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P29416

- HEXA_MOUSE

UniProt

P29416 - HEXA_MOUSE

Protein

Beta-hexosaminidase subunit alpha

Gene

Hexa

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Responsible for the degradation of GM2 gangliosides, and a variety of other molecules containing terminal N-acetyl hexosamines, in the brain and other tissues.

    Catalytic activityi

    Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei323 – 3231Proton donorBy similarity

    GO - Molecular functioni

    1. beta-N-acetylhexosaminidase activity Source: MGI

    GO - Biological processi

    1. adult walking behavior Source: MGI
    2. carbohydrate metabolic process Source: InterPro
    3. cell morphogenesis involved in neuron differentiation Source: MGI
    4. ganglioside catabolic process Source: MGI
    5. glycosaminoglycan metabolic process Source: MGI
    6. lipid storage Source: MGI
    7. locomotory behavior Source: MGI
    8. lysosome organization Source: MGI
    9. myelination Source: MGI
    10. neuromuscular process controlling balance Source: MGI
    11. neuromuscular process controlling posture Source: MGI
    12. sensory perception of sound Source: MGI
    13. sexual reproduction Source: MGI
    14. skeletal system development Source: MGI

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Enzyme and pathway databases

    ReactomeiREACT_196554. Hyaluronan uptake and degradation.
    REACT_198960. Keratan sulfate degradation.
    REACT_198981. CS/DS degradation.
    REACT_199008. Glycosphingolipid metabolism.

    Protein family/group databases

    CAZyiGH20. Glycoside Hydrolase Family 20.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-hexosaminidase subunit alpha (EC:3.2.1.52)
    Alternative name(s):
    Beta-N-acetylhexosaminidase subunit alpha
    Short name:
    Hexosaminidase subunit A
    N-acetyl-beta-glucosaminidase subunit alpha
    Gene namesi
    Name:Hexa
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 9

    Organism-specific databases

    MGIiMGI:96073. Hexa.

    Subcellular locationi

    GO - Cellular componenti

    1. lysosome Source: MGI
    2. membrane Source: MGI

    Keywords - Cellular componenti

    Lysosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222By similarityAdd
    BLAST
    Propeptidei23 – 8866By similarityPRO_0000011995Add
    BLAST
    Chaini89 – 528440Beta-hexosaminidase subunit alphaPRO_0000011996Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi58 ↔ 104By similarity
    Glycosylationi115 – 1151N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi157 – 1571N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi277 ↔ 328By similarity
    Glycosylationi295 – 2951N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi487 – 4871N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi504 ↔ 521By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    MaxQBiP29416.
    PaxDbiP29416.
    PRIDEiP29416.

    PTM databases

    PhosphoSiteiP29416.

    Expressioni

    Tissue specificityi

    Ubiquitous. Most abundant in testis, adrenal, epididymis and heart. Low levels seen in the liver.1 Publication

    Gene expression databases

    ArrayExpressiP29416.
    BgeeiP29416.
    CleanExiMM_HEXA.
    GenevestigatoriP29416.

    Interactioni

    Subunit structurei

    There are 3 forms of beta-hexosaminidase: hexosaminidase A is a trimer composed of one alpha chain, one beta-A chain and one beta-B chain; hexosaminidase B is a tetramer of two beta-A and two beta-B chains; hexosaminidase S is a homodimer of two alpha chains. The two beta chains are derived from the cleavage of a precursor chain By similarity.By similarity

    Protein-protein interaction databases

    BioGridi200280. 1 interaction.
    IntActiP29416. 1 interaction.
    STRINGi10090.ENSMUSP00000026262.

    Structurei

    3D structure databases

    ProteinModelPortaliP29416.
    SMRiP29416. Positions 23-527.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni422 – 4232Critical for hydrolyzis GM2 gangliosidesBy similarity

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 20 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG3525.
    GeneTreeiENSGT00390000008107.
    HOGENOMiHOG000157972.
    HOVERGENiHBG005961.
    InParanoidiQ91XG3.
    KOiK12373.
    OMAiWHLVDDS.
    OrthoDBiEOG7KDFB6.
    TreeFamiTF313036.

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    3.30.379.10. 1 hit.
    InterProiIPR025705. Beta_hexosaminidase_sua/sub.
    IPR029018. Chitobiase/Hex_dom_2-like.
    IPR015883. Glyco_hydro_20_cat-core.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    IPR029019. HEX_eukaryotic_N.
    [Graphical view]
    PfamiPF00728. Glyco_hydro_20. 1 hit.
    PF14845. Glycohydro_20b2. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001093. B-hxosamndse_ab_euk_. 1 hit.
    PRINTSiPR00738. GLHYDRLASE20.
    SUPFAMiSSF51445. SSF51445. 1 hit.
    SSF55545. SSF55545. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    P29416-1 [UniParc]FASTAAdd to Basket

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    MAGCRLWVSL LLAAALACLA TALWPWPQYI QTYHRRYTLY PNNFQFRYHV    50
    SSAAQAGCVV LDEAFRRYRN LLFGSGSWPR PSFSNKQQTL GKNILVVSVV 100
    TAECNEFPNL ESVENYTLTI NDDQCLLASE TVWGALRGLE TFSQLVWKSA 150
    EGTFFINKTK IKDFPRFPHR GVLLDTSRHY LPLSSILDTL DVMAYNKFNV 200
    FHWHLVDDSS FPYESFTFPE LTRKGSFNPV THIYTAQDVK EVIEYARLRG 250
    IRVLAEFDTP GHTLSWGPGA PGLLTPCYSG SHLSGTFGPV NPSLNSTYDF 300
    MSTLFLEISS VFPDFYLHLG GDEVDFTCWK SNPNIQAFMK KKGFTDFKQL 350
    ESFYIQTLLD IVSDYDKGYV VWQEVFDNKV KVRPDTIIQV WREEMPVEYM 400
    LEMQDITRAG FRALLSAPWY LNRVKYGPDW KDMYKVEPLA FHGTPEQKAL 450
    VIGGEACMWG EYVDSTNLVP RLWPRAGAVA ERLWSSNLTT NIDFAFKRLS 500
    HFRCELVRRG IQAQPISVGY CEQEFEQT 528
    Length:528
    Mass (Da):60,613
    Last modified:July 27, 2011 - v2
    Checksum:i95DEA72D767094EF
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti56 – 561A → G in CAA45615. (PubMed:1379046)Curated
    Sequence conflicti56 – 561A → G in AAC53246. (PubMed:7833835)Curated
    Sequence conflicti237 – 2371Q → E in X79061. (PubMed:7896264)Curated
    Sequence conflicti237 – 2371Q → E in X79062. (PubMed:7896264)Curated
    Sequence conflicti455 – 4551E → Q in X79061. (PubMed:7896264)Curated
    Sequence conflicti455 – 4551E → Q in X79062. (PubMed:7896264)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X64331 mRNA. Translation: CAA45615.1.
    U05837
    , U05824, U05825, U05826, U05827, U05828, U05829, U05830, U05831, U05832, U05833, U05834, U05835, U05836 Genomic DNA. Translation: AAC53246.1.
    U07721
    , U07709, U07710, U07711, U07712, U07713, U07714, U07715, U07716, U07717, U07718, U07719, U07720 Unassigned DNA. Translation: AAA18777.1.
    U07631 mRNA. Translation: AAA18775.1.
    X79061 Genomic DNA. No translation available.
    X79062 Genomic DNA. No translation available.
    AK075895 mRNA. Translation: BAC36036.1.
    AK075911 mRNA. Translation: BAC36049.1.
    AK144168 mRNA. Translation: BAE25744.1.
    AK159814 mRNA. Translation: BAE35394.1.
    CH466522 Genomic DNA. Translation: EDL25971.1.
    BC010755 mRNA. Translation: AAH10755.1.
    CCDSiCCDS23250.1.
    PIRiI48253.
    RefSeqiNP_034551.2. NM_010421.4.
    UniGeneiMm.2284.

    Genome annotation databases

    EnsembliENSMUST00000026262; ENSMUSP00000026262; ENSMUSG00000025232.
    GeneIDi15211.
    KEGGimmu:15211.
    UCSCiuc009pxw.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X64331 mRNA. Translation: CAA45615.1 .
    U05837
    , U05824 , U05825 , U05826 , U05827 , U05828 , U05829 , U05830 , U05831 , U05832 , U05833 , U05834 , U05835 , U05836 Genomic DNA. Translation: AAC53246.1 .
    U07721
    , U07709 , U07710 , U07711 , U07712 , U07713 , U07714 , U07715 , U07716 , U07717 , U07718 , U07719 , U07720 Unassigned DNA. Translation: AAA18777.1 .
    U07631 mRNA. Translation: AAA18775.1 .
    X79061 Genomic DNA. No translation available.
    X79062 Genomic DNA. No translation available.
    AK075895 mRNA. Translation: BAC36036.1 .
    AK075911 mRNA. Translation: BAC36049.1 .
    AK144168 mRNA. Translation: BAE25744.1 .
    AK159814 mRNA. Translation: BAE35394.1 .
    CH466522 Genomic DNA. Translation: EDL25971.1 .
    BC010755 mRNA. Translation: AAH10755.1 .
    CCDSi CCDS23250.1.
    PIRi I48253.
    RefSeqi NP_034551.2. NM_010421.4.
    UniGenei Mm.2284.

    3D structure databases

    ProteinModelPortali P29416.
    SMRi P29416. Positions 23-527.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 200280. 1 interaction.
    IntActi P29416. 1 interaction.
    STRINGi 10090.ENSMUSP00000026262.

    Protein family/group databases

    CAZyi GH20. Glycoside Hydrolase Family 20.

    PTM databases

    PhosphoSitei P29416.

    Proteomic databases

    MaxQBi P29416.
    PaxDbi P29416.
    PRIDEi P29416.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000026262 ; ENSMUSP00000026262 ; ENSMUSG00000025232 .
    GeneIDi 15211.
    KEGGi mmu:15211.
    UCSCi uc009pxw.1. mouse.

    Organism-specific databases

    CTDi 3073.
    MGIi MGI:96073. Hexa.

    Phylogenomic databases

    eggNOGi COG3525.
    GeneTreei ENSGT00390000008107.
    HOGENOMi HOG000157972.
    HOVERGENi HBG005961.
    InParanoidi Q91XG3.
    KOi K12373.
    OMAi WHLVDDS.
    OrthoDBi EOG7KDFB6.
    TreeFami TF313036.

    Enzyme and pathway databases

    Reactomei REACT_196554. Hyaluronan uptake and degradation.
    REACT_198960. Keratan sulfate degradation.
    REACT_198981. CS/DS degradation.
    REACT_199008. Glycosphingolipid metabolism.

    Miscellaneous databases

    NextBioi 287777.
    PROi P29416.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P29416.
    Bgeei P29416.
    CleanExi MM_HEXA.
    Genevestigatori P29416.

    Family and domain databases

    Gene3Di 3.20.20.80. 1 hit.
    3.30.379.10. 1 hit.
    InterProi IPR025705. Beta_hexosaminidase_sua/sub.
    IPR029018. Chitobiase/Hex_dom_2-like.
    IPR015883. Glyco_hydro_20_cat-core.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    IPR029019. HEX_eukaryotic_N.
    [Graphical view ]
    Pfami PF00728. Glyco_hydro_20. 1 hit.
    PF14845. Glycohydro_20b2. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001093. B-hxosamndse_ab_euk_. 1 hit.
    PRINTSi PR00738. GLHYDRLASE20.
    SUPFAMi SSF51445. SSF51445. 1 hit.
    SSF55545. SSF55545. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and sequence analysis of a cDNA encoding the alpha-subunit of mouse beta-N-acetylhexosaminidase and comparison with the human enzyme."
      Beccari T., Hoade J., Orlacchio A., Stirling J.L.
      Biochem. J. 285:593-596(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Testis.
    2. "Organization of the gene for the alpha-subunit of mouse beta-N-acetylhexosaminidase (HEXa)."
      Bianconi S., Beccari T., Stirling J.L., Sheardown S., Orlacchio A.
      Biochem. Mol. Biol. Int. 34:579-586(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Structure and expression of the mouse beta-hexosaminidase genes, Hexa and Hexb."
      Yamanaka S., Johnson O.N., Norflus F., Boles D.J., Proia R.L.
      Genomics 21:588-596(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: C57BL/6 X CBA.
      Tissue: Liver.
    4. "Structural organization, sequence, and expression of the mouse HEXA gene encoding the alpha subunit of hexosaminidase A."
      Wakamatsu N., Benoit G., Lamhonwah A.-M., Zhang Z.-X., Trasler J.M., Triggs-Raine B.L., Gravel R.A.
      Genomics 24:110-119(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
      Strain: 129/Sv.
      Tissue: Liver.
    5. "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: BALB/c and C57BL/6J.
      Tissue: Tongue.
    6. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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: Colon.

    Entry informationi

    Entry nameiHEXA_MOUSE
    AccessioniPrimary (citable) accession number: P29416
    Secondary accession number(s): Q64246, Q91XG3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 116 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