ID NAGAB_BOVIN Reviewed; 411 AA.
AC Q58DH9;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 29-MAY-2013, entry version 57.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC Pecora; Bovidae; Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
CC -!- FUNCTION: Removes terminal alpha-N-acetylgalactosamine residues
CC from glycolipids and glycopeptides. Required for the breakdown of
CC glycolipids (By similarity).
CC -!- CATALYTIC ACTIVITY: Cleavage of non-reducing alpha-(1->3)-N-
CC acetylgalactosamine residues from human blood group A and AB mucin
CC glycoproteins, Forssman hapten and blood group A lacto series
CC glycolipids.
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- SUBCELLULAR LOCATION: Lysosome (By similarity).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 27 family.
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DR EMBL; BT021618; AAX46465.1; -; mRNA.
DR IPI; IPI00697359; -.
DR RefSeq; NP_001039814.1; NM_001046349.1.
DR UniGene; Bt.57867; -.
DR ProteinModelPortal; Q58DH9; -.
DR SMR; Q58DH9; 18-402.
DR CAZy; GH27; Glycoside Hydrolase Family 27.
DR PRIDE; Q58DH9; -.
DR GeneID; 533357; -.
DR KEGG; bta:533357; -.
DR CTD; 4668; -.
DR eggNOG; NOG68897; -.
DR HOGENOM; HOG000161224; -.
DR HOVERGEN; HBG001989; -.
DR InParanoid; Q58DH9; -.
DR KO; K01204; -.
DR OrthoDB; EOG4S1T77; -.
DR BioCyc; CATTLE:533357-MONOMER; -.
DR ChEMBL; CHEMBL5079; -.
DR NextBio; 20876014; -.
DR GO; GO:0005737; C:cytoplasm; ISS:RefGenome.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0004557; F:alpha-galactosidase activity; ISS:RefGenome.
DR GO; GO:0008456; F:alpha-N-acetylgalactosaminidase activity; ISS:UniProtKB.
DR GO; GO:0016052; P:carbohydrate catabolic process; ISS:UniProtKB.
DR GO; GO:0016139; P:glycoside catabolic process; ISS:RefGenome.
DR GO; GO:0046477; P:glycosylceramide catabolic process; ISS:RefGenome.
DR GO; GO:0009311; P:oligosaccharide metabolic process; ISS:RefGenome.
DR Gene3D; 2.60.40.1180; -; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR013780; Glyco_hydro_13_b.
DR InterPro; IPR002241; Glyco_hydro_27.
DR InterPro; IPR000111; Glyco_hydro_GHD.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF02065; Melibiase; 1.
DR PRINTS; PR00740; GLHYDRLASE27.
DR SUPFAM; SSF51445; Glyco_hydro_cat; 1.
DR PROSITE; PS00512; ALPHA_GALACTOSIDASE; 1.
PE 2: Evidence at transcript level;
KW Complete proteome; Disulfide bond; Glycoprotein; Glycosidase;
KW Hydrolase; Lysosome; Phosphoprotein; Reference proteome; Signal.
FT SIGNAL 1 17 By similarity.
FT CHAIN 18 411 Alpha-N-acetylgalactosaminidase.
FT /FTId=PRO_0000001017.
FT REGION 78 79 Substrate binding (By similarity).
FT ACT_SITE 156 156 Nucleophile (By similarity).
FT ACT_SITE 217 217 Proton donor (By similarity).
FT BINDING 154 154 Substrate (By similarity).
FT BINDING 188 188 Substrate (By similarity).
FT BINDING 213 213 Substrate (By similarity).
FT BINDING 217 217 Substrate (By similarity).
FT MOD_RES 322 322 Phosphoserine (By similarity).
FT CARBOHYD 124 124 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 177 177 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 201 201 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 359 359 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 385 385 N-linked (GlcNAc...) (Potential).
FT DISULFID 38 80 By similarity.
FT DISULFID 42 49 By similarity.
FT DISULFID 127 158 By similarity.
FT DISULFID 187 209 By similarity.
SQ SEQUENCE 411 AA; 46533 MW; 69039FB69B869144 CRC64;
MLLKTVLLLA LASQVLVLEN GLLRKPPMGW LAWERFRCNI DCSEDPKNCI SEQLFMEMAD
RLAQDGWRDL GYVYLNIDDC WIGGRDAKGN LVPDRKRFPH GIAFLADYAH SLGLKLGIYE
DLGNFTCMGY PGTTLDKVVQ DAQTFAEWKV DMLKLDGCYS TPQERAEGYP KMAAALNATG
RPIAFSCSWP AYEGGLPPKV NYTLLADICN LWRNFDDIQD SWRSVLSVLD WFVTHQDVLQ
PIAGPGHWND PDMLLIGNFG LSFEQAQAQM ALWTVLAAPL FMSTDLRTIS AQNMDILQNP
LMIKINQDPL GIQGRRILKE KSHIEVYLRP LASEASAIVF FSRRMDMPYH YHSSLARLNF
SSSVVYEAQD VYTGDIISGL QDKTNFTVII NPSGVVMWYL YPIRKLEIPQ Q
//
