Beta-hexosaminidase subunit alpha precursor

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Reviewed, UniProtKB/Swiss-Prot P29416 (HEXA_MOUSE)

Last modified October 13, 2009. Version 74. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Beta-hexosaminidase subunit alpha
    EC=3.2.1.52
Alternative name(s):
    N-acetyl-beta-glucosaminidase subunit alpha
    Beta-N-acetylhexosaminidase subunit alpha
      Short name=Hexosaminidase subunit A

Gene names

Name:

Hexa

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length	528 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

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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 an 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.

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Ontologies

Keywords
Cellular component	Lysosome
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond Glycoprotein Zymogen
Gene Ontology (GO)
Biological process	adult walking behavior Inferred from mutant phenotype. Source: MGI ganglioside catabolic process Inferred from mutant phenotype. Source: MGI glycosaminoglycan metabolic process Inferred from genetic interaction. Source: MGI lipid storage Inferred from mutant phenotype. Source: MGI lysosome organization Inferred from mutant phenotype. Source: MGI myelination Inferred from genetic interaction. Source: MGI neuromuscular process controlling balance Inferred from genetic interaction. Source: MGI neuromuscular process controlling posture Inferred from mutant phenotype. Source: MGI sensory perception of sound Inferred from genetic interaction. Source: MGI sexual reproduction Inferred from mutant phenotype. Source: MGI skeletal system development Inferred from genetic interaction. Source: MGI
Cellular component	lysosome Inferred from direct assay. Source: MGI membrane Inferred from direct assay. Source: MGI
Molecular function	beta-N-acetylhexosaminidase activity Inferred from direct assay. Source: MGI cation binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 22

By similarity

Propeptide

23 – 88

By similarity

PRO_0000011995

Chain

89 – 528

440

Beta-hexosaminidase subunit alpha

PRO_0000011996

Sites

Active site

323

Proton donor By similarity

Amino acid modifications

Glycosylation

115

N-linked (GlcNAc...) Potential

Glycosylation

157

N-linked (GlcNAc...) Potential

Glycosylation

295

N-linked (GlcNAc...) Potential

Glycosylation

487

N-linked (GlcNAc...) Potential

Disulfide bond

58 ↔ 104

By similarity

Disulfide bond

277 ↔ 328

By similarity

Disulfide bond

504 ↔ 521

By similarity

Experimental info

Sequence conflict

G → A Ref.3

Sequence conflict

G → A Ref.4

Sequence conflict

237

Q → E Ref.4

Sequence conflict

455

E → Q Ref.4

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Sequences

Sequence

Length

Mass (Da)

Tools

P29416-1 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: 5C723B82DAEC3B43
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FASTA

528

60,599

        10         20         30         40         50         60 
MAGCRLWVSL LLAAALACLA TALWPWPQYI QTYHRRYTLY PNNFQFRYHV SSAAQGGCVV 

        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

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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: 1379046] [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: 7833835] [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: 7959736] [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: 7896264] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY. Strain: 129/Sv. Tissue: Liver.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	X64331 mRNA. Translation: CAA45615.1. U05837 U05836 Genomic DNA. Translation: AAC53246.1. U07721 U07720 Unassigned DNA. Translation: AAA18777.1. U07631 mRNA. Translation: AAA18775.1. X79061 Genomic DNA. No translation available. X79062 Genomic DNA. No translation available.
IPI	IPI00125522.
PIR	I48253.
RefSeq	NP_034551.2.
UniGene	Mm.2284
3D structure databases
HSSP	HSSP built from PDB template 1NOW based on UniProtKB P07686.
SMR	P29416. Positions 23-527.
ModBase	Search...
Protein-protein interaction databases
STRING	P29416.
Protein family/group databases
CAZy	GH20. Glycoside Hydrolase Family 20.
Proteomic databases
PRIDE	P29416.
Genome annotation databases
Ensembl	ENSMUST00000026262; ENSMUSP00000026262; ENSMUSG00000025232; Mus musculus. [Genome view]
GeneID	15211.
KEGG	mmu:15211.
Organism-specific databases
MGI	MGI:96073. Hexa.
Phylogenomic databases
HOGENOM	P29416.
HOVERGEN	P29416.
Enzyme and pathway databases
BRENDA	3.2.1.52. 244.
Gene expression databases
ArrayExpress	P29416.
Bgee	P29416.
CleanEx	MM_HEXA.
Genevestigator	P29416.
GermOnline	ENSMUSG00000025232. Mus musculus.
Family and domain databases
InterPro	IPR001540. Glyco_hydro_20. IPR015883. Glyco_hydro_20_cat-core. IPR013781. Glyco_hydro_sg_catalytic. IPR015882. HexNAc-like_b. [Graphical view]
Gene3D	G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
PANTHER	PTHR22600. Glyco_hydro_20. 1 hit.
Pfam	PF00728. Glyco_hydro_20. 1 hit. PF02838. Glyco_hydro_20b. 1 hit. [Graphical view]
PRINTS	PR00738. GLHYDRLASE20.
ProtoNet	Search...
Other Resources
SOURCE	Search...

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Entry information

Entry name

HEXA_MOUSE

Accession

Primary (citable) accession number: P29416
Secondary accession number(s): Q64246

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	April 1, 1993
Last modified:	October 13, 2009
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents