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Database: UniProt/SWISS-PROT
Entry: GALT9_HUMAN
LinkDB: GALT9_HUMAN
Original site: GALT9_HUMAN 
ID   GALT9_HUMAN             Reviewed;         603 AA.
AC   Q9HCQ5; Q52LR8; Q6NT54; Q8NFR1;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 3.
DT   05-DEC-2018, entry version 141.
DE   RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 9;
DE            EC=2.4.1.41 {ECO:0000269|PubMed:12407114};
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;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Brain;
RX   PubMed=10978536; DOI=10.1016/S0167-4781(00)00180-9;
RA   Toba S., Tenno M., Konishi M., Mikami T., Itoh N., Kurosaka A.;
RT   "Brain-specific expression of a novel human UDP-GalNAc:polypeptide N-
RT   acetylgalactosaminyltransferase (GalNAc-T9).";
RL   Biochim. Biophys. Acta 1493:264-268(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Kidney;
RA   Guo J.H., Zan Q., Yu L.;
RL   Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Colon;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX   PubMed=12407114; DOI=10.1074/jbc.M203094200;
RA   Zhang Y., Iwasaki H., Wang H., Kudo T., Kalka T.B., Hennet T.,
RA   Kubota T., Cheng L., Inaba N., Gotoh M., Togayachi A., Guo J.-M.,
RA   Hisatomi H., Nakajima K., Nishihara S., Nakamura M., Marth J.D.,
RA   Narimatsu H.;
RT   "Cloning and characterization of a new human UDP-N-acetyl-alpha-D-
RT   galactosamine:polypeptide N-acetylgalactosaminyltransferase,
RT   designated pp-GalNAc-T13, that is specifically expressed in neurons
RT   and synthesizes GalNAc alpha-serine/threonine antigen.";
RL   J. Biol. Chem. 278:573-584(2003).
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:0000269|PubMed:10978536, ECO:0000269|PubMed:12407114}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-seryl-[protein] + UDP-N-acetyl-alpha-D-galactosamine =
CC         H(+) + O(3)-[N-acetyl-alpha-D-galactosaminyl]-L-seryl-[protein]
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:0000269|PubMed:12407114};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-threonyl-[protein] + UDP-N-acetyl-alpha-D-galactosamine
CC         = H(+) + O(3)-[N-acetyl-alpha-D-galactosaminyl]-L-threonyl-
CC         [protein] + 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:0000269|PubMed:12407114};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000269|PubMed:12407114}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250};
CC       Single-pass type II membrane protein {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9HCQ5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9HCQ5-2; Sequence=VSP_011206;
CC   -!- TISSUE SPECIFICITY: Specifically expressed in brain. Not expressed
CC       in heart, placenta, lung, liver, skeletal muscle, kidney,
CC       pancreas, spleen, thymus, prostate, testis, ovary, small
CC       intestine, colon and leukocyte. In brain, it is expressed in
CC       cerebellum, frontal lobe, temporal lobe, putamen and spinal cord,
CC       weakly expressed in cerebral cortex. Not expressed in medulla and
CC       occipital pole. {ECO:0000269|PubMed:10978536}.
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}.
CC   -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
CC       Note=Polypeptide N-acetylgalactosaminyltransferase 9;
CC       URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_491";
DR   EMBL; AB040672; BAB13699.2; -; mRNA.
DR   EMBL; AF458594; AAM49722.1; -; mRNA.
DR   EMBL; BC093817; AAH93817.2; -; mRNA.
DR   EMBL; BC093819; AAH93819.2; -; mRNA.
DR   CCDS; CCDS41866.1; -. [Q9HCQ5-2]
DR   CCDS; CCDS81755.1; -. [Q9HCQ5-1]
DR   RefSeq; NP_001116108.1; NM_001122636.1.
DR   RefSeq; NP_068580.2; NM_021808.3. [Q9HCQ5-2]
DR   UniGene; Hs.301062; -.
DR   UniGene; Hs.658249; -.
DR   ProteinModelPortal; Q9HCQ5; -.
DR   SMR; Q9HCQ5; -.
DR   BioGrid; 119094; 2.
DR   IntAct; Q9HCQ5; 1.
DR   STRING; 9606.ENSP00000380488; -.
DR   CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR   CAZy; GT27; Glycosyltransferase Family 27.
DR   iPTMnet; Q9HCQ5; -.
DR   PhosphoSitePlus; Q9HCQ5; -.
DR   BioMuta; GALNT9; -.
DR   DMDM; 143811393; -.
DR   PaxDb; Q9HCQ5; -.
DR   PeptideAtlas; Q9HCQ5; -.
DR   PRIDE; Q9HCQ5; -.
DR   ProteomicsDB; 81785; -.
DR   ProteomicsDB; 81786; -. [Q9HCQ5-2]
DR   DNASU; 50614; -.
DR   Ensembl; ENST00000397325; ENSP00000380488; ENSG00000182870. [Q9HCQ5-2]
DR   Ensembl; ENST00000541995; ENSP00000440544; ENSG00000182870. [Q9HCQ5-2]
DR   GeneID; 50614; -.
DR   KEGG; hsa:50614; -.
DR   UCSC; uc001uka.3; human. [Q9HCQ5-1]
DR   CTD; 50614; -.
DR   DisGeNET; 50614; -.
