ID   HEXD_BOVIN              Reviewed;         346 AA.
AC   A6QNR0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 2.
DT   08-NOV-2023, entry version 78.
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 {ECO:0000250|UniProtKB:Q8WVB3};
GN   Synonyms=HEXDC {ECO:0000250|UniProtKB:Q8WVB3};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Colon;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Has hexosaminidase activity. Responsible for the cleavage of
CC       the monosaccharides N-acetylglucosamine (GlcNAc) and N-
CC       acetylgalactosamine (GalNAc) from cellular substrates. Has a preference
CC       for galactosaminide over glucosaminide substrates.
CC       {ECO:0000250|UniProtKB:Q3U4H6, ECO:0000250|UniProtKB:Q8WVB3}.
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:0000250|UniProtKB:Q3U4H6,
CC         ECO:0000250|UniProtKB:Q8WVB3};
CC   -!- ACTIVITY REGULATION: Inhibited by O-(2-acetamido-2-deoxy-D-
CC       glucopyranosylidene)amino N-phenylcarbamate (PUGNAc) (By similarity).
CC       Inhibited by galacto-NAG-thiazoline (By similarity).
CC       {ECO:0000250|UniProtKB:Q3U4H6, ECO:0000250|UniProtKB:Q8WVB3}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250|UniProtKB:Q3U4H6}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q3U4H6}. Nucleus
CC       {ECO:0000250|UniProtKB:Q3U4H6}. Extracellular vesicle
CC       {ECO:0000250|UniProtKB:Q8WVB3}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI48959.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; BC148958; AAI48959.1; ALT_INIT; mRNA.
DR   AlphaFoldDB; A6QNR0; -.
DR   SMR; A6QNR0; -.
DR   STRING; 9913.ENSBTAP00000024186; -.
DR   PaxDb; 9913-ENSBTAP00000024186; -.
DR   eggNOG; ENOG502QRCP; Eukaryota.
DR   InParanoid; A6QNR0; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:1903561; C:extracellular vesicle; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004563; F:beta-N-acetylhexosaminidase activity; ISS:UniProtKB.
DR   GO; GO:0015929; F:hexosaminidase activity; ISS:UniProtKB.
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   CDD; cd06565; GH20_GcnA-like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR015883; Glyco_hydro_20_cat.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR038901; HEXDC-like.
DR   PANTHER; PTHR21040:SF6; HEXOSAMINIDASE D; 1.
DR   PANTHER; PTHR21040; UNCHARACTERIZED; 1.
DR   Pfam; PF00728; Glyco_hydro_20; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Disulfide bond; Glycosidase; Hydrolase; Nucleus;
KW   Reference proteome.
FT   CHAIN           1..346
FT                   /note="Hexosaminidase D"
FT                   /id="PRO_0000316789"
FT   ACT_SITE        141
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   346 AA;  39284 MW;  3C83027219F13081 CRC64;
     MRLVHLDLKG APPKVCYLSE IFPLFRALGA NGILIEYEDM FPYEGHLRLL RAKHAYSPSE
     IKEILHLATL NELEVIPLVQ TFGHMEFVLK HEALAHLREV ARFPNTLNPH KEESLALVTA
     MIDQVMELHP GARWFHVGCD EVYYLGEGET SRQWLQQEPN SKAKLCLSHM EAVASHMRAR
     YPTTTPLMWD DMLRDIPEDQ LSGSRVPQLV EPVLWDYGAD LDLHGKALLV EKYRKSGFSW
     LWAASAFKGA TGVNQSLTPI EHHLRNHLQW LQVAGSVPAD TLRGIILTGW QRYDHFSVLC
     ELLPVGIPSL AVCLQALLHG DFAENVKARV ENFLGISSLE EMSFRR
//