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 03-AUG-2022, entry version 159.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE 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 project:
RT 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., Kubota T.,
RA Cheng L., Inaba N., Gotoh M., Togayachi A., Guo J.-M., Hisatomi H.,
RA Nakajima K., Nishihara S., Nakamura M., Marth J.D., Narimatsu H.;
RT "Cloning and characterization of a new human UDP-N-acetyl-alpha-D-
RT galactosamine:polypeptide N-acetylgalactosaminyltransferase, designated pp-
RT GalNAc-T13, that is specifically expressed in neurons and synthesizes
RT GalNAc alpha-serine/threonine antigen.";
RL J. Biol. Chem. 278:573-584(2003).
CC -!- FUNCTION: Catalyzes the initial reaction in O-linked oligosaccharide
CC biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a
CC serine or threonine residue on the protein receptor. Does not
CC glycosylate apomucin or SDC3. {ECO:0000269|PubMed:10978536,
CC ECO:0000269|PubMed:12407114}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-seryl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-O-
CC [N-acetyl-alpha-D-galactosaminyl]-L-seryl-[protein] + H(+) + UDP;
CC Xref=Rhea:RHEA:23956, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:12788,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:53604,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:67138; EC=2.4.1.41;
CC Evidence={ECO:0000269|PubMed:12407114};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-threonyl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-
CC O-[N-acetyl-alpha-D-galactosaminyl]-L-threonyl-[protein] + H(+) +
CC UDP; Xref=Rhea:RHEA:52424, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11689, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:67138, ChEBI:CHEBI:87075; EC=2.4.1.41;
CC 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}; Single-
CC 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 in
CC heart, placenta, lung, liver, skeletal muscle, kidney, pancreas,
CC spleen, thymus, prostate, testis, ovary, small intestine, colon and
CC leukocyte. In brain, it is expressed in cerebellum, frontal lobe,
CC temporal lobe, putamen and spinal cord, weakly expressed in cerebral
CC cortex. Not expressed in medulla and occipital pole.
CC {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), which
CC is probably involved in manganese coordination and substrate binding
CC and the C-terminal domain (domain B, also called Gal/GalNAc-T motif),
CC which is probably involved in catalytic reaction and UDP-Gal binding.
CC {ECO:0000250}.
CC -!- DOMAIN: The ricin B-type lectin domain binds to GalNAc and contributes
CC 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";
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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 AlphaFoldDB; Q9HCQ5; -.
DR SMR; Q9HCQ5; -.
DR BioGRID; 119094; 53.
DR IntAct; Q9HCQ5; 1.
DR STRING; 9606.ENSP00000380488; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR CAZy; GT27; Glycosyltransferase Family 27.
DR GlyGen; Q9HCQ5; 1 site.
DR iPTMnet; Q9HCQ5; -.
DR PhosphoSitePlus; Q9HCQ5; -.
DR BioMuta; GALNT9; -.
DR DMDM; 143811393; -.
DR MassIVE; Q9HCQ5; -.
DR PaxDb; Q9HCQ5; -.
DR PeptideAtlas; Q9HCQ5; -.
DR PRIDE; Q9HCQ5; -.
DR ProteomicsDB; 81785; -. [Q9HCQ5-1]
DR ProteomicsDB; 81786; -. [Q9HCQ5-2]
DR Antibodypedia; 32061; 148 antibodies from 21 providers.
DR DNASU; 50614; -.
DR Ensembl; ENST00000397325.6; ENSP00000380488.2; ENSG00000182870.13. [Q9HCQ5-2]
DR Ensembl; ENST00000541995.5; ENSP00000440544.1; ENSG00000182870.13. [Q9HCQ5-2]
DR Ensembl; ENST00000671997.1; ENSP00000500654.1; ENSG00000288490.1. [Q9HCQ5-2]
DR Ensembl; ENST00000673376.1; ENSP00000500593.1; ENSG00000288490.1. [Q9HCQ5-2]
DR GeneID; 50614; -.
DR KEGG; hsa:50614; -.
DR UCSC; uc001uka.3; human. [Q9HCQ5-1]
DR CTD; 50614; -.
DR DisGeNET; 50614; -.
DR GeneCards; GALNT9; -.
DR HGNC; HGNC:4131; GALNT9.
DR HPA; ENSG00000182870; Tissue enhanced (brain, thyroid gland).
DR MIM; 606251; gene.
DR neXtProt; NX_Q9HCQ5; -.
DR OpenTargets; ENSG00000182870; -.
DR PharmGKB; PA28544; -.
DR VEuPathDB; HostDB:ENSG00000182870; -.
DR eggNOG; KOG3736; Eukaryota.
DR GeneTree; ENSGT00940000156599; -.
DR HOGENOM; CLU_013477_2_2_1; -.
DR InParanoid; Q9HCQ5; -.
DR OMA; QYVHRRY; -.
DR OrthoDB; 273006at2759; -.
DR PhylomeDB; Q9HCQ5; -.
DR TreeFam; TF313267; -.
DR BRENDA; 2.4.1.41; 2681.
DR PathwayCommons; Q9HCQ5; -.
DR Reactome; R-HSA-913709; O-linked glycosylation of mucins.
DR SignaLink; Q9HCQ5; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 50614; 14 hits in 1063 CRISPR screens.
DR ChiTaRS; GALNT9; human.
DR GenomeRNAi; 50614; -.
DR Pharos; Q9HCQ5; Tbio.
DR PRO; PR:Q9HCQ5; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9HCQ5; protein.
DR Bgee; ENSG00000182870; Expressed in right hemisphere of cerebellum and 88 other tissues.
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; IBA:GO_Central.
DR GO; GO:0016266; P:O-glycan processing; TAS:Reactome.
DR GO; GO:0006493; P:protein O-linked glycosylation; IBA:GO_Central.
DR CDD; cd02510; pp-GalNAc-T; 1.
DR CDD; cd00161; RICIN; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR045885; GalNAc-T.
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 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; Disulfide bond; Glycoprotein; Glycosyltransferase;
KW Golgi apparatus; Lectin; Manganese; Membrane; Metal-binding;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..603
FT /note="Polypeptide N-acetylgalactosaminyltransferase 9"
FT /id="PRO_0000059120"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..29
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..603
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 464..600
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REGION 150..261
FT /note="Catalytic subdomain A"
FT REGION 318..380
FT /note="Catalytic subdomain B"
FT BINDING 191
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 222
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 245
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 247
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 377
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 380
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 385
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 460
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 141..372
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 363..442
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 477..493
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 525..540
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 567..587
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT VAR_SEQ 1..366
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_011206"
FT CONFLICT 539
FT /note="K -> R (in Ref. 1; BAB13699)"
FT /evidence="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