DR   EuPathDB; HostDB:ENSG00000182870.12; -.
DR   GeneCards; GALNT9; -.
DR   HGNC; HGNC:4131; GALNT9.
DR   HPA; HPA075016; -.
DR   MIM; 606251; gene.
DR   neXtProt; NX_Q9HCQ5; -.
DR   OpenTargets; ENSG00000182870; -.
DR   PharmGKB; PA28544; -.
DR   GeneTree; ENSGT00940000156599; -.
DR   HOGENOM; HOG000038228; -.
DR   HOVERGEN; HBG051699; -.
DR   InParanoid; Q9HCQ5; -.
DR   KO; K00710; -.
DR   PhylomeDB; Q9HCQ5; -.
DR   TreeFam; TF313267; -.
DR   BRENDA; 2.4.1.41; 2681.
DR   Reactome; R-HSA-913709; O-linked glycosylation of mucins.
DR   UniPathway; UPA00378; -.
DR   ChiTaRS; GALNT9; human.
DR   GenomeRNAi; 50614; -.
DR   PRO; PR:Q9HCQ5; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   Bgee; ENSG00000182870; Expressed in 109 organ(s), highest expression level in right hemisphere of cerebellum.
DR   CleanEx; HS_GALNT9; -.
DR   ExpressionAtlas; Q9HCQ5; baseline and differential.
DR   Genevisible; Q9HCQ5; HS.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR   GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
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; TAS:Reactome.
DR   GO; GO:0016266; P:O-glycan processing; TAS:Reactome.
DR   GO; GO:0006493; P:protein O-linked glycosylation; NAS:UniProtKB.
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   1: Evidence at protein level;
KW   Alternative splicing; Complete proteome; Disulfide bond; Glycoprotein;
KW   Glycosyltransferase; Golgi apparatus; Lectin; Manganese; Membrane;
KW   Metal-binding; Reference proteome; Signal-anchor; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    603       Polypeptide N-
FT                                acetylgalactosaminyltransferase 9.
FT                                /FTId=PRO_0000059120.
FT   TOPO_DOM      1      6       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM      7     29       Helical; Signal-anchor for type II
FT                                membrane protein. {ECO:0000255}.
FT   TOPO_DOM     30    603       Lumenal. {ECO:0000255}.
FT   DOMAIN      464    600       Ricin B-type lectin.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00174}.
FT   REGION      150    261       Catalytic subdomain A.
FT   REGION      318    380       Catalytic subdomain B.
FT   METAL       245    245       Manganese. {ECO:0000250}.
FT   METAL       247    247       Manganese. {ECO:0000250}.
FT   METAL       377    377       Manganese. {ECO:0000250}.
FT   BINDING     191    191       Substrate. {ECO:0000250}.
FT   BINDING     222    222       Substrate. {ECO:0000250}.
FT   BINDING     380    380       Substrate. {ECO:0000250}.
FT   BINDING     385    385       Substrate. {ECO:0000250}.
FT   CARBOHYD    460    460       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    141    372       {ECO:0000255|PROSITE-ProRule:PRU00174}.
FT   DISULFID    363    442       {ECO:0000255|PROSITE-ProRule:PRU00174}.
FT   DISULFID    477    493       {ECO:0000255|PROSITE-ProRule:PRU00174}.
FT   DISULFID    525    540       {ECO:0000255|PROSITE-ProRule:PRU00174}.
FT   DISULFID    567    587       {ECO:0000255|PROSITE-ProRule:PRU00174}.
FT   VAR_SEQ       1    366       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|Ref.2}.
FT                                /FTId=VSP_011206.
FT   CONFLICT    539    539       K -> R (in Ref. 1; BAB13699).
FT                                {ECO:0000305}.
SQ   SEQUENCE   603 AA;  68359 MW;  4B5888733D8577CF CRC64;
     MAVARKIRTL LTVNILVFVG IVLFSVYCRL QGRSQELVRI VSGDRRVRSR HAKVGTLGDR
     EAILQRLDHL EEVVYNQLNG LAKPIGLVEG PGGLGQGGLA ATLRDDGQEA EGKYEEYGYN
     AQLSDRISLD RSIPDYRPRK CRQMSYAQDL PQVSVVFIFV NEALSVILRS VHSVVNHTPS
     QLLKEVILVD DNSDNVELKF NLDQYVNKRY PGLVKIVRNS RREGLIRARL QGWKAATAPV
     VGFFDAHVEF NTGWAEPALS RIREDRRRIV LPAIDNIKYS TFEVQQYANA AHGYNWGLRC
     MYIIPPQDWL DRGDESAPIR TPAMIGCSFV VDREYFGDIG LLDPGMEVYG GENVELGMRV
     WQCGGSMEVL PCSRVAHIER TRKPYNNDID YYAKRNALRA AEVWMDDFKS HVYMAWNIPM
     SNPGVDFGDV SERLALRQRL KCRSFKWYLE NVYPEMRVYN NTLTYGEVRN SKASAYCLDQ
     GAEDGDRAIL YPCHGMSSQL VRYSADGLLQ LGPLGSTAFL PDSKCLVDDG TGRMPTLKKC
     EDVARPTQRL WDFTQSGPIV SRATGRCLEV EMSKDANFGL RLVVQRCSGQ KWMIRNWIKH
     ARH
//
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