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Q8BVW0

- GANC_MOUSE

UniProt

Q8BVW0 - GANC_MOUSE

Protein

Neutral alpha-glucosidase C

Gene

Ganc

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 90 (01 Oct 2014)
      Sequence version 2 (07 Jun 2004)
      Previous versions | rss
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    Functioni

    Has alpha-glucosidase activity.By similarity

    Catalytic activityi

    Hydrolysis of terminal, non-reducing 1,4-linked D-glucose residues with release of D-glucose.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei495 – 4951NucleophilePROSITE-ProRule annotation
    Active sitei498 – 4981By similarity
    Active sitei571 – 5711Proton donorBy similarity

    GO - Molecular functioni

    1. alpha-1,4-glucosidase activity Source: MGI
    2. carbohydrate binding Source: InterPro

    GO - Biological processi

    1. glucose metabolic process Source: MGI

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Protein family/group databases

    CAZyiGH31. Glycoside Hydrolase Family 31.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Neutral alpha-glucosidase C (EC:3.2.1.-)
    Gene namesi
    Name:Ganc
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:1923301. Ganc.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 898898Neutral alpha-glucosidase CPRO_0000185366Add
    BLAST

    Proteomic databases

    MaxQBiQ8BVW0.
    PaxDbiQ8BVW0.
    PRIDEiQ8BVW0.

    PTM databases

    PhosphoSiteiQ8BVW0.

    Expressioni

    Gene expression databases

    CleanExiMM_GANC.
    GenevestigatoriQ8BVW0.

    Interactioni

    Protein-protein interaction databases

    IntActiQ8BVW0. 1 interaction.
    MINTiMINT-4095605.
    STRINGi10090.ENSMUSP00000116898.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8BVW0.
    SMRiQ8BVW0. Positions 208-896.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 31 family.Curated

    Phylogenomic databases

    eggNOGiCOG1501.
    HOVERGENiHBG051683.
    InParanoidiQ8BVW0.
    KOiK12317.

    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. 2 hits.
    PROSITEiPS00129. GLYCOSYL_HYDROL_F31_1. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8BVW0-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MEAAEKEEIS VEDEAVDKTI FKDCGKIAFY RRQKQQLTKT TTYQALLGSV    50
    DTEQDSTRFQ IISEATKIPL VAEVYGIEKD IFRLKINEET PLKPRLVCSG 100
    DTGSLILTNR KGDLKCHVSA NPFKIDLLSK NEAVISINSL GQLYFEHLQV 150
    PHKQRATKGN GQNTPAATSQ ENQEDLGLWE EKFGKFVDVK ANGPSSVGLD 200
    FSLHGFEHLY GIPQHAESHQ LKNTRDGDAY RLYNLDVYGY QVHDKMGIYG 250
    SVPYLLAHKQ GRTVGIFWLN ASETLVEINT EPAVEYTLTQ MGPAAAKPKV 300
    RCRTDVHWMS ESGIIDVFLL TGPTPADVFK QYSYITGTQA MPPLFSLGYH 350
    QCRWNYEDEQ DVKAVDAGFD EHDIPYDVMW LDIEHTEDKK YFTWDKKRFA 400
    NPKRMQELLR SKKRKLVVIS DPHIKVDPDY TVYAQAKEQG FFVKNPEGGD 450
    FEGVCWPGLS SYLDFTNPKV REWYSSLFAF PVYQGSTDIL FLWNDMNEPS 500
    VFRGPELTMH KSAVHYGDWE HRELHNIYGF YQQMATAEGL IQRSKGKERP 550
    FVLSRSFFAG SQKYGAVWTG DNKAEWSYLK ISIPMLLTLS VSGISFCGAD 600
    VGGFIGNPEA ELLVRWYQAG AYQPFFRGHA TMNTKRREPW LFGEEYTQLI 650
    REAIRQRYAL LPYLYSLFYH THVSSQPVMR PLWVEYPDDL ETFAVEDEYM 700
    LGSALLVHPV TDPQTATIDV FLPGSDEVWY DSKTFAYWKG GCTVKIPVTL 750
    DTIPVFQRGG SVVPVKTTVG TSTGWMADSP YELRVALSTQ GSAVGELYLD 800
    DGHSFQYLHQ NQFLYRKFLF CSSVLTNRCA NEKGHYPSKC IVEQILVLGL 850
    KKKPSSVTTH LSDGRAQPAA FTYCAETSAL RLEKLSLRIG EDWEVRVG 898
    Length:898
    Mass (Da):102,008
    Last modified:June 7, 2004 - v2
    Checksum:i6AE5A1EBADBA52C0
    GO
    Isoform 2 (identifier: Q8BVW0-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         95-95: R → RYEVPDVINSKLGTVR
         154-199: QRATKGNGQN...KANGPSSVGL → LYTLLALKIY...SFLPFPPTRL
         200-898: Missing.

    Note: No experimental confirmation available. May be due to an intron retention.

    Show »
    Length:214
    Mass (Da):24,335
    Checksum:i369B89CE2AFD9565
    GO

    Sequence cautioni

    The sequence BAC36303.1 differs from that shown. Reason: Erroneous initiation.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei95 – 951R → RYEVPDVINSKLGTVR in isoform 2. 1 PublicationVSP_010619
    Alternative sequencei154 – 19946QRATK…SSVGL → LYTLLALKIYLNGACLEYQL PWTRVFTLAQQMPYCLSFLP FPPTRL in isoform 2. 1 PublicationVSP_010620Add
    BLAST
    Alternative sequencei200 – 898699Missing in isoform 2. 1 PublicationVSP_010621Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK034155 mRNA. Translation: BAC28611.1.
    AK036238 mRNA. Translation: BAC29357.1.
    AK076333 mRNA. Translation: BAC36303.1. Different initiation.
    RefSeqiNP_766260.2. NM_172672.2.
    UniGeneiMm.38851.

    Genome annotation databases

    GeneIDi76051.
    KEGGimmu:76051.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK034155 mRNA. Translation: BAC28611.1 .
    AK036238 mRNA. Translation: BAC29357.1 .
    AK076333 mRNA. Translation: BAC36303.1 . Different initiation.
    RefSeqi NP_766260.2. NM_172672.2.
    UniGenei Mm.38851.

    3D structure databases

    ProteinModelPortali Q8BVW0.
    SMRi Q8BVW0. Positions 208-896.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q8BVW0. 1 interaction.
    MINTi MINT-4095605.
    STRINGi 10090.ENSMUSP00000116898.

    Chemistry

    BindingDBi Q8BVW0.
    ChEMBLi CHEMBL3635.

    Protein family/group databases

    CAZyi GH31. Glycoside Hydrolase Family 31.

    PTM databases

    PhosphoSitei Q8BVW0.

    Proteomic databases

    MaxQBi Q8BVW0.
    PaxDbi Q8BVW0.
    PRIDEi Q8BVW0.

    Protocols and materials databases

    DNASUi 76051.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 76051.
    KEGGi mmu:76051.

    Organism-specific databases

    CTDi 2595.
    MGIi MGI:1923301. Ganc.

    Phylogenomic databases

    eggNOGi COG1501.
    HOVERGENi HBG051683.
    InParanoidi Q8BVW0.
    KOi K12317.

    Miscellaneous databases

    NextBioi 344511.
    PROi Q8BVW0.
    SOURCEi Search...

    Gene expression databases

    CleanExi MM_GANC.
    Genevestigatori Q8BVW0.

    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. 2 hits.
    PROSITEi PS00129. GLYCOSYL_HYDROL_F31_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Strain: C57BL/6J.
      Tissue: Cerebellum, Diencephalon and Skin.

    Entry informationi

    Entry nameiGANC_MOUSE
    AccessioniPrimary (citable) accession number: Q8BVW0
    Secondary accession number(s): Q8BH03
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2004
    Last sequence update: June 7, 2004
    Last modified: October 1, 2014
    This is version 90 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3