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P70699

- LYAG_MOUSE

UniProt

P70699 - LYAG_MOUSE

Protein

Lysosomal alpha-glucosidase

Gene

Gaa

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 2 (16 Aug 2004)
      Previous versions | rss
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    Functioni

    Essential for the degradation of glygogen to glucose in lysosomes.

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei518 – 5181NucleophilePROSITE-ProRule annotation
    Active sitei521 – 5211By similarity

    GO - Molecular functioni

    1. alpha-1,4-glucosidase activity Source: MGI
    2. carbohydrate binding Source: InterPro
    3. maltose alpha-glucosidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. cardiac muscle contraction Source: Ensembl
    2. diaphragm contraction Source: MGI
    3. glycogen catabolic process Source: MGI
    4. glycogen metabolic process Source: MGI
    5. heart morphogenesis Source: MGI
    6. locomotory behavior Source: MGI
    7. lysosome organization Source: MGI
    8. muscle cell cellular homeostasis Source: MGI
    9. neuromuscular process controlling balance Source: MGI
    10. neuromuscular process controlling posture Source: MGI
    11. regulation of the force of heart contraction Source: MGI
    12. striated muscle contraction Source: MGI
    13. tissue development Source: MGI
    14. tongue morphogenesis Source: Ensembl
    15. vacuolar sequestering Source: Ensembl
    16. ventricular cardiac muscle tissue morphogenesis Source: Ensembl

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Protein family/group databases

    CAZyiGH31. Glycoside Hydrolase Family 31.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lysosomal alpha-glucosidase (EC:3.2.1.20)
    Alternative name(s):
    Acid maltase
    Gene namesi
    Name:Gaa
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:95609. Gaa.

    Subcellular locationi

    GO - Cellular componenti

    1. lysosomal membrane Source: UniProtKB-SubCell
    2. lysosome Source: MGI

    Keywords - Cellular componenti

    Lysosome, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2727Sequence AnalysisAdd
    BLAST
    Propeptidei28 – 6942By similarityPRO_0000018569Add
    BLAST
    Chaini70 – 953884Lysosomal alpha-glucosidasePRO_0000018570Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi82 ↔ 109PROSITE-ProRule annotation
    Disulfide bondi92 ↔ 108PROSITE-ProRule annotation
    Disulfide bondi103 ↔ 127PROSITE-ProRule annotation
    Glycosylationi140 – 1401N-linked (GlcNAc...)1 Publication
    Glycosylationi233 – 2331N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi390 – 3901N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi470 – 4701N-linked (GlcNAc...)1 Publication
    Glycosylationi883 – 8831N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi926 – 9261N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi933 – 9331N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiP70699.
    PaxDbiP70699.
    PRIDEiP70699.

    PTM databases

    PhosphoSiteiP70699.

    Expressioni

    Gene expression databases

    ArrayExpressiP70699.
    BgeeiP70699.
    CleanExiMM_GAA.
    GenevestigatoriP70699.

    Interactioni

    Protein-protein interaction databases

    IntActiP70699. 1 interaction.
    MINTiMINT-4100796.

    Structurei

    3D structure databases

    ProteinModelPortaliP70699.
    SMRiP70699. Positions 89-953.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini80 – 13152P-typePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 31 family.Curated
    Contains 1 P-type (trefoil) domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG1501.
    GeneTreeiENSGT00740000115444.
    HOGENOMiHOG000041175.
    HOVERGENiHBG006297.
    InParanoidiP70699.
    KOiK12316.
    OMAiSSEMGYT.
    OrthoDBiEOG77HDD0.
    PhylomeDBiP70699.
    TreeFamiTF314577.

