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Q22492 (HEXA_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 99. 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 A

EC=3.2.1.52
Alternative name(s):
Beta-N-acetylhexosaminidase
N-acetyl-beta-glucosaminidase
Gene names
Name:hex-1
ORF Names:T14F9.3
OrganismCaenorhabditis elegans [Reference proteome]
Taxonomic identifier6239 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis

Protein attributes

Sequence length555 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Responsible for the degradation of GM2 gangliosides, and a variety of other molecules containing terminal N-acetyl hexosamines. Degrades chitotriose. Ref.1

Catalytic activity

Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides. Ref.1

Subcellular location

Lysosome Potential.

Tissue specificity

Expressed in coelomocytes and neurons of the pharyngeal region and nerve cord. Ref.1

Developmental stage

Expressed throughout the life cycle. Ref.1

Disruption phenotype

Worms show reduced degradation of p-nitrophenyl-beta-N-acetylglucosaminide and no chitotriosidase activity. Ref.1

Sequence similarities

Belongs to the glycosyl hydrolase 20 family.

Biophysicochemical properties

Kinetic parameters:

KM=1.1 mM for p-nitrophenyl-beta-N-acetylglucosaminide Ref.1

pH dependence:

Optimum pH is 5.5.

Ontologies

Keywords
   Cellular componentLysosome
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from direct assay Ref.1. Source: UniProtKB

   Cellular_componentlysosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionbeta-N-acetylhexosaminidase activity

Inferred from direct assay Ref.1. Source: UniProtKB

hexosaminidase activity

Inferred from direct assay Ref.1. Source: WormBase

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 555537Beta-hexosaminidase A
PRO_0000012009

Sites

Active site3251Proton donor By similarity

Amino acid modifications

Glycosylation471N-linked (GlcNAc...) Potential
Glycosylation3511N-linked (GlcNAc...) Ref.3 Ref.4 Ref.5
Glycosylation4121N-linked (GlcNAc...) Potential
Glycosylation4601N-linked (GlcNAc...) Ref.3 Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q22492 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 5E797F9FD82F6BB4

FASTA55564,379
        10         20         30         40         50         60 
MRLLIPILIF ALITTAVTWF YGRDDPDRWS VGGVWPLPKK IVYGSKNRTI TYDKIGIDLG 

        70         80         90        100        110        120 
DKKDCDILLS MADNYMNKWL FPFPVEMKTG GTEDFIITVT VKDECPSGPP VHGASEEYLL 

       130        140        150        160        170        180 
RVSLTEAVIN AQTVWGALRA MESLSHLVFY DHKSQEYQIR TVEIFDKPRF PVRGIMIDSS 

       190        200        210        220        230        240 
RHFLSVNVIK RQLEIMSMNK LNVLHWHLVD SESFPYTSVK FPELHGVGAY SPRHVYSRED 

       250        260        270        280        290        300 
IADVIAFARL RGIRVIPEFD LPGHTSSWRG RKGFLTECFD EKGVETFLPN LVDPMNEANF 

       310        320        330        340        350        360 
DFISEFLEEV TETFPDQFLH LGGDEVSDYI VECWERNKKI RKFMEEKGFG NDTVLLENYF 

       370        380        390        400        410        420 
FEKLYKIVEN LKLKRKPIFW QEVFDNNIPD PNAVIHIWKG NTHEEIYEQV KNITSQNFPV 

       430        440        450        460        470        480 
IVSACWYLNY IKYGADWRDE IRGTAPSNSR YYYCDPTNFN GTVAQKELVW GGIAAIWGEL 

       490        500        510        520        530        540 
VDNTNIEARL WPRASAAAER LWSPAEKTQR AEDAWPRMHE LRCRLVSRGY RIQPNNNPDY 

       550 
CPFEFDEPPA TKTEL 

« Hide

References

« Hide 'large scale' references
[1]"Biosynthesis of truncated N-linked oligosaccharides results from non-orthologous hexosaminidase-mediated mechanisms in nematodes, plants, and insects."
Gutternigg M., Kretschmer-Lubich D., Paschinger K., Rendic D., Hader J., Geier P., Ranftl R., Jantsch V., Lochnit G., Wilson I.B.H.
J. Biol. Chem. 282:27825-27840(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
[2]"Genome sequence of the nematode C. elegans: a platform for investigating biology."
The C. elegans sequencing consortium
Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bristol N2.
[3]"Lectin affinity capture, isotope-coded tagging and mass spectrometry to identify N-linked glycoproteins."
Kaji H., Saito H., Yamauchi Y., Shinkawa T., Taoka M., Hirabayashi J., Kasai K., Takahashi N., Isobe T.
Nat. Biotechnol. 21:667-672(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-351 AND ASN-460, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Bristol N2.
[4]"Identification of the hydrophobic glycoproteins of Caenorhabditis elegans."
Fan X., She Y.-M., Bagshaw R.D., Callahan J.W., Schachter H., Mahuran D.J.
Glycobiology 15:952-964(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-351, IDENTIFICATION BY MASS SPECTROMETRY.
[5]"Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis elegans and suggests an atypical translocation mechanism for integral membrane proteins."
Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T., Taoka M., Takahashi N., Isobe T.
Mol. Cell. Proteomics 6:2100-2109(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-351 AND ASN-460, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Bristol N2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM748820 mRNA. Translation: CAO72174.1.
FO081076 Genomic DNA. Translation: CCD68941.1.
PIRT29377.
RefSeqNP_508409.1. NM_076008.6.
UniGeneCel.353.

3D structure databases

ProteinModelPortalQ22492.
SMRQ22492. Positions 90-547.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH20. Glycoside Hydrolase Family 20.

Proteomic databases

PaxDbQ22492.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaT14F9.3; T14F9.3; WBGene00020509.
GeneID180533.
KEGGcel:CELE_T14F9.3.
UCSCT14F9.3. c. elegans.

Organism-specific databases

CTD180533.
WormBaseT14F9.3; CE07499; WBGene00020509; hex-1.

Phylogenomic databases

eggNOGCOG3525.
GeneTreeENSGT00390000008107.
HOGENOMHOG000157972.
InParanoidQ22492.
KOK12373.
OMADSESFPY.
PhylomeDBQ22492.

Enzyme and pathway databases

BRENDA3.2.1.52. 1045.
SABIO-RKQ22492.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
3.30.379.10. 1 hit.
InterProIPR025705. 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]
PfamPF00728. Glyco_hydro_20. 1 hit.
PF14845. Glycohydro_20b2. 1 hit.
[Graphical view]
PIRSFPIRSF001093. B-hxosamndse_ab_euk_. 1 hit.
PRINTSPR00738. GLHYDRLASE20.
SUPFAMSSF51445. SSF51445. 1 hit.
SSF55545. SSF55545. 1 hit.
ProtoNetSearch...

Other

NextBio909772.
PROQ22492.

Entry information

Entry nameHEXA_CAEEL
AccessionPrimary (citable) accession number: Q22492
Secondary accession number(s): A7DY65
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: June 11, 2014
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Caenorhabditis elegans

Caenorhabditis elegans: entries, gene names and cross-references to WormBase