HEXD_BOVIN
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 03-AUG-2022, entry version 74.
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; A6QNR0; -.
DR PRIDE; A6QNR0; -.
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 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 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