    Family and domain databases

    Gene3Di4.10.110.10. 1 hit.
    InterProiIPR011013. Gal_mutarotase_SF_dom.
    IPR000322. Glyco_hydro_31.
    IPR025887. Glyco_hydro_31_N_dom.
    IPR017853. Glycoside_hydrolase_SF.
    IPR000519. P_trefoil.
    IPR017957. P_trefoil_CS.
    [Graphical view]
    PfamiPF13802. Gal_mutarotas_2. 1 hit.
    PF01055. Glyco_hydro_31. 1 hit.
    PF00088. Trefoil. 1 hit.
    [Graphical view]
    SMARTiSM00018. PD. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 2 hits.
    SSF74650. SSF74650. 1 hit.
    PROSITEiPS00129. GLYCOSYL_HYDROL_F31_1. 1 hit.
    PS00707. GLYCOSYL_HYDROL_F31_2. 1 hit.
    PS00025. P_TREFOIL_1. 1 hit.
    PS51448. P_TREFOIL_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P70699-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNIRKPLCSN SVVGACTLIS LTTAVILGHL MLRELMLLPQ DLHESSSGLW    50
    KTYRPHHQEG YKPGPLHIQE QTEQPKEAPT QCDVPPSSRF DCAPDKGISQ 100
    EQCEARGCCY VPAGQVLKEP QIGQPWCFFP PSYPSYRLEN LSSTESGYTA 150
    TLTRTSPTFF PKDVLTLQLE VLMETDSRLH FKIKDPASKR YEVPLETPRV 200
    LSQAPSPLYS VEFSEEPFGV IVRRKLGGRV LLNTTVAPLF FADQFLQLST 250
    SLPSQHITGL GEHLSPLMLS TDWARITLWN RDTPPSQGTN LYGSHPFYLA 300
    LEDGGLAHGV FLLNSNAMDV ILQPSPALTW RSTGGILDVY VFLGPEPKSV 350
    VQQYLDVVGY PFMPPYWGLG FHLCRWGYSS TAIVRQVVEN MTRTHFPLDV 400
    QWNDLDYMDA RRDFTFNQDS FADFPDMVRE LHQDGRRYMM IVDPAISSAG 450
    PAGSYRPYDE GLRRGVFITN ETGQPLIGKV WPGTTAFPDF TNPETLDWWQ 500
    DMVSEFHAQV PFDGMWLDMN EPSNFVRGSQ QGCPNNELEN PPYVPGVVGG 550
    ILQAATICAS SHQFLSTHYN LHNLYGLTEA IASSRALVKT RGTRPFVISR 600
    STFSGHGRYA GHWTGDVRSS WEHLAYSVPD ILQFNLLGVP LVGADICGFI 650
    GDTSEELCVR WTQLGAFYPF MRNHNDLNSV PQEPYRFSET AQQAMRKAFA 700
    LRYALLPYLY TLFHRAHVRG DTVARPLFLE FPEDPSTWSV DRQLLWGPAL 750
    LITPVLEPGK TEVTGYFPKG TWYNMQMVSV DSLGTLPSPS SASSFRSAVQ 800
    SKGQWLTLEA PLDTINVHLR EGYIIPLQGP SLTTTESRKQ PMALAVALTA 850
    SGEADGELFW DDGESLAVLE RGAYTLVTFS AKNNTIVNKL VRVTKEGAEL 900
    QLREVTVLGV ATAPTQVLSN GIPVSNFTYS PDNKSLAIPV SLLMGELFQI 950
    SWS 953
    Length:953
    Mass (Da):106,248
    Last modified:August 16, 2004 - v2
    Checksum:i956B89685FB5FF81
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti62 – 621K → E in AAB06943. 1 PublicationCurated
    Sequence conflicti254 – 2541S → A in AAB06943. 1 PublicationCurated
    Sequence conflicti430 – 4312EL → DV in AAB06943. 1 PublicationCurated
    Sequence conflicti434 – 4341D → G1 PublicationCurated
    Sequence conflicti434 – 4341D → G(PubMed:15489334)Curated
    Sequence conflicti481 – 4811W → C in AAB06943. 1 PublicationCurated
    Sequence conflicti615 – 6151G → E in AAB06943. 1 PublicationCurated
    Sequence conflicti619 – 6191S → T in AAB06943. 1 PublicationCurated
    Sequence conflicti732 – 7321P → R in AAB06943. 1 PublicationCurated
    Sequence conflicti777 – 7771M → V1 PublicationCurated
    Sequence conflicti777 – 7771M → V(PubMed:15489334)Curated
    Sequence conflicti871 – 8711R → H in AAB06943. 1 PublicationCurated
    Sequence conflicti903 – 9031R → K in AAB06943. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U49351 mRNA. Translation: AAB06943.1.
    AK052211 mRNA. Translation: BAC34888.1.
    AK088481 mRNA. Translation: BAC40382.1.
    AK139333 mRNA. Translation: BAE23960.1.
    AK146538 mRNA. Translation: BAE27243.1.
    AK150970 mRNA. Translation: BAE30001.1.
    BC010210 mRNA. Translation: AAH10210.1.
    CCDSiCCDS25713.1.
    RefSeqiNP_001152796.1. NM_001159324.1.
    NP_032090.3. NM_008064.3.
    UniGeneiMm.4793.

