ID A0A2I0U9D6_LIMLA Unreviewed; 558 AA. AC A0A2I0U9D6; DT 28-FEB-2018, integrated into UniProtKB/TrEMBL. DT 28-FEB-2018, sequence version 1. DT 27-NOV-2024, entry version 23. DE RecName: Full=Beta-hexosaminidase {ECO:0000256|PIRNR:PIRNR001093}; DE EC=3.2.1.52 {ECO:0000256|PIRNR:PIRNR001093}; GN ORFNames=llap_7024 {ECO:0000313|EMBL:PKU42669.1}; OS Limosa lapponica baueri. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Neoaves; Charadriiformes; Scolopacidae; OC Limosa. OX NCBI_TaxID=1758121 {ECO:0000313|EMBL:PKU42669.1, ECO:0000313|Proteomes:UP000233556}; RN [1] {ECO:0000313|Proteomes:UP000233556} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Lima N.C., Parody-Merino A.M., Battley P.F., Fidler A.E., Prosdocimi F.; RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000233556} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Lima N.C.B., Parody-Merino A.M., Battley P.F., Fidler A.E., Prosdocimi F.; RT "Genome sequence of the Bar-tailed Godwit (Limosa lapponica baueri)."; RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Hydrolyzes the non-reducing end N-acetyl-D-hexosamine and/or CC sulfated N-acetyl-D-hexosamine of glycoconjugates, such as the CC oligosaccharide moieties from proteins and neutral glycolipids, or from CC certain mucopolysaccharides. The isozyme B does not hydrolyze each of CC these substrates, however hydrolyzes efficiently neutral CC oligosaccharide. Only the isozyme A is responsible for the degradation CC of GM2 gangliosides in the presence of GM2A. During fertilization is CC responsible, at least in part, for the zona block to polyspermy. CC Present in the cortical granules of non-activated oocytes, is CC exocytosed during the cortical reaction in response to oocyte CC activation and inactivates the sperm galactosyltransferase-binding CC site, accounting for the block in sperm binding to the zona pellucida. CC {ECO:0000256|ARBA:ARBA00045511}. CC -!- CATALYTIC ACTIVITY: CC Reaction=N-acetyl-beta-D-6-sulfogalactosaminyl-(1->4)-alpha-L-iduronyl- CC (1->3)-N-acetyl-D-6-sulfogalactosamine + H2O = alpha-L-iduronyl- CC (1->3)-N-acetyl-D-6-sulfogalactosamine + N-acetyl-D-6- CC sulfogalactosamine; Xref=Rhea:RHEA:64384, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:152567, ChEBI:CHEBI:152568, ChEBI:CHEBI:153064; CC Evidence={ECO:0000256|ARBA:ARBA00023541}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64385; CC Evidence={ECO:0000256|ARBA:ARBA00023541}; CC -!- CATALYTIC ACTIVITY: CC Reaction=N-acetyl-beta-D-galactosaminyl-(1->4)-beta-D-3- CC sulfogalactosyl-(1->4)-beta-D-glucosyl-(1<->1')-ceramide + H2O = a CC beta-D-3-sulfogalactosyl-(1->4)-beta-D-glucosyl-(1<->1')-ceramide + CC N-acetyl-beta-D-galactosamine; Xref=Rhea:RHEA:48276, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:28497, ChEBI:CHEBI:90163, CC ChEBI:CHEBI:90164; Evidence={ECO:0000256|ARBA:ARBA00023953}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48277; CC Evidence={ECO:0000256|ARBA:ARBA00023953}; 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:0000256|ARBA:ARBA00001231, CC ECO:0000256|PIRNR:PIRNR001093}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a ganglioside GM2 (d18:1(4E)) + H2O = a ganglioside GM3 CC (d18:1(4E)) + N-acetyl-beta-D-galactosamine; Xref=Rhea:RHEA:47940, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:28497, ChEBI:CHEBI:60065, CC ChEBI:CHEBI:71502; Evidence={ECO:0000256|ARBA:ARBA00043767}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47941; CC Evidence={ECO:0000256|ARBA:ARBA00043767}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a ganglioside GM2 + H2O = a ganglioside GM3 + N-acetyl-beta-D- CC galactosamine; Xref=Rhea:RHEA:47968, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:28497, ChEBI:CHEBI:79210, ChEBI:CHEBI:79218; CC Evidence={ECO:0000256|ARBA:ARBA00043827}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47969; CC Evidence={ECO:0000256|ARBA:ARBA00043827}; CC -!- CATALYTIC ACTIVITY: CC Reaction=beta-D-GalNAc-(1->4)-alpha-L-IdoA-(1->3)-beta-D-GalNAc-4- CC sulfate-(1->4)-alpha-L-IdoA-(1->3)-D-GalNAc-4-sulfate + H2O = alpha- CC L-IdoA-(1->3)-beta-D-GalNAc-4-sulfate-(1->4)-alpha-L-IdoA-(1->3)-D- CC GalNAc-4-sulfate + N-acetyl-D-galactosamine; Xref=Rhea:RHEA:64372, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:28037, ChEBI:CHEBI:152565, CC ChEBI:CHEBI:152566; Evidence={ECO:0000256|ARBA:ARBA00023505}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64373; CC Evidence={ECO:0000256|ARBA:ARBA00023505}; CC -!- SUBUNIT: There are 3 forms of beta-hexosaminidase: hexosaminidase A is CC a heterodimer composed of one subunit alpha and one subunit beta (chain CC A and B); hexosaminidase B is a homodimer of two beta subunits (two CC chains A and B); hexosaminidase S is a homodimer of two alpha subunits. CC The composition of the dimer (isozyme A versus isozyme S) has a CC significant effect on the substrate specificity of the alpha subunit CC active site. {ECO:0000256|ARBA:ARBA00046959}. CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, Cortical CC granule {ECO:0000256|ARBA:ARBA00037865}. Lysosome CC {ECO:0000256|ARBA:ARBA00004371}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family. CC {ECO:0000256|ARBA:ARBA00006285, ECO:0000256|PIRNR:PIRNR001093}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; KZ505970; PKU42669.1; -; Genomic_DNA. DR AlphaFoldDB; A0A2I0U9D6; -. DR SMR; A0A2I0U9D6; -. DR Proteomes; UP000233556; Unassembled WGS sequence. DR GO; GO:0060473; C:cortical granule; IEA:UniProtKB-SubCell. DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; IEA:TreeGrafter. DR GO; GO:0004563; F:beta-N-acetylhexosaminidase activity; IEA:UniProtKB-EC. DR GO; GO:0102148; F:N-acetyl-beta-D-galactosaminidase activity; IEA:UniProtKB-EC. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR GO; GO:0006689; P:ganglioside catabolic process; IEA:TreeGrafter. DR GO; GO:0030203; P:glycosaminoglycan metabolic process; IEA:TreeGrafter. DR CDD; cd06562; GH20_HexA_HexB-like; 1. DR FunFam; 3.20.20.80:FF:000049; Beta-hexosaminidase A; 1. DR Gene3D; 3.30.379.10; Chitobiase/beta-hexosaminidase domain 2-like; 1. DR Gene3D; 3.20.20.80; Glycosidases; 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; BETA-HEXOSAMINIDASE; 1. DR PANTHER; PTHR22600:SF38; BETA-HEXOSAMINIDASE SUBUNIT BETA; 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; (Trans)glycosidases; 1. DR SUPFAM; SSF55545; beta-N-acetylhexosaminidase-like domain; 1. PE 3: Inferred from homology; KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, KW ECO:0000256|PIRSR:PIRSR001093-2}; KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PIRNR:PIRNR001093}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR001093}; KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098}; KW Lysosome {ECO:0000256|ARBA:ARBA00023228}; KW Reference proteome {ECO:0000313|Proteomes:UP000233556}; KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}. FT SIGNAL 1..18 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 19..558 FT /note="Beta-hexosaminidase" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5014190499" FT DOMAIN 52..178 FT /note="Beta-hexosaminidase eukaryotic type N-terminal" FT /evidence="ECO:0000259|Pfam:PF14845" FT DOMAIN 200..516 FT /note="Glycoside hydrolase family 20 catalytic" FT /evidence="ECO:0000259|Pfam:PF00728" FT ACT_SITE 355 FT /note="Proton donor" FT /evidence="ECO:0000256|PIRSR:PIRSR001093-1" FT DISULFID 87..137 FT /evidence="ECO:0000256|PIRSR:PIRSR001093-2" FT DISULFID 309..360 FT /evidence="ECO:0000256|PIRSR:PIRSR001093-2" FT DISULFID 534..551 FT /evidence="ECO:0000256|PIRSR:PIRSR001093-2" SQ SEQUENCE 558 AA; 62896 MW; DDC3972197437471 CRC64; MGLAGLLLGL FLVPAVLVST SLRHGVPPTE PEAPPELAEW ESVSGTVRED SLWPLPQWLR TSRRQLQLAP GRFQLVHGAG SSAGPGCGLL QDAFRRYYEY MFGQSRGRTW GRGPPGGLGG PELLELQVVI EAPDPGCNSY PHLASSEAYH LTVTEPVAIL KADEVWGALR GLETFSQLVH EDDYGSFLVN ESEIDDFPRF AHRGILLDTS RHYLPLKSIL TNLDAMAFNK FNVLHWHIVD DQSFPYQSIY FPELSDKGAY SYNHIYTPTD VRLVIEYARL RGIRVIPEFD TPGHTQSWGK GQKDLLTPCY SGKHPTGSFG PVNPILNTTY DFMTKFYKEI SNVFPDAYIH LGGDEVDFNC WKSNPDVREF MKQQGFGIDY AKLESYYIQK ILDIVSSNNK GYVVWQEVFD NKAQLKPDTV VQVWIGNNYA HELSSVTGAG FTAILSAPWY LDYISYGQDW KKYYSVEPLN FPGSEKQKKL LIGGEACLWG EFVDATNLTP RLWPRASAVG ERLWSSRNVT NLQDAYERLT NHRCRMLRRG IAAEPVFTGY CAHEARGQ //