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Database: UniProt
Entry: Q58DH9
LinkDB: Q58DH9
Original site: Q58DH9 
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-OCT-2014, entry version 66.
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). {ECO:0000250}.
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. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 27 family.
CC       {ECO:0000305}.
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DR   EMBL; BT021618; AAX46465.1; -; mRNA.
DR   RefSeq; NP_001039814.1; NM_001046349.1.
DR   UniGene; Bt.57867; -.
DR   ProteinModelPortal; Q58DH9; -.
DR   SMR; Q58DH9; 18-402.
DR   ChEMBL; CHEMBL5079; -.
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   NextBio; 20876014; -.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-KW.
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.
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; SSF51445; 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       {ECO:0000250}.
FT   CHAIN        18    411       Alpha-N-acetylgalactosaminidase.
FT                                /FTId=PRO_0000001017.
FT   REGION       78     79       Substrate binding. {ECO:0000250}.
FT   ACT_SITE    156    156       Nucleophile. {ECO:0000250}.
FT   ACT_SITE    217    217       Proton donor. {ECO:0000250}.
FT   BINDING     154    154       Substrate. {ECO:0000250}.
FT   BINDING     188    188       Substrate. {ECO:0000250}.
FT   BINDING     213    213       Substrate. {ECO:0000250}.
FT   BINDING     217    217       Substrate. {ECO:0000250}.
FT   MOD_RES     322    322       Phosphoserine. {ECO:0000250}.
FT   CARBOHYD    124    124       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    177    177       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    201    201       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    359    359       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    385    385       N-linked (GlcNAc...). {ECO:0000255}.
FT   DISULFID     38     80       {ECO:0000250}.
FT   DISULFID     42     49       {ECO:0000250}.
FT   DISULFID    127    158       {ECO:0000250}.
FT   DISULFID    187    209       {ECO:0000250}.
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
//
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