HEXA_CAEEL
ID HEXA_CAEEL Reviewed; 555 AA.
AC Q22492; A7DY65;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Beta-hexosaminidase A;
DE EC=3.2.1.52;
DE AltName: Full=Beta-N-acetylhexosaminidase;
DE AltName: Full=N-acetyl-beta-glucosaminidase;
DE Flags: Precursor;
GN Name=hex-1; ORFNames=T14F9.3;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=17636254; DOI=10.1074/jbc.m704235200;
RA Gutternigg M., Kretschmer-Lubich D., Paschinger K., Rendic D., Hader J.,
RA Geier P., Ranftl R., Jantsch V., Lochnit G., Wilson I.B.H.;
RT "Biosynthesis of truncated N-linked oligosaccharides results from non-
RT orthologous hexosaminidase-mediated mechanisms in nematodes, plants, and
RT insects.";
RL J. Biol. Chem. 282:27825-27840(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-351 AND ASN-460, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=12754521; DOI=10.1038/nbt829;
RA Kaji H., Saito H., Yamauchi Y., Shinkawa T., Taoka M., Hirabayashi J.,
RA Kasai K., Takahashi N., Isobe T.;
RT "Lectin affinity capture, isotope-coded tagging and mass spectrometry to
RT identify N-linked glycoproteins.";
RL Nat. Biotechnol. 21:667-672(2003).
RN [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-351, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=15888633; DOI=10.1093/glycob/cwi075;
RA Fan X., She Y.-M., Bagshaw R.D., Callahan J.W., Schachter H., Mahuran D.J.;
RT "Identification of the hydrophobic glycoproteins of Caenorhabditis
RT elegans.";
RL Glycobiology 15:952-964(2005).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-351 AND ASN-460, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA Taoka M., Takahashi N., Isobe T.;
RT "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT elegans and suggests an atypical translocation mechanism for integral
RT membrane proteins.";
RL Mol. Cell. Proteomics 6:2100-2109(2007).
CC -!- FUNCTION: Responsible for the degradation of GM2 gangliosides, and a
CC variety of other molecules containing terminal N-acetyl hexosamines.
CC Degrades chitotriose. {ECO:0000269|PubMed:17636254}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine
CC residues in N-acetyl-beta-D-hexosaminides.; EC=3.2.1.52;
CC Evidence={ECO:0000269|PubMed:17636254};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.1 mM for p-nitrophenyl-beta-N-acetylglucosaminide
CC {ECO:0000269|PubMed:17636254};
CC pH dependence:
CC Optimum pH is 5.5. {ECO:0000269|PubMed:17636254};
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in coelomocytes and neurons of the
CC pharyngeal region and nerve cord. {ECO:0000269|PubMed:17636254}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout the life cycle.
CC {ECO:0000269|PubMed:17636254}.
CC -!- DISRUPTION PHENOTYPE: Worms show reduced degradation of p-nitrophenyl-
CC beta-N-acetylglucosaminide and no chitotriosidase activity.
CC {ECO:0000269|PubMed:17636254}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family. {ECO:0000305}.
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DR EMBL; AM748820; CAO72174.1; -; mRNA.
DR EMBL; FO081076; CCD68941.1; -; Genomic_DNA.
DR PIR; T29377; T29377.
DR RefSeq; NP_508409.1; NM_076008.6.
DR AlphaFoldDB; Q22492; -.
DR SMR; Q22492; -.
DR STRING; 6239.T14F9.3; -.
DR CAZy; GH20; Glycoside Hydrolase Family 20.
DR iPTMnet; Q22492; -.
DR EPD; Q22492; -.
DR PaxDb; Q22492; -.
DR PeptideAtlas; Q22492; -.
DR EnsemblMetazoa; T14F9.3.1; T14F9.3.1; WBGene00020509.
DR EnsemblMetazoa; T14F9.3.2; T14F9.3.2; WBGene00020509.
DR GeneID; 180533; -.
DR KEGG; cel:CELE_T14F9.3; -.
DR UCSC; T14F9.3; c. elegans.
