPMFIEHP EFAELYHIDN QFYWSNSGLL
760 770 780 790 800
VKPVTEPGQS ETEMVFPPGI FYEFASLHSF INNGTDLIEK NISAPLDKIP
810 820 830 840 850
LFIEGGHIIT MKDKYRRSSM LMKNDPYVIV IAPDTEGRAV GDLYVDDGET
860 870 880 890 900
FGYQRGEYVE TQFIFENNTL KNVRSHIPEN LTGIHHNTLR NTNIEKIIIA
910 920 930 940 950
KNNLQHNITL KDSIKVKKNG EESSLPTRSS YENDNKITIL NLSLDITEDW

EVIF
Length:954
Mass (Da):110,266
Last modified:October 1, 1994 - v1
Checksum:i92E93572F04FB009
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z36098 Genomic DNA. Translation: CAA85192.1.
BK006936 Genomic DNA. Translation: DAA07344.1.
PIRiS46105.
RefSeqiNP_009788.3. NM_001178577.3.

Genome annotation databases

EnsemblFungiiYBR229C; YBR229C; YBR229C.
GeneIDi852530.
KEGGisce:YBR229C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z36098 Genomic DNA. Translation: CAA85192.1.
BK006936 Genomic DNA. Translation: DAA07344.1.
PIRiS46105.
RefSeqiNP_009788.3. NM_001178577.3.

3D structure databases

ProteinModelPortaliP38138.
SMRiP38138. Positions 290-897.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32924. 114 interactions.
DIPiDIP-5754N.
IntActiP38138. 3 interactions.
MINTiMINT-1364745.

Protein family/group databases

CAZyiGH31. Glycoside Hydrolase Family 31.

Proteomic databases

MaxQBiP38138.
PaxDbiP38138.
PeptideAtlasiP38138.
PRIDEiP38138.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYBR229C; YBR229C; YBR229C.
GeneIDi852530.
KEGGisce:YBR229C.

Organism-specific databases

CYGDiYBR229c.
EuPathDBiFungiDB:YBR229C.
SGDiS000000433. ROT2.

Phylogenomic databases

eggNOGiCOG1501.
GeneTreeiENSGT00760000119229.
HOGENOMiHOG000115864.
InParanoidiP38138.
KOiK05546.
OMAiSHKLEVS.
OrthoDBiEOG7G7KXG.

Enzyme and pathway databases

UniPathwayiUPA00957.
BioCyciYEAST:YBR229C-MONOMER.

Miscellaneous databases

NextBioi971580.
PROiP38138.

Family and domain databases

InterProiIPR011013. Gal_mutarotase_SF_dom.
IPR000322. Glyco_hydro_31.
IPR030458. Glyco_hydro_31_AS.
IPR025887. Glyco_hydro_31_N_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF13802. Gal_mutarotas_2. 1 hit.
PF01055. Glyco_hydro_31. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF74650. SSF74650. 3 hits.
PROSITEiPS00129. GLYCOSYL_HYDROL_F31_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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.

Entry informationi

Entry nameiGLU2A_YEAST
AccessioniPrimary (citable) accession number: P38138
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: July 22, 2015
This is version 119 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 238 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

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 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.