ID F1QUU0_DANRE Unreviewed; 464 AA. AC F1QUU0; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 03-AUG-2022, entry version 66. DE RecName: Full=Beta-N-acetylhexosaminidase {ECO:0000256|ARBA:ARBA00012663}; DE EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663}; GN OrderedLocusNames=hexb {ECO:0000313|Ensembl:ENSDARP00000088748, GN ECO:0000313|ZFIN:ZDB-GENE-030131-2333}; GN ORFNames=SO:0001217 {ECO:0000313|ZFIN:ZDB-GENE-030131-2333}; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Danionidae; Danioninae; Danio. OX NCBI_TaxID=7955 {ECO:0000313|Ensembl:ENSDARP00000088748}; RN [1] {ECO:0000313|Ensembl:ENSDARP00000088748} RP IDENTIFICATION. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000088748}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. RN [2] {ECO:0000313|Ensembl:ENSDARP00000088748} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000088748}; RX PubMed=23594743; DOI=10.1038/nature12111; RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M., RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I., RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J., RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y., RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B., RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S., RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G., RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P., RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N., RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J., RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J., RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D., RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S., RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E., RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A., RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J., RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E., RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C., RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C., RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M., RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F., RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M., RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M., RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C., RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.; RT "The zebrafish reference genome sequence and its relationship to the human RT genome."; RL Nature 496:498-503(2013). CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + N-acetyl-beta-D-6-sulfogalactosaminyl-(1->4)-alpha-L- CC iduronyl-(1->3)-N-acetyl-D-6-sulfogalactosamine = 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=H2O + N-acetyl-beta-D-galactosaminyl-(1->4)-beta-D-3- CC sulfogalactosyl-(1->4)-beta-D-glucosyl-(1<->1')-ceramide = a beta-D- CC 3-sulfogalactosyl-(1->4)-beta-D-glucosyl-(1<->1')-ceramide + N- CC acetyl-beta-D-galactosamine; Xref=Rhea:RHEA:48276, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:28497, ChEBI:CHEBI:90163, ChEBI:CHEBI:90164; CC 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 -!- 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 -!- CATALYTIC ACTIVITY: CC Reaction=ganglioside GM2 (d18:1(4E)) + H2O = 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:ARBA00023546}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47941; CC Evidence={ECO:0000256|ARBA:ARBA00023546}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ganglioside GM2 + H2O = 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:ARBA00023512}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47969; CC Evidence={ECO:0000256|ARBA:ARBA00023512}; CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000256|ARBA:ARBA00004371}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family. CC {ECO:0000256|ARBA:ARBA00006285}. 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; FP016255; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; NP_001296792.1; NM_001309863.1. DR Ensembl; ENSDART00000097975.4; ENSDARP00000088748.3; ENSDARG00000034368.10. DR GeneID; 323613; -. DR CTD; 3074; -. DR ZFIN; ZDB-GENE-030131-2333; hexb. DR ZFIN; ZDB-GENE-030131-2333; SO:0001217. DR GeneTree; ENSGT00390000008107; -. DR OrthoDB; 545162at2759; -. DR Proteomes; UP000814640; Chromosome 5. DR Bgee; ENSDARG00000034368; Expressed in intestine and 24 other tissues. DR ExpressionAtlas; F1QUU0; baseline and differential. 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; IBA:GO_Central. DR GO; GO:0015929; F:hexosaminidase activity; IMP:ZFIN. DR GO; GO:0102148; F:N-acetyl-beta-D-galactosaminidase activity; IEA:UniProtKB-EC. DR GO; GO:0001525; P:angiogenesis; IMP:ZFIN. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. 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 Glycosidase {ECO:0000256|ARBA:ARBA00023295}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Proteomics identification {ECO:0007829|PeptideAtlas:F1QUU0}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1..19 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 20..464 FT /note="Beta-N-acetylhexosaminidase" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5003273202" FT DOMAIN 37..160 FT /note="Glycohydro_20b2" FT /evidence="ECO:0000259|Pfam:PF14845" FT DOMAIN 182..447 FT /note="Glyco_hydro_20" FT /evidence="ECO:0000259|Pfam:PF00728" FT ACT_SITE 338 FT /note="Proton donor" FT /evidence="ECO:0000256|PIRSR:PIRSR001093-1" SQ SEQUENCE 464 AA; 52966 MW; 139FFD70A53A4066 CRC64; MLCLLKFTPL FLVVAVCHGW LFGDLFEKQK ELDEISLWPL PQKYQSSAVA FKLSAASFQI VHAKQSTAGP SCSLLENAFR RYFEYMFGEL KRQEKSRKKA FDSDLSELQV WITSADPECD GYPSLRTDES YSLSVDETSA VLKAANVWGA LRGLETFSQL VYEDDYGVRN INKTDISDFP RFAHRGILLD SSRHFLPLKV ILANLEAMAM NKFNVFHWHI VDDPSFPFMS RTFPELSQKG AYHPFTHVYT PSDVKMVIEF ARMRGIRVVA EFDTPGHTQS WGNGIKDLLT PCYSGSSPSG SFGPVNPILN SSYEFMAQLF KEISTVFPDA YIHLGGDEVD FSCWKSNPDI QKFMNQQGFG TDYSKLESFY IQRLLDIVAA TKKGYMVWQE VFDNGVKLKD DTVVEVWKGN DMKEELQNVT GAGFTTILSA PWYLDYISYG QDWQRYYKVE PLDFTGQFLQ SNSF //