HEXD_MOUSE
ID HEXD_MOUSE Reviewed; 486 AA.
AC Q3U4H6; B7UUP4; B7UUP5; Q6NSQ8;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Hexosaminidase D {ECO:0000305};
DE EC=3.2.1.52;
DE AltName: Full=Beta-N-acetylhexosaminidase;
DE AltName: Full=Beta-hexosaminidase D;
DE AltName: Full=Hexosaminidase domain-containing protein;
DE AltName: Full=N-acetyl-beta-galactosaminidase;
GN Name=Hexd; Synonyms=Hexdc {ECO:0000312|MGI:MGI:3605542};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, CATALYTIC
RP ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=19040401; DOI=10.1042/bj20081630;
RA Gutternigg M., Rendic D., Voglauer R., Iskratsch T., Wilson I.B.;
RT "Mammalian cells contain a second nucleocytoplasmic hexosaminidase.";
RL Biochem. J. 419:83-90(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=NOD;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-486 (ISOFORM 2).
RC STRAIN=FVB/N-3; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Has hexosaminidase activity (PubMed:19040401). Responsible
CC for the cleavage of the monosaccharides N-acetylglucosamine (GlcNAc)
CC and N-acetylgalactosamine (GalNAc) from cellular substrates. Has a
CC preference for galactosaminide over glucosaminide substrates (By
CC similarity). {ECO:0000250|UniProtKB:Q8WVB3,
CC ECO:0000269|PubMed:19040401}.
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:19040401};
CC -!- ACTIVITY REGULATION: Inhibited by O-(2-acetamido-2-deoxy-D-
CC glucopyranosylidene)amino N-phenylcarbamate (PUGNAc). Inhibited by
CC galacto-NAG-thiazoline (By similarity). {ECO:0000250|UniProtKB:Q8WVB3,
CC ECO:0000269|PubMed:19040401}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.25 mM for p-nitrophenyl-beta-N-acetylgalactosaminide
CC {ECO:0000269|PubMed:19040401};
CC pH dependence:
CC Optimum pH is 5.5. {ECO:0000269|PubMed:19040401};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius.
CC {ECO:0000269|PubMed:19040401};
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000269|PubMed:19040401}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19040401}. Nucleus
CC {ECO:0000269|PubMed:19040401}. Extracellular vesicle
CC {ECO:0000250|UniProtKB:Q8WVB3}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3U4H6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3U4H6-2; Sequence=VSP_030778;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:19040401}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH69960.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; FM204885; CAR57923.1; -; mRNA.
DR EMBL; FM204886; CAR57924.1; -; mRNA.
DR EMBL; AK154237; BAE32455.1; -; mRNA.
DR EMBL; AL808021; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC069960; AAH69960.1; ALT_INIT; mRNA.
DR CCDS; CCDS49013.1; -. [Q3U4H6-1]
DR RefSeq; NP_001001333.2; NM_001001333.2. [Q3U4H6-1]
DR RefSeq; NP_001139545.1; NM_001146073.1. [Q3U4H6-2]
DR RefSeq; XP_006533327.1; XM_006533264.2. [Q3U4H6-2]
DR RefSeq; XP_006533328.1; XM_006533265.3. [Q3U4H6-2]
DR RefSeq; XP_006533329.1; XM_006533266.1. [Q3U4H6-2]
DR RefSeq; XP_006533330.1; XM_006533267.2. [Q3U4H6-2]
DR RefSeq; XP_006533331.1; XM_006533268.3. [Q3U4H6-2]
DR RefSeq; XP_006533332.1; XM_006533269.2. [Q3U4H6-2]
DR AlphaFoldDB; Q3U4H6; -.
DR SMR; Q3U4H6; -.
DR STRING; 10090.ENSMUSP00000101723; -.
DR CAZy; GH20; Glycoside Hydrolase Family 20.
DR iPTMnet; Q3U4H6; -.
DR PhosphoSitePlus; Q3U4H6; -.
DR MaxQB; Q3U4H6; -.
DR PaxDb; Q3U4H6; -.
