NAGAB_RAT
ID NAGAB_RAT Reviewed; 415 AA.
AC Q66H12;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Alpha-N-acetylgalactosaminidase;
DE EC=3.2.1.49;
DE AltName: Full=Alpha-galactosidase B;
DE Flags: Precursor;
GN Name=Naga;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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: 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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 27 family. {ECO:0000305}.
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DR EMBL; BC082084; AAH82084.1; -; mRNA.
DR RefSeq; NP_001012120.1; NM_001012120.1.
DR RefSeq; XP_006242149.1; XM_006242087.3.
DR RefSeq; XP_006242150.1; XM_006242088.3.
DR AlphaFoldDB; Q66H12; -.
DR SMR; Q66H12; -.
DR IntAct; Q66H12; 1.
DR STRING; 10116.ENSRNOP00000060590; -.
DR CAZy; GH27; Glycoside Hydrolase Family 27.
DR GlyGen; Q66H12; 4 sites.
DR jPOST; Q66H12; -.
DR PaxDb; Q66H12; -.
DR PRIDE; Q66H12; -.
DR Ensembl; ENSRNOT00000068020; ENSRNOP00000060590; ENSRNOG00000008064.
DR GeneID; 315165; -.
DR KEGG; rno:315165; -.
DR UCSC; RGD:1306025; rat.
DR CTD; 4668; -.
DR RGD; 1306025; Naga.
DR eggNOG; KOG2366; Eukaryota.
DR GeneTree; ENSGT00390000008751; -.
DR HOGENOM; CLU_013093_0_0_1; -.
DR InParanoid; Q66H12; -.
DR OMA; NAFGCDI; -.
DR OrthoDB; 964130at2759; -.
DR PhylomeDB; Q66H12; -.
DR TreeFam; TF312909; -.
DR PRO; PR:Q66H12; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000008064; Expressed in jejunum and 20 other tissues.
DR Genevisible; Q66H12; RN.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0004557; F:alpha-galactosidase activity; IBA:GO_Central.
DR GO; GO:0008456; F:alpha-N-acetylgalactosaminidase activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0016052; P:carbohydrate catabolic process; ISS:UniProtKB.
DR GO; GO:0019377; P:glycolipid catabolic process; ISS:UniProtKB.
DR GO; GO:0016139; P:glycoside catabolic process; IBA:GO_Central.
DR GO; GO:0046477; P:glycosylceramide catabolic process; IBA:GO_Central.
DR GO; GO:0009311; P:oligosaccharide metabolic process; IBA:GO_Central.
DR CDD; cd14792; GH27; 1.
DR Gene3D; 2.60.40.1180; -; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR002241; Glyco_hydro_27.
DR InterPro; IPR000111; Glyco_hydro_27/36_CS.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR035373; Melibiase/NAGA_C.
DR PANTHER; PTHR11452; PTHR11452; 1.
DR Pfam; PF16499; Melibiase_2; 1.
DR Pfam; PF17450; Melibiase_2_C; 1.
DR PRINTS; PR00740; GLHYDRLASE27.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS00512; ALPHA_GALACTOSIDASE; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Lipid metabolism;
KW Lysosome; Phosphoprotein; Reference proteome; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000250"
FT CHAIN 18..415
FT /note="Alpha-N-acetylgalactosaminidase"
FT /id="PRO_0000001020"
FT ACT_SITE 156
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 217
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 78..79
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 154
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 188
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 213
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 217
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 322
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17050"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17050"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 385
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 38..80
FT /evidence="ECO:0000250"
FT DISULFID 42..49
FT /evidence="ECO:0000250"
FT DISULFID 127..158
FT /evidence="ECO:0000250"
FT DISULFID 187..209
FT /evidence="ECO:0000250"
SQ SEQUENCE 415 AA; 46871 MW; 57605634B3F74C6E CRC64;
MLQKTVLLLA LVAQVLMLEN GLLRTPPMGW LAWERFRCNI NCEEDPKNCI SERLFMEMAD
RLAQDGWRDL GYVYLNIDDC WIGGRDATGR LIPDPKRFPH GIAFLADYAH SLGLKLGIYE
DMGKMTCMGY PGTTLDKVEL DAATFAEWKV DMLKLDGCYS TPKERAEGYP KMAAALNATG
RPIAFSCSWP AYEGGLPPKV NYTEVAGTCN LWRNYKDIQD SWKSVLSILD WFVKHQDILQ
PVSGPGHWND PDMLLIGNFG LSFDESRAQM ALWTVLAAPL FMSTDLRTIS PQNIDILQNP
LLIKINQDPL GIQGRLIFKS KSHIEVFKRN LSDDASALVF FSRRTDMPYH FHCSLLELNY
PKGSVYEGQN VFTGDIISGL HPETNFTVII NPSGVVMWYL YPVKGLGIYT MMSQL