    Genome annotation databases

    EnsembliENSMUST00000026666; ENSMUSP00000026666; ENSMUSG00000025579.
    ENSMUST00000106259; ENSMUSP00000101866; ENSMUSG00000025579.
    GeneIDi14387.
    KEGGimmu:14387.
    UCSCiuc007mqg.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U49351 mRNA. Translation: AAB06943.1 .
    AK052211 mRNA. Translation: BAC34888.1 .
    AK088481 mRNA. Translation: BAC40382.1 .
    AK139333 mRNA. Translation: BAE23960.1 .
    AK146538 mRNA. Translation: BAE27243.1 .
    AK150970 mRNA. Translation: BAE30001.1 .
    BC010210 mRNA. Translation: AAH10210.1 .
    CCDSi CCDS25713.1.
    RefSeqi NP_001152796.1. NM_001159324.1.
    NP_032090.3. NM_008064.3.
    UniGenei Mm.4793.

    3D structure databases

    ProteinModelPortali P70699.
    SMRi P70699. Positions 89-953.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P70699. 1 interaction.
    MINTi MINT-4100796.

    Chemistry

    BindingDBi P70699.
    ChEMBLi CHEMBL1667668.

    Protein family/group databases

    CAZyi GH31. Glycoside Hydrolase Family 31.

    PTM databases

    PhosphoSitei P70699.

    Proteomic databases

    MaxQBi P70699.
    PaxDbi P70699.
    PRIDEi P70699.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000026666 ; ENSMUSP00000026666 ; ENSMUSG00000025579 .
    ENSMUST00000106259 ; ENSMUSP00000101866 ; ENSMUSG00000025579 .
    GeneIDi 14387.
    KEGGi mmu:14387.
    UCSCi uc007mqg.2. mouse.

    Organism-specific databases

    CTDi 2548.
    MGIi MGI:95609. Gaa.

    Phylogenomic databases

    eggNOGi COG1501.
    GeneTreei ENSGT00740000115444.
    HOGENOMi HOG000041175.
    HOVERGENi HBG006297.
    InParanoidi P70699.
    KOi K12316.
    OMAi SSEMGYT.
    OrthoDBi EOG77HDD0.
    PhylomeDBi P70699.
    TreeFami TF314577.

    Miscellaneous databases

    NextBioi 285901.
    PROi P70699.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P70699.
    Bgeei P70699.
    CleanExi MM_GAA.
    Genevestigatori P70699.

    Family and domain databases

    Gene3Di 4.10.110.10. 1 hit.
    InterProi IPR011013. Gal_mutarotase_SF_dom.
    IPR000322. Glyco_hydro_31.
    IPR025887. Glyco_hydro_31_N_dom.
    IPR017853. Glycoside_hydrolase_SF.
    IPR000519. P_trefoil.
    IPR017957. P_trefoil_CS.
    [Graphical view ]
    Pfami PF13802. Gal_mutarotas_2. 1 hit.
    PF01055. Glyco_hydro_31. 1 hit.
    PF00088. Trefoil. 1 hit.
    [Graphical view ]
    SMARTi SM00018. PD. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 2 hits.
    SSF74650. SSF74650. 1 hit.
    PROSITEi PS00129. GLYCOSYL_HYDROL_F31_1. 1 hit.
    PS00707. GLYCOSYL_HYDROL_F31_2. 1 hit.
    PS00025. P_TREFOIL_1. 1 hit.
    PS51448. P_TREFOIL_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of the mouse liver cDNA encoding lysosomal alpha-glucosidase."
      Ding J.H., Yang B.Z., Reuser A.J.J., Roe C.R.
      Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: BALB/c.
      Tissue: Liver.
    2. "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].
      Strain: C57BL/6J and NOD.
      Tissue: Bone marrow, Brain cortex, Heart and Thymus.
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: FVB/N.
      Tissue: Mammary tumor.
    4. Lubec G., Sunyer B., Chen W.-Q.
      Submitted (JAN-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 376-385, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: OF1.
      Tissue: Hippocampus.
    5. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
      Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
      Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-140 AND ASN-470.

    Entry informationi

    Entry nameiLYAG_MOUSE
    AccessioniPrimary (citable) accession number: P70699
    Secondary accession number(s): Q3UJB2, Q8BGI6, Q91Z45
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: August 16, 2004
    Last modified: October 1, 2014
    This is version 123 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, Direct protein sequencing, 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