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Database: UniProt/SWISS-PROT
Entry: GALT9_MACFA
LinkDB: GALT9_MACFA
Original site: GALT9_MACFA 
ID   GALT9_MACFA             Reviewed;         606 AA.
AC   Q9GM01;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   16-JAN-2019, entry version 83.
DE   RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 9;
DE            EC=2.4.1.41 {ECO:0000250|UniProtKB:Q9HCQ5};
DE   AltName: Full=Polypeptide GalNAc transferase 9;
DE            Short=GalNAc-T9;
DE            Short=pp-GaNTase 9;
DE   AltName: Full=Protein-UDP acetylgalactosaminyltransferase 9;
DE   AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 9;
GN   Name=GALNT9; ORFNames=QnpA-13140;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Parietal cortex;
RA   Osada N., Hida M., Kusuda J., Tanuma R., Iseki K., Hirai M., Terao K.,
RA   Suzuki Y., Sugano S., Hashimoto K.;
RT   "Isolation of full-length cDNA clones from macaque brain cDNA
RT   libraries.";
RL   Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the initial reaction in O-linked
CC       oligosaccharide biosynthesis, the transfer of an N-acetyl-D-
CC       galactosamine residue to a serine or threonine residue on the
CC       protein receptor. Does not glycosylate apomucin or SDC3.
CC       {ECO:0000250|UniProtKB:Q9HCQ5}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-seryl-[protein] + UDP-N-acetyl-alpha-D-galactosamine =
CC         3-O-[N-acetyl-alpha-D-galactosaminyl]-L-seryl-[protein] + H(+) +
CC         UDP; Xref=Rhea:RHEA:23956, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:12788, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999,
CC         ChEBI:CHEBI:53604, ChEBI:CHEBI:58223, ChEBI:CHEBI:67138;
CC         EC=2.4.1.41; Evidence={ECO:0000250|UniProtKB:Q9HCQ5};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-threonyl-[protein] + UDP-N-acetyl-alpha-D-galactosamine
CC         = 3-O-[N-acetyl-alpha-D-galactosaminyl]-L-threonyl-[protein] +
CC         H(+) + UDP; Xref=Rhea:RHEA:52424, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11689, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:67138, ChEBI:CHEBI:87075;
CC         EC=2.4.1.41; Evidence={ECO:0000250|UniProtKB:Q9HCQ5};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000250|UniProtKB:Q9HCQ5}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250};
CC       Single-pass type II membrane protein {ECO:0000250}.
CC   -!- DOMAIN: There are two conserved domains in the glycosyltransferase
CC       region: the N-terminal domain (domain A, also called GT1 motif),
CC       which is probably involved in manganese coordination and substrate
CC       binding and the C-terminal domain (domain B, also called
CC       Gal/GalNAc-T motif), which is probably involved in catalytic
CC       reaction and UDP-Gal binding. {ECO:0000250}.
CC   -!- DOMAIN: The ricin B-type lectin domain binds to GalNAc and
CC       contributes to the glycopeptide specificity. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. GalNAc-T
CC       subfamily. {ECO:0000305}.
DR   EMBL; AB050509; BAB17277.1; -; mRNA.
DR   RefSeq; NP_001306356.1; NM_001319427.1.
DR   UniGene; Mfa.1709; -.
DR   ProteinModelPortal; Q9GM01; -.
DR   SMR; Q9GM01; -.
DR   CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR   CAZy; GT27; Glycosyltransferase Family 27.
DR   GeneID; 102117136; -.
DR   KEGG; mcf:102117136; -.
DR   CTD; 50614; -.
DR   HOVERGEN; HBG051699; -.
DR   KO; K00710; -.
DR   UniPathway; UPA00378; -.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004653; F:polypeptide N-acetylgalactosaminyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   CDD; cd00161; RICIN; 1.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR001173; Glyco_trans_2-like.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR035992; Ricin_B-like_lectins.
DR   InterPro; IPR000772; Ricin_B_lectin.
DR   InterPro; IPR001202; WW_dom.
DR   Pfam; PF00535; Glycos_transf_2; 1.
DR   Pfam; PF00652; Ricin_B_lectin; 1.
DR   SMART; SM00458; RICIN; 1.
DR   SUPFAM; SSF50370; SSF50370; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
DR   PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW   Lectin; Manganese; Membrane; Metal-binding; Signal-anchor;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN         1    606       Polypeptide N-
FT                                acetylgalactosaminyltransferase 9.
FT                                /FTId=PRO_0000059121.
FT   TOPO_DOM      1      6       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM      7     29       Helical; Signal-anchor for type II
FT                                membrane protein.
FT   TOPO_DOM     30    606       Lumenal. {ECO:0000255}.
FT   DOMAIN      467    603       Ricin B-type lectin.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00174}.
FT   REGION      153    264       Catalytic subdomain A.
FT   REGION      321    383       Catalytic subdomain B.
FT   METAL       248    248       Manganese. {ECO:0000250}.
FT   METAL       250    250       Manganese. {ECO:0000250}.
FT   METAL       380    380       Manganese. {ECO:0000250}.
FT   BINDING     194    194       Substrate. {ECO:0000250}.
FT   BINDING     225    225       Substrate. {ECO:0000250}.
FT   BINDING     383    383       Substrate. {ECO:0000250}.
FT   BINDING     388    388       Substrate. {ECO:0000250}.
FT   CARBOHYD    463    463       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    144    375       {ECO:0000255|PROSITE-ProRule:PRU00174}.
FT   DISULFID    366    445       {ECO:0000255|PROSITE-ProRule:PRU00174}.
FT   DISULFID    480    496       {ECO:0000255|PROSITE-ProRule:PRU00174}.
FT   DISULFID    528    543       {ECO:0000255|PROSITE-ProRule:PRU00174}.
FT   DISULFID    570    590       {ECO:0000255|PROSITE-ProRule:PRU00174}.
SQ   SEQUENCE   606 AA;  68318 MW;  A00A97C02BD3BBBD CRC64;
     MAVARKIRTL LTVNILVFVG IVLFSVYCRL QGRSQELVRP LSGGCRPRPA TPAPGSPLRS
     GGPRAVVAGR AELVLKGQLP AEPCSPGRLM VPEAEAEAQG GLAATLRDDG QEAEGKYEEY
     GYNAQLSDRI SLDRSIPDYR PRKCRHMSYA QDLPQVSVVF IFVNEALSVI LRSVHSVVNH
     TPSQLLKEVI LVDDNSDNVE LKFNLDQYVN KRYPGLVKIV RNSRREGLIR ARLQGWKAAT
     APVVGFFDAH VEFNTGWAEP ALSRIREDRR RIVLPAIDNI KYSTFEVQQY ANAAHGYNWG
     LWCMYIIPPQ DWLDRGDESA PIRTPAMIGC SFVVDREYFG DIGLLDPGME VYGGENVELG
     MRVWQCGGSM EVLPCSRVAH IERTRKPYNN DIDYYAKRNA LRAAEVWMDD FKSHVYMAWN
     IPMTNPGVDF GDVSERLALR QRLKCRSFKW YLENVYPEMR IYNNTLTYGE VRNSKASGYC
     LDQGAEDGDR AILYPCHGMS SQLVRYSADG LLQLGPLGST AFLPDSKCLV DDGRGRTPTL
     RKCEDVARPT QRLWDFTQSG PIVSRATGRC LEVEMSKDAN FGLRLVVQRC SGQKWMIRNW
     IKHARH
//
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