DR PRIDE; Q3U4H6; -.
DR ProteomicsDB; 269702; -. [Q3U4H6-1]
DR ProteomicsDB; 269703; -. [Q3U4H6-2]
DR Antibodypedia; 10115; 80 antibodies from 18 providers.
DR DNASU; 238023; -.
DR Ensembl; ENSMUST00000038831; ENSMUSP00000048479; ENSMUSG00000039307. [Q3U4H6-2]
DR Ensembl; ENSMUST00000106117; ENSMUSP00000101723; ENSMUSG00000039307. [Q3U4H6-1]
DR GeneID; 238023; -.
DR KEGG; mmu:238023; -.
DR UCSC; uc007mvl.2; mouse. [Q3U4H6-1]
DR UCSC; uc007mvm.2; mouse. [Q3U4H6-2]
DR CTD; 238023; -.
DR MGI; MGI:3605542; Hexdc.
DR VEuPathDB; HostDB:ENSMUSG00000039307; -.
DR eggNOG; ENOG502QRCP; Eukaryota.
DR GeneTree; ENSGT00390000014852; -.
DR InParanoid; Q3U4H6; -.
DR OMA; DEAYHVA; -.
DR OrthoDB; 1021041at2759; -.
DR TreeFam; TF314313; -.
DR BRENDA; 3.2.1.52; 3474.
DR SABIO-RK; Q3U4H6; -.
DR BioGRID-ORCS; 238023; 2 hits in 73 CRISPR screens.
DR PRO; PR:Q3U4H6; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q3U4H6; protein.
DR Bgee; ENSMUSG00000039307; Expressed in animal zygote and 234 other tissues.
DR ExpressionAtlas; Q3U4H6; baseline and differential.
DR Genevisible; Q3U4H6; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:1903561; C:extracellular vesicle; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0004563; F:beta-N-acetylhexosaminidase activity; IDA:MGI.
DR GO; GO:0015929; F:hexosaminidase activity; ISS:MGI.
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 InterPro; IPR015883; Glyco_hydro_20_cat.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR038901; HEXDC-like.
DR PANTHER; PTHR21040; PTHR21040; 1.
DR Pfam; PF00728; Glyco_hydro_20; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Disulfide bond; Glycosidase; Hydrolase;
KW Nucleus; Reference proteome.
FT CHAIN 1..486
FT /note="Hexosaminidase D"
FT /id="PRO_0000316791"
FT REGION 467..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 149
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT VAR_SEQ 328
FT /note="G -> GALDYSASEPGHLYMDCVVRPGAPADCAATTFHMFTGKQPPGLAGAP
FT QDAVPFAHSTQRSGVLSEHFCLWTVSG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:19040401"
FT /id="VSP_030778"
SQ SEQUENCE 486 AA; 54576 MW; 8F8EFEB55BB0350F CRC64;
MSSPTPFKMR LVHLDLKGAP PKVSYLSEVF PLFHALGANG LLIEYEDMFP YEGHLRLLRA
KHAYSPSEVT EILRLARLSE LEVIPLVQTF GHMEFVLKHA AFAHLREVAL FPNTLNPHEA
ESLALVQAMI DQILELHRDV RWLHIGCDEV YYLGEGETSK QWLQQEQNSH AKLCLSHMQA
VASHVLTQHP GVTPLVWDDM LRDIPQEQLK ASGVPQLVEP VLWDYGADLD VHGKVFLIGK
YQECGFQRLW AASAFKGATG ASQALPPVEH HIRNHELWLQ VAGSGPKDAL QGIILTGWQR
YDHFSVLCEL LPVGIPSLAA CLQSLVHGGF AEDVRLRAER FLGVSSLEIA DTVSEGAGSF
PGSDIHALVT QISLHLRSSV DTLLERNRYV TGWFSPYHRR RKLVHPVMIQ HIQPEALSLL
SRWNNLVQQL EVALQPVFYP DTIEEWLEEN VLPSLQRLQD LLQDLGEAAA RQPPPTSPGW
DTGQNP
