GALT6_HUMAN
ID GALT6_HUMAN Reviewed; 622 AA.
AC Q8NCL4; Q8IYH4; Q9H6G2; Q9UIV5;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 6;
DE EC=2.4.1.41;
DE AltName: Full=Polypeptide GalNAc transferase 6;
DE Short=GalNAc-T6;
DE Short=pp-GaNTase 6;
DE AltName: Full=Protein-UDP acetylgalactosaminyltransferase 6;
DE AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 6;
GN Name=GALNT6;
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], ENZYME ACTIVITY, AND TISSUE SPECIFICITY.
RC TISSUE=Gastric carcinoma;
RX PubMed=10464263; DOI=10.1074/jbc.274.36.25362;
RA Bennett E.P., Hassan H., Mandel U., Hollingsworth M.A., Akisawa N.,
RA Ikematsu Y., Merkx G., Geurts van Kessel A., Olofsson S., Clausen H.;
RT "Cloning and characterization of a close homologue of human UDP-N-acetyl--
RT D-galactosamine:polypeptide N-acetylgalactosaminyltransferase-T3,
RT designated GalNAc-T6. Evidence for genetic but not functional redundancy.";
RL J. Biol. Chem. 274:25362-25370(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney epithelium, and Mammary gland;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymph;
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).
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. May participate in
CC synthesis of oncofetal fibronectin. Has activity toward Muc1a, Muc2,
CC EA2 and fibronectin peptides.
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:10464263};
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:10464263};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- INTERACTION:
CC Q8NCL4; O60333-2: KIF1B; NbExp=3; IntAct=EBI-3907241, EBI-10975473;
CC Q8NCL4; O43933: PEX1; NbExp=3; IntAct=EBI-3907241, EBI-988601;
CC Q8NCL4; O76024: WFS1; NbExp=3; IntAct=EBI-3907241, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in placenta and trachea. Weakly expressed
CC in brain and pancreas. Expressed in fibroblast. Weakly or not expressed
CC in lung, liver, muscle, kidney, spleen, thymus, prostate, testis,
CC ovary, intestine, colon, leukocyte, stomach, thyroid, spinal cord,
CC lymph node, trachea, adrenal gland and bone marrow.
CC {ECO:0000269|PubMed:10464263}.
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 -!- SEQUENCE CAUTION:
CC Sequence=BAB15297.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
CC Note=Polypeptide N-acetylgalactosaminyltransferase 6;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_488";
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DR EMBL; Y08565; CAA69876.1; -; mRNA.
DR EMBL; AK025961; BAB15297.1; ALT_INIT; mRNA.
DR EMBL; AK074658; BAC11118.1; -; mRNA.
DR EMBL; BC035822; AAH35822.2; -; mRNA.
DR CCDS; CCDS8813.1; -.
DR RefSeq; NP_009141.2; NM_007210.3.
DR RefSeq; XP_005268664.1; XM_005268607.1.
DR RefSeq; XP_006719277.1; XM_006719214.2.
DR RefSeq; XP_011536121.1; XM_011537819.2.
DR RefSeq; XP_011536124.1; XM_011537822.2.
DR RefSeq; XP_016874233.1; XM_017018744.1.
DR RefSeq; XP_016874234.1; XM_017018745.1.
DR AlphaFoldDB; Q8NCL4; -.
DR SMR; Q8NCL4; -.
DR BioGRID; 116393; 54.
DR IntAct; Q8NCL4; 28.
DR MINT; Q8NCL4; -.
DR STRING; 9606.ENSP00000444171; -.
DR BindingDB; Q8NCL4; -.
DR ChEMBL; CHEMBL4523400; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR CAZy; GT27; Glycosyltransferase Family 27.
DR GlyGen; Q8NCL4; 2 sites.
DR iPTMnet; Q8NCL4; -.
DR PhosphoSitePlus; Q8NCL4; -.
DR BioMuta; GALNT6; -.
DR DMDM; 51316028; -.
DR EPD; Q8NCL4; -.
DR jPOST; Q8NCL4; -.
DR MassIVE; Q8NCL4; -.
DR MaxQB; Q8NCL4; -.
DR PaxDb; Q8NCL4; -.
DR PeptideAtlas; Q8NCL4; -.
DR PRIDE; Q8NCL4; -.
DR ProteomicsDB; 72903; -.
DR Antibodypedia; 14380; 201 antibodies from 22 providers.
DR DNASU; 11226; -.
DR Ensembl; ENST00000356317.8; ENSP00000348668.2; ENSG00000139629.16.
DR Ensembl; ENST00000543196.6; ENSP00000444171.1; ENSG00000139629.16.
DR GeneID; 11226; -.
DR KEGG; hsa:11226; -.
DR MANE-Select; ENST00000356317.8; ENSP00000348668.2; NM_007210.4; NP_009141.2.
DR UCSC; uc001ryk.3; human.
DR CTD; 11226; -.
DR DisGeNET; 11226; -.
DR GeneCards; GALNT6; -.
DR HGNC; HGNC:4128; GALNT6.
DR HPA; ENSG00000139629; Tissue enhanced (stomach).
DR MIM; 605148; gene.
DR neXtProt; NX_Q8NCL4; -.
DR OpenTargets; ENSG00000139629; -.
DR PharmGKB; PA28541; -.
DR VEuPathDB; HostDB:ENSG00000139629; -.
DR eggNOG; KOG3736; Eukaryota.
DR GeneTree; ENSGT00940000160845; -.
DR HOGENOM; CLU_013477_0_3_1; -.
DR InParanoid; Q8NCL4; -.
DR OMA; QRELRHN; -.
DR OrthoDB; 606683at2759; -.
DR PhylomeDB; Q8NCL4; -.
DR TreeFam; TF313267; -.
DR BRENDA; 2.4.1.41; 2681.
DR PathwayCommons; Q8NCL4; -.
DR Reactome; R-HSA-913709; O-linked glycosylation of mucins.
DR SignaLink; Q8NCL4; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 11226; 10 hits in 1080 CRISPR screens.
DR ChiTaRS; GALNT6; human.
DR GeneWiki; GALNT6; -.
DR GenomeRNAi; 11226; -.
DR Pharos; Q8NCL4; Tbio.
DR PRO; PR:Q8NCL4; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q8NCL4; protein.
DR Bgee; ENSG00000139629; Expressed in parotid gland and 156 other tissues.
DR ExpressionAtlas; Q8NCL4; baseline and differential.
DR Genevisible; Q8NCL4; HS.
DR GO; GO:0005794; C:Golgi apparatