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P29416 (HEXA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Hexa
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length528 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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 activity

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

Subunit structure

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.

Subcellular location

Lysosome.

Tissue specificity

Ubiquitous. Most abundant in testis, adrenal, epididymis and heart. Low levels seen in the liver. Ref.4

Sequence similarities

Belongs to the glycosyl hydrolase 20 family.

Ontologies

Keywords
   Cellular componentLysosome
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Glycoprotein
Zymogen
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processadult walking behavior

Inferred from mutant phenotype PubMed 14972652. Source: MGI

carbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

cell morphogenesis involved in neuron differentiation

Inferred from mutant phenotype PubMed 14972652. Source: MGI

ganglioside catabolic process

Inferred from mutant phenotype PubMed 7937929PubMed 8789434PubMed 9223328PubMed 9645704. Source: MGI

glycosaminoglycan metabolic process

Inferred from genetic interaction PubMed 8896570. Source: MGI

lipid storage

Inferred from mutant phenotype PubMed 10021458PubMed 14972652PubMed 9223328. Source: MGI

locomotory behavior

Inferred from genetic interaction PubMed 8896570. Source: MGI

lysosome organization

Inferred from mutant phenotype PubMed 10591619PubMed 14972652PubMed 7937929PubMed 8747922PubMed 9103204PubMed 9302266PubMed 9645704. Source: MGI

myelination

Inferred from genetic interaction PubMed 9184660. Source: MGI

neuromuscular process controlling balance

Inferred from genetic interaction PubMed 8896570. Source: MGI

neuromuscular process controlling posture

Inferred from mutant phenotype PubMed 14972652. Source: MGI

sensory perception of sound

Inferred from genetic interaction PubMed 8896570. Source: MGI

sexual reproduction

Inferred from mutant phenotype PubMed 9645704. Source: MGI

skeletal system development

Inferred from genetic interaction PubMed 8896570PubMed 9184660. Source: MGI

   Cellular_componentlysosome

Inferred from direct assay PubMed 11854359PubMed 9645704. Source: MGI

membrane

Inferred from direct assay PubMed 11854359. Source: MGI

   Molecular_functionbeta-N-acetylhexosaminidase activity

Inferred from direct assay PubMed 11854359PubMed 1914521PubMed 8747922PubMed 9417048. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 By similarity
Propeptide23 – 8866 By similarity
PRO_0000011995
Chain89 – 528440Beta-hexosaminidase subunit alpha
PRO_0000011996

Regions

Region422 – 4232Critical for hydrolyzis GM2 gangliosides By similarity

Sites

Active site3231Proton donor By similarity

Amino acid modifications

Glycosylation1151N-linked (GlcNAc...) Potential
Glycosylation1571N-linked (GlcNAc...) Potential
Glycosylation2951N-linked (GlcNAc...) Potential
Glycosylation4871N-linked (GlcNAc...) Potential
Disulfide bond58 ↔ 104 By similarity
Disulfide bond277 ↔ 328 By similarity
Disulfide bond504 ↔ 521 By similarity

Experimental info

Sequence conflict561A → G in CAA45615. Ref.1
Sequence conflict561A → G in AAC53246. Ref.2
Sequence conflict2371Q → E in X79061. Ref.4
Sequence conflict2371Q → E in X79062. Ref.4
Sequence conflict4551E → Q in X79061. Ref.4
Sequence conflict4551E → Q in X79062. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P29416 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 95DEA72D767094EF

FASTA52860,613
        10         20         30         40         50         60 
MAGCRLWVSL LLAAALACLA TALWPWPQYI QTYHRRYTLY PNNFQFRYHV SSAAQAGCVV 

        70         80         90        100        110        120 
LDEAFRRYRN LLFGSGSWPR PSFSNKQQTL GKNILVVSVV TAECNEFPNL ESVENYTLTI 

       130        140        150        160        170        180 
NDDQCLLASE TVWGALRGLE TFSQLVWKSA EGTFFINKTK IKDFPRFPHR GVLLDTSRHY 

       190        200        210        220        230        240 
LPLSSILDTL DVMAYNKFNV FHWHLVDDSS FPYESFTFPE LTRKGSFNPV THIYTAQDVK 

       250        260        270        280        290        300 
EVIEYARLRG IRVLAEFDTP GHTLSWGPGA PGLLTPCYSG SHLSGTFGPV NPSLNSTYDF 

       310        320        330        340        350        360 
MSTLFLEISS VFPDFYLHLG GDEVDFTCWK SNPNIQAFMK KKGFTDFKQL ESFYIQTLLD 

       370        380        390        400        410        420 
IVSDYDKGYV VWQEVFDNKV KVRPDTIIQV WREEMPVEYM LEMQDITRAG FRALLSAPWY 

       430        440        450        460        470        480 
LNRVKYGPDW KDMYKVEPLA FHGTPEQKAL VIGGEACMWG EYVDSTNLVP RLWPRAGAVA 

       490        500        510        520 
ERLWSSNLTT NIDFAFKRLS HFRCELVRRG IQAQPISVGY CEQEFEQT 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X64331 mRNA. Translation: CAA45615.1.
U05837 expand/collapse EMBL AC list , U05824, U05825, U05826, U05827, U05828, U05829, U05830, U05831, U05832, U05833, U05834, U05835, U05836 Genomic DNA. Translation: AAC53246.1.
U07721 expand/collapse EMBL AC list , 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.
PIRI48253.
RefSeqNP_034551.2. NM_010421.4.
UniGeneMm.2284.

3D structure databases

ProteinModelPortalP29416.
SMRP29416. Positions 23-527.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid200280. 1 interaction.
IntActP29416. 1 interaction.
STRING10090.ENSMUSP00000026262.

Protein family/group databases

CAZyGH20. Glycoside Hydrolase Family 20.

PTM databases

PhosphoSiteP29416.

Proteomic databases

PaxDbP29416.
PRIDEP29416.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000026262; ENSMUSP00000026262; ENSMUSG00000025232.
GeneID15211.
KEGGmmu:15211.
UCSCuc009pxw.1. mouse.

Organism-specific databases

CTD3073.
MGIMGI:96073. Hexa.

Phylogenomic databases

eggNOGCOG3525.
GeneTreeENSGT00390000008107.
HOGENOMHOG000157972.
HOVERGENHBG005961.
InParanoidQ91XG3.
KOK12373.
OMAKVKVRPD.
OrthoDBEOG7KDFB6.
TreeFamTF313036.

Gene expression databases

ArrayExpressP29416.
BgeeP29416.
CleanExMM_HEXA.
GenevestigatorP29416.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR025705. Beta_hexosaminidase_sua/sub.
IPR015883. Glyco_hydro_20_cat-core.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF00728. Glyco_hydro_20. 1 hit.
[Graphical view]
PIRSFPIRSF001093. B-hxosamndse_ab_euk_. 1 hit.
PRINTSPR00738. GLHYDRLASE20.
SUPFAMSSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Other

NextBio287777.
PROP29416.
SOURCESearch...

Entry information

Entry nameHEXA_MOUSE
AccessionPrimary (citable) accession number: P29416
Secondary accession number(s): Q64246, Q91XG3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 111 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries