NAGAB_BOSIN
ID NAGAB_BOSIN Reviewed; 12 AA.
AC P83127;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 29-SEP-2021, entry version 36.
DE RecName: Full=Alpha-N-acetylgalactosaminidase;
DE EC=3.2.1.49;
DE AltName: Full=Alpha-galactosidase B;
DE Flags: Fragment;
GN Name=NAGA;
OS Bos indicus (Zebu).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9915;
RN [1]
RP PROTEIN SEQUENCE, TISSUE SPECIFICITY, AND GLYCOSYLATION.
RC TISSUE=Fetal cotyledon;
RX PubMed=12405451; DOI=10.1051/rnd:2002021;
RA Sousa N.M., Remy B., El Amiri B., De Figueiredo J.R., Banga-Mboko H.,
RA Dias Goncalves P.B., Beckers J.-F.M.P.;
RT "Characterization of pregnancy-associated glycoproteins extracted from zebu
RT (Bos indicus) placentas removed at different gestational periods.";
RL Reprod. Nutr. Dev. 42:227-241(2002).
CC -!- FUNCTION: Removes terminal alpha-N-acetylgalactosamine residues from
CC glycolipids and glycopeptides. Required for the breakdown of
CC glycolipids. {ECO:0000250|UniProtKB:P17050}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of non-reducing alpha-(1->3)-N-acetylgalactosamine
CC residues from human blood group A and AB mucin glycoproteins,
CC Forssman hapten and blood group A lacto series glycolipids.;
CC EC=3.2.1.49;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a neolactoside IV(3)-alpha-GalNAc,IV(2)-alpha-Fuc-
CC nLc4Cer(d18:1(4E)) + H2O = a neolactoside IV(2)-alpha-Fuc-
CC nLc4Cer(d18:1(4E)) + N-acetyl-alpha-D-galactosamine;
CC Xref=Rhea:RHEA:48212, ChEBI:CHEBI:15377, ChEBI:CHEBI:28471,
CC ChEBI:CHEBI:28691, ChEBI:CHEBI:40356;
CC Evidence={ECO:0000250|UniProtKB:P17050};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48213;
CC Evidence={ECO:0000250|UniProtKB:P17050};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a neolactoside IV(3)-alpha-GalNAc,IV(2)-alpha-Fuc-
CC nLc4Cer(d18:0) + H2O = a neolactoside IV(2)-alpha-Fuc-nLc4Cer(d18:0)
CC + N-acetyl-alpha-D-galactosamine; Xref=Rhea:RHEA:49304,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:40356, ChEBI:CHEBI:91118,
CC ChEBI:CHEBI:91119; Evidence={ECO:0000250|UniProtKB:P17050};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49305;
CC Evidence={ECO:0000250|UniProtKB:P17050};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=globoside IV3GalNAc-Gb4Cer + H2O = globoside Gb4Cer + N-
CC acetyl-alpha-D-galactosamine; Xref=Rhea:RHEA:48412,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:40356, ChEBI:CHEBI:88167,
CC ChEBI:CHEBI:90400; Evidence={ECO:0000250|UniProtKB:P17050};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48413;
CC Evidence={ECO:0000250|UniProtKB:P17050};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P17050}.
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:P17050}.
CC -!- TISSUE SPECIFICITY: Placenta. {ECO:0000269|PubMed:12405451}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:12405451}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 27 family. {ECO:0000305}.
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DR Proteomes; UP000515132; Genome assembly.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0008456; F:alpha-N-acetylgalactosaminidase activity; ISS:UniProtKB.
DR GO; GO:0016052; P:carbohydrate catabolic process; ISS:UniProtKB.
DR GO; GO:0019377; P:glycolipid catabolic process; ISS:UniProtKB.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glycoprotein; Glycosidase; Hydrolase;
KW Lipid metabolism; Lysosome; Reference proteome.
FT CHAIN 1..>12
FT /note="Alpha-N-acetylgalactosaminidase"
FT /id="PRO_0000134872"
FT NON_TER 12
SQ SEQUENCE 12 AA; 1325 MW; 53B124381F240727 CRC64;
LENGLLRKPP MG
