P29416 (HEXA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

Hexa

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

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

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 component	Lysosome
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond Glycoprotein Zymogen
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	adult 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 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_component	lysosome Inferred from direct assay PubMed 11854359PubMed 9645704. Source: MGI membrane Inferred from direct assay PubMed 11854359. Source: MGI
Molecular_function	beta-N-acetylhexosaminidase activity Inferred from direct assay PubMed 11854359PubMed 1914521PubMed 8747922PubMed 9417048. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 22	22	By similarity
	Propeptide	23 – 88	66	By similarity		PRO_0000011995
	Chain	89 – 528	440	Beta-hexosaminidase subunit alpha		PRO_0000011996
Regions
	Region	422 – 423	2	Critical for hydrolyzis GM2 gangliosides By similarity
Sites
	Active site	323	1	Proton donor By similarity
Amino acid modifications
	Glycosylation	115	1	N-linked (GlcNAc...) Potential
	Glycosylation	157	1	N-linked (GlcNAc...) Potential
	Glycosylation	295	1	N-linked (GlcNAc...) Potential
	Glycosylation	487	1	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	56	1	A → G in CAA45615. Ref.1
	Sequence conflict	56	1	A → G in AAC53246. Ref.2
	Sequence conflict	237	1	Q → E in X79061. Ref.4
	Sequence conflict	237	1	Q → E in X79062. Ref.4
	Sequence conflict	455	1	E → Q in X79061. Ref.4
	Sequence conflict	455	1	E → Q in X79062. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P29416 [UniParc]. Last modified July 27, 2011. Version 2. Checksum: 95DEA72D767094EF	FASTA	528	60,613
	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

References

	« Hide 'large scale' referencesShow '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. , 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 , 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.
IPI	IPI00125522.
PIR	I48253.
RefSeq	NP_034551.2. NM_010421.4.
UniGene	Mm.2284.
3D structure databases
HSSP	HSSP built from PDB template 1NOW based on UniProtKB P07686.
ProteinModelPortal	P29416.
SMR	P29416. Positions 23-527.
ModBase	Search...
Protein-protein interaction databases
IntAct	P29416. 1 interaction.
STRING	10090.ENSMUSP00000026262.
Protein family/group databases
CAZy	GH20. Glycoside Hydrolase Family 20.
PTM databases
PhosphoSite	P29416.
Proteomic databases
PaxDb	P29416.
PRIDE	P29416.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000026262; ENSMUSP00000026262; ENSMUSG00000025232.
GeneID	15211.
KEGG	mmu:15211.
Organism-specific databases
CTD	3073.
MGI	MGI:96073. Hexa.
Phylogenomic databases
eggNOG	COG3525.
GeneTree	ENSGT00390000008107.
HOGENOM	HOG000157972.
HOVERGEN	HBG005961.
InParanoid	Q91XG3.
KO	K12373.
OMA	KVKVRPD.
OrthoDB	EOG42Z4Q7.
Gene expression databases
ArrayExpress	P29416.
Bgee	P29416.
CleanEx	MM_HEXA.
Genevestigator	P29416.
GermOnline	ENSMUSG00000025232. Mus musculus.
Family and domain databases
Gene3D	3.20.20.80. 1 hit.
InterPro	IPR025705. Beta_hexosaminidase_sua/sub. IPR015883. Glyco_hydro_20_cat-core. IPR015882. Glyco_hydro_20b. IPR013781. Glyco_hydro_catalytic_dom. IPR017853. Glycoside_hydrolase_SF. [Graphical view]
Pfam	PF00728. Glyco_hydro_20. 1 hit. PF02838. Glyco_hydro_20b. 1 hit. [Graphical view]
PIRSF	PIRSF001093. B-hxosamndse_ab_euk_. 1 hit.
PRINTS	PR00738. GLHYDRLASE20.
SUPFAM	SSF51445. Glyco_hydro_cat. 1 hit.
ProtoNet	Search...
Other
NextBio	287777.
SOURCE	Search...

Entry information

Entry name

HEXA_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 103 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program