Q22492 (HEXA_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Caenorhabditis elegans [Reference proteome]

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length	555 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 component	Lysosome
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	carbohydrate metabolic process Inferred from direct assay Ref.1. Source: UniProtKB
Cellular_component	lysosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	beta-N-acetylhexosaminidase activity Inferred from direct assay Ref.1. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 18	18	Potential
	Chain	19 – 555	537	Beta-hexosaminidase A		PRO_0000012009
Sites
	Active site	325	1	Proton donor By similarity
Amino acid modifications
	Glycosylation	47	1	N-linked (GlcNAc...) Potential
	Glycosylation	351	1	N-linked (GlcNAc...) Ref.3 Ref.4 Ref.5
	Glycosylation	412	1	N-linked (GlcNAc...) Potential
	Glycosylation	460	1	N-linked (GlcNAc...) Ref.3 Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Q22492 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 5E797F9FD82F6BB4	FASTA	555	64,379
	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

References

	« Hide 'large scale' referencesShow '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, 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, 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, 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.
PIR	T29377.
RefSeq	NP_508409.1. NM_076008.6.
UniGene	Cel.353.
3D structure databases
ProteinModelPortal	Q22492.
SMR	Q22492. Positions 90-547.
ModBase	Search...
Protein family/group databases
CAZy	GH20. Glycoside Hydrolase Family 20.
Proteomic databases
PaxDb	Q22492.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	T14F9.3.1; T14F9.3.1; T14F9.3. T14F9.3.2; T14F9.3.2; T14F9.3.
GeneID	180533.
KEGG	cel:CELE_T14F9.3.
UCSC	T14F9.3. c. elegans.
Organism-specific databases
CTD	180533.
WormBase	T14F9.3; CE07499; WBGene00020509; hex-1.
Phylogenomic databases
eggNOG	COG3525.
GeneTree	ENSGT00390000008107.
HOGENOM	HOG000157972.
InParanoid	Q22492.
KO	K12373.
OMA	SMADNYM.
Enzyme and pathway databases
BRENDA	3.2.1.52. 1045.
SABIO-RK	Q22492.
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	909772.

Entry information

Entry name

HEXA_CAEEL

Accession

Primary (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:	May 1, 2013
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Caenorhabditis annotation project