DR CTD; 180533; -.
DR WormBase; T14F9.3; CE07499; WBGene00020509; hex-1.
DR eggNOG; KOG2499; Eukaryota.
DR GeneTree; ENSGT00390000008107; -.
DR HOGENOM; CLU_007082_0_2_1; -.
DR InParanoid; Q22492; -.
DR OMA; VEVWPMP; -.
DR OrthoDB; 545162at2759; -.
DR PhylomeDB; Q22492; -.
DR BRENDA; 3.2.1.52; 1045.
DR Reactome; R-CEL-1660662; Glycosphingolipid metabolism.
DR Reactome; R-CEL-2022857; Keratan sulfate degradation.
DR Reactome; R-CEL-2024101; CS/DS degradation.
DR Reactome; R-CEL-2160916; Hyaluronan uptake and degradation.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR SABIO-RK; Q22492; -.
DR PRO; PR:Q22492; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00020509; Expressed in material anatomical entity and 5 other tissues.
DR GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0004563; F:beta-N-acetylhexosaminidase activity; IDA:UniProtKB.
DR GO; GO:0015929; F:hexosaminidase activity; IDA:WormBase.
DR GO; GO:0102148; F:N-acetyl-beta-D-galactosaminidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IDA:UniProtKB.
DR GO; GO:0006689; P:ganglioside catabolic process; IBA:GO_Central.
DR GO; GO:0030203; P:glycosaminoglycan metabolic process; IBA:GO_Central.
DR Gene3D; 3.30.379.10; -; 1.
DR InterPro; IPR025705; Beta_hexosaminidase_sua/sub.
DR InterPro; IPR015883; Glyco_hydro_20_cat.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR029018; Hex-like_dom2.
DR InterPro; IPR029019; HEX_eukaryotic_N.
DR PANTHER; PTHR22600; PTHR22600; 1.
DR Pfam; PF00728; Glyco_hydro_20; 1.
DR Pfam; PF14845; Glycohydro_20b2; 1.
DR PIRSF; PIRSF001093; B-hxosamndse_ab_euk; 1.
DR PRINTS; PR00738; GLHYDRLASE20.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF55545; SSF55545; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Glycosidase; Hydrolase; Lysosome; Reference proteome; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..555
FT /note="Beta-hexosaminidase A"
FT /id="PRO_0000012009"
FT ACT_SITE 325
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 351
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754521,
FT ECO:0000269|PubMed:15888633, ECO:0000269|PubMed:17761667"
FT CARBOHYD 412
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 460
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754521,
FT ECO:0000269|PubMed:17761667"
SQ SEQUENCE 555 AA; 64379 MW; 5E797F9FD82F6BB4 CRC64;
MRLLIPILIF ALITTAVTWF YGRDDPDRWS VGGVWPLPKK IVYGSKNRTI TYDKIGIDLG
DKKDCDILLS MADNYMNKWL FPFPVEMKTG GTEDFIITVT VKDECPSGPP VHGASEEYLL
RVSLTEAVIN AQTVWGALRA MESLSHLVFY DHKSQEYQIR TVEIFDKPRF PVRGIMIDSS
RHFLSVNVIK RQLEIMSMNK LNVLHWHLVD SESFPYTSVK FPELHGVGAY SPRHVYSRED
IADVIAFARL RGIRVIPEFD LPGHTSSWRG RKGFLTECFD EKGVETFLPN LVDPMNEANF
DFISEFLEEV TETFPDQFLH LGGDEVSDYI VECWERNKKI RKFMEEKGFG NDTVLLENYF
FEKLYKIVEN LKLKRKPIFW QEVFDNNIPD PNAVIHIWKG NTHEEIYEQV KNITSQNFPV
IVSACWYLNY IKYGADWRDE IRGTAPSNSR YYYCDPTNFN GTVAQKELVW GGIAAIWGEL
VDNTNIEARL WPRASAAAER LWSPAEKTQR AEDAWPRMHE LRCRLVSRGY RIQPNNNPDY
CPFEFDEPPA TKTEL
