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Q0V8R6 (HEXA_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length529 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 By similarity.

Catalytic activity

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

Subcellular location

Lysosome By similarity.

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 electronic annotation. Source: Compara

carbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

cell morphogenesis involved in neuron differentiation

Inferred from electronic annotation. Source: Compara

ganglioside catabolic process

Inferred from electronic annotation. Source: Compara

glycosaminoglycan metabolic process

Inferred from electronic annotation. Source: Compara

lipid storage

Inferred from electronic annotation. Source: Compara

lysosome organization

Inferred from electronic annotation. Source: Compara

myelination

Inferred from electronic annotation. Source: Compara

neuromuscular process controlling balance

Inferred from electronic annotation. Source: Compara

neuromuscular process controlling posture

Inferred from electronic annotation. Source: Compara

sensory perception of sound

Inferred from electronic annotation. Source: Compara

sexual reproduction

Inferred from electronic annotation. Source: Compara

skeletal system development

Inferred from electronic annotation. Source: Compara

   Cellular_componentlysosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

membrane

Inferred from electronic annotation. Source: Compara

   Molecular_functionbeta-N-acetylhexosaminidase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 By similarity
Propeptide23 – 8866 By similarity
PRO_0000274203
Chain89 – 529441Beta-hexosaminidase subunit alpha
PRO_0000274204

Regions

Region423 – 4242Critical 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
Disulfide bond58 ↔ 104 By similarity
Disulfide bond277 ↔ 328 By similarity
Disulfide bond505 ↔ 522 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0V8R6 [UniParc].

Last modified September 5, 2006. Version 1.
Checksum: 878641B502FCD3A9

FASTA52960,353
        10         20         30         40         50         60 
MAGSTLRFSL LLAAAFAGRA TALWPWPQYI QTSELRYTIF PQSFQFQYHL SSAAQVGCSV 

        70         80         90        100        110        120 
LDEAFQRYRD LLFGSVAFRF PHPIEKRHTS EKNSLVVLVV TPGCDQFPSL GSVENYTLTI 

       130        140        150        160        170        180 
NDEQSLLLSE TVWGALRGLE TFSQLIWRSP EGTFYVNKTD IEDFPRFPHR GLLLDTSRHY 

       190        200        210        220        230        240 
LPLASILDTL DVMAYNKFNV FHWHLVDDSS FPYESFTFPE LTKKGSYNPA THIYTAQDVK 

       250        260        270        280        290        300 
EVIEYARLRG IRVLAEFDTP GHTLSWGPGV PGLLTPCYSG SHPSGTFGPV NPALNNTYEF 

       310        320        330        340        350        360 
MSTFFLEIST VFPDFYLHLG GDEVDFTCWK SNPDIQAFMK KKGFGDDFKK LESFYIQTLL 

       370        380        390        400        410        420 
DIVSAYGKGY VVWQEVFDNK VKVRPDTIIQ VWREEIPVKY VKELALVTRA GFRALLSAPW 

       430        440        450        460        470        480 
YLNHITYGPD WKEIYLVEPL AFEGSPEQKA LVIGGEACMW GEYVDSTNLV PRLWPRAGAV 

       490        500        510        520 
AERLWSNKMV SNLDFAFKRL AHFRCELLRR GVQAQPLSVG YCDMEFEQT

« Hide

References

[1]"Characterization of 954 bovine full-CDS cDNA sequences."
Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.
BMC Genomics 6:166-166(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BT026152 mRNA. Translation: ABG66991.1.
IPIIPI00702413.
RefSeqNP_001068632.1. NM_001075164.2.
UniGeneBt.6065.

3D structure databases

ProteinModelPortalQ0V8R6.
SMRQ0V8R6. Positions 23-528.
ModBaseSearch...

Protein-protein interaction databases

STRING9913.ENSBTAP00000017261.

Protein family/group databases

CAZyGH20. Glycoside Hydrolase Family 20.

Proteomic databases

PRIDEQ0V8R6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000017261; ENSBTAP00000017261; ENSBTAG00000012981.
GeneID504468.
KEGGbta:504468.

Organism-specific databases

CTD3073.

Phylogenomic databases

eggNOGCOG3525.
GeneTreeENSGT00390000008107.
HOGENOMHOG000157972.
HOVERGENHBG005961.
InParanoidQ0V8R6.
KOK12373.
OMAKVKVRPD.
OrthoDBEOG42Z4Q7.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR025705. 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]
PfamPF00728. Glyco_hydro_20. 1 hit.
PF02838. Glyco_hydro_20b. 1 hit.
[Graphical view]
PIRSFPIRSF001093. B-hxosamndse_ab_euk_. 1 hit.
PRINTSPR00738. GLHYDRLASE20.
SUPFAMSSF51445. Glyco_hydro_cat. 1 hit.
ProtoNetSearch...

Other

ChEMBLCHEMBL1075052.
NextBio20866675.

Entry information

Entry nameHEXA_BOVIN
AccessionPrimary (citable) accession number: Q0V8R6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 6, 2007
Last sequence update: September 5, 2006
Last modified: May 1, 2013
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

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