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P29416

- HEXA_MOUSE

UniProt

P29416 - HEXA_MOUSE

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Protein
Beta-hexosaminidase subunit alpha
Gene
Hexa
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript leveli

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 donor By similarity

GO - Molecular functioni

  1. beta-N-acetylhexosaminidase activity Source: MGI
Complete GO annotation...

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
Complete GO annotation...

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
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222 By similarity
Add
BLAST
Propeptidei23 – 8866 By similarity
PRO_0000011995Add
BLAST
Chaini89 – 528440Beta-hexosaminidase subunit alpha
PRO_0000011996Add
BLAST

Amino acid modifications

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

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliP29416.
SMRiP29416. Positions 23-527.

Family & Domainsi

Region

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

Sequence similaritiesi

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

« Hide

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti56 – 561A → G in CAA45615. 1 Publication
Sequence conflicti56 – 561A → G in AAC53246. 1 Publication
Sequence conflicti237 – 2371Q → E in X79061. 1 Publication
Sequence conflicti237 – 2371Q → E in X79062. 1 Publication
Sequence conflicti455 – 4551E → Q in X79061. 1 Publication
Sequence conflicti455 – 4551E → Q in X79062. 1 Publication

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...

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 115 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

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