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P38138

- GLU2A_YEAST

UniProt

P38138 - GLU2A_YEAST

Protein

Glucosidase 2 subunit alpha

Gene

ROT2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 1 (01 Oct 1994)
      Previous versions | rss
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    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

    Pathwayi

    Sites

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

    GO - Molecular functioni

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

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro
    2. fungal-type cell wall biogenesis Source: SGD

    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: Chromosome II

    Organism-specific databases

    CYGDiYBR229c.
    SGDiS000000433. ROT2.

    Subcellular locationi

    Endoplasmic reticulum 1 Publication

    GO - Cellular componenti

    1. endoplasmic reticulum Source: SGD
    2. endoplasmic reticulum lumen Source: SGD
    3. glucosidase II complex Source: SGD

    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.

    Expressioni

    Gene expression databases

    GenevestigatoriP38138.

    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. 115 interactions.
    DIPiDIP-5754N.
    IntActiP38138. 3 interactions.
    MINTiMINT-1364745.
    STRINGi4932.YBR229C.

    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.
    GeneTreeiENSGT00740000115152.
    HOGENOMiHOG000115864.
    KOiK05546.
    OMAiAIDDQLY.
    OrthoDBiEOG7G7KXG.

    Family and domain databases

    InterProiIPR011013. Gal_mutarotase_SF_dom.
    IPR000322. Glyco_hydro_31.
    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

    MVLLKWLVCQ LVFFTAFSHA FTDYLLKKCA QSGFCHRNRV YAENIAKSHH    50
    CYYKVDAESI AHDPLENVLH ATIIKTIPRL EGDDIAVQFP FSLSFLQDHS 100
    VRFTINEKER MPTNSSGLLI SSQRFNETWK YAFDKKFQEE ANRTSIPQFH 150
    FLKQKQTVNS FWSKISSFLS LSNSTADTFH LRNGDVSVEI FAEPFQLKVY 200
    WQNALKLIVN EQNFLNIEHH RTKQENFAHV LPEETTFNMF KDNFLYSKHD 250
    SMPLGPESVA LDFSFMGSTN VYGIPEHATS LRLMDTSGGK EPYRLFNVDV 300
    FEYNIGTSQP MYGSIPFMFS SSSTSIFWVN AADTWVDIKY DTSKNKTMTH 350
    WISENGVIDV VMSLGPDIPT IIDKFTDLTG RPFLPPISSI GYHQCRWNYN 400
    DEMDVLTVDS QMDAHMIPYD FIWLDLEYTN DKKYFTWKQH SFPNPKRLLS 450
    KLKKLGRNLV VLIDPHLKKD YEISDRVINE NVAVKDHNGN DYVGHCWPGN 500
    SIWIDTISKY GQKIWKSFFE RFMDLPADLT NLFIWNDMNE PSIFDGPETT 550
    APKDLIHDNY IEERSVHNIY GLSVHEATYD AIKSIYSPSD KRPFLLTRAF 600
    FAGSQRTAAT WTGDNVANWD YLKISIPMVL SNNIAGMPFI GADIAGFAED 650
    PTPELIARWY QAGLWYPFFR AHAHIDTKRR EPYLFNEPLK SIVRDIIQLR 700
    YFLLPTLYTM FHKSSVTGFP IMNPMFIEHP EFAELYHIDN QFYWSNSGLL 750
    VKPVTEPGQS ETEMVFPPGI FYEFASLHSF INNGTDLIEK NISAPLDKIP 800
    LFIEGGHIIT MKDKYRRSSM LMKNDPYVIV IAPDTEGRAV GDLYVDDGET 850
    FGYQRGEYVE TQFIFENNTL KNVRSHIPEN LTGIHHNTLR NTNIEKIIIA 900
    KNNLQHNITL KDSIKVKKNG EESSLPTRSS YENDNKITIL NLSLDITEDW 950
    EVIF 954
    Length:954
    Mass (Da):110,266
    Last modified:October 1, 1994 - v1
    Checksum:i92E93572F04FB009
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z36098 Genomic DNA. Translation: CAA85192.1 .
    BK006936 Genomic DNA. Translation: DAA07344.1 .
    PIRi S46105.
    RefSeqi NP_009788.3. NM_001178577.3.

    3D structure databases

    ProteinModelPortali P38138.
    SMRi P38138. Positions 290-897.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32924. 115 interactions.
    DIPi DIP-5754N.
    IntActi P38138. 3 interactions.
    MINTi MINT-1364745.
    STRINGi 4932.YBR229C.

    Protein family/group databases

    CAZyi GH31. Glycoside Hydrolase Family 31.

    Proteomic databases

    MaxQBi P38138.
    PaxDbi P38138.
    PeptideAtlasi P38138.
    PRIDEi P38138.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YBR229C ; YBR229C ; YBR229C .
    GeneIDi 852530.
    KEGGi sce:YBR229C.

    Organism-specific databases

    CYGDi YBR229c.
    SGDi S000000433. ROT2.

    Phylogenomic databases

    eggNOGi COG1501.
    GeneTreei ENSGT00740000115152.
    HOGENOMi HOG000115864.
    KOi K05546.
    OMAi AIDDQLY.
    OrthoDBi EOG7G7KXG.

    Enzyme and pathway databases

    UniPathwayi UPA00957 .
    BioCyci YEAST:YBR229C-MONOMER.

    Miscellaneous databases

    NextBioi 971580.

    Gene expression databases

    Genevestigatori P38138.

    Family and domain databases

    InterProi IPR011013. Gal_mutarotase_SF_dom.
    IPR000322. Glyco_hydro_31.
    IPR025887. Glyco_hydro_31_N_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF13802. Gal_mutarotas_2. 1 hit.
    PF01055. Glyco_hydro_31. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    SSF74650. SSF74650. 3 hits.
    PROSITEi PS00129. GLYCOSYL_HYDROL_F31_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 111 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