ID F1QUU0_DANRE Unreviewed; 464 AA. AC F1QUU0; A0A8M1P2A4; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 24-JUL-2024, entry version 77. DE RecName: Full=Beta-hexosaminidase subunit beta {ECO:0000256|ARBA:ARBA00040637}; DE EC=3.2.1.52 {ECO:0000256|ARBA:ARBA00012663}; DE AltName: Full=Beta-N-acetylhexosaminidase subunit beta {ECO:0000256|ARBA:ARBA00042342}; DE AltName: Full=N-acetyl-beta-glucosaminidase subunit beta {ECO:0000256|ARBA:ARBA00042832}; GN Name=hexb {ECO:0000313|Ensembl:ENSDARP00000088748, GN ECO:0000313|RefSeq:NP_001296792.1, GN ECO:0000313|ZFIN:ZDB-GENE-030131-2333}; GN Synonyms=fc04h11 {ECO:0000313|RefSeq:NP_001296792.1}, hexa GN {ECO:0000313|RefSeq:NP_001296792.1}, si:dkey-35i22.2 GN {ECO:0000313|RefSeq:NP_001296792.1}, wu:fc04h11 GN {ECO:0000313|RefSeq:NP_001296792.1}, wu:fv09f06 GN {ECO:0000313|RefSeq:NP_001296792.1}; 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, ECO:0000313|Proteomes:UP000000437} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000088748}; RX PubMed=23594743; DOI=10.1038/nature12111; RG Genome Reference Consortium Zebrafish; 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., Eliott D., RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B., RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M., RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M., RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J., RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D., RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K., RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R., RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D., RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M., RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M., RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D., RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J., RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I., RA Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M., RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M., RA Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B., RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P., RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R., RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I., RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., RA 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). RN [3] {ECO:0000313|RefSeq:NP_001296792.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001296792.1}; RX PubMed=26469318; RA Elkon R., Milon B., Morrison L., Shah M., Vijayakumar S., Racherla M., RA Leitch C.C., Silipino L., Hadi S., Weiss-Gayet M., Barras E., Schmid C.D., RA Ait-Lounis A., Barnes A., Song Y., Eisenman D.J., Eliyahu E., RA Frolenkov G.I., Strome S.E., Durand B., Zaghloul N.A., Jones S.M., RA Reith W., Hertzano R.; RT "RFX transcription factors are essential for hearing in mice."; RL Nat. Commun. 6:8549-8549(2015). RN [4] {ECO:0000313|RefSeq:NP_001296792.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001296792.1}; RX PubMed=26774477; RA Shen K., Sidik H., Talbot W.S.; RT "The Rag-Ragulator Complex Regulates Lysosome Function and Phagocytic Flux RT in Microglia."; RL Cell Rep. 14:547-559(2016). RN [5] {ECO:0000313|RefSeq:NP_001296792.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001296792.1}; RX PubMed=28252024; RA Bayes A., Collins M.O., Reig-Viader R., Gou G., Goulding D., Izquierdo A., RA Choudhary J.S., Emes R.D., Grant S.G.; RT "Evolution of complexity in the zebrafish synapse proteome."; RL Nat. Commun. 8:14613-14613(2017). RN [6] {ECO:0000313|RefSeq:NP_001296792.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001296792.1}; RX PubMed=30399334; RA Meireles A.M., Shen K., Zoupi L., Iyer H., Bouchard E.L., Williams A., RA Talbot W.S.; RT "The Lysosomal Transcription Factor TFEB Represses Myelination Downstream RT of the Rag-Ragulator Complex."; RL Dev. Cell 47:319-330(2018). RN [7] {ECO:0000313|RefSeq:NP_001296792.1} RP IDENTIFICATION. RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001296792.1}; RG RefSeq; RL Submitted (APR-2024) to UniProtKB. 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=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 -!- 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}. 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 AGR; ZFIN:ZDB-GENE-030131-2333; -. DR CTD; 3074; -. DR ZFIN; ZDB-GENE-030131-2333; hexb. DR OrthoDB; 178991at2759; -. DR Proteomes; UP000000437; Chromosome 5. DR Bgee; ENSDARG00000034368; Expressed in intestine and 24 other cell types or tissues. DR GO; GO:0060473; C:cortical granule; IEA:UniProtKB-SubCell. 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; 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 1: Evidence at protein level; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157}; KW Glycosidase {ECO:0000256|ARBA:ARBA00023295}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Proteomics identification {ECO:0007829|PeptideAtlas:F1QUU0}; KW Reference proteome {ECO:0000313|Proteomes:UP000000437}; KW Signal {ECO:0000256|SAM:SignalP, ECO:0000313|RefSeq:NP_001296792.1}. FT SIGNAL 1..19 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 20..464 FT /note="Beta-hexosaminidase subunit beta" FT /evidence="ECO:0000256|SAM:SignalP, FT ECO:0000313|RefSeq:NP_001296792.1" FT /id="PRO_5035035376" FT DOMAIN 37..160 FT /note="Beta-hexosaminidase eukaryotic type N-terminal" FT /evidence="ECO:0000259|Pfam:PF14845" FT DOMAIN 182..446 FT /note="Glycoside hydrolase family 20 catalytic" 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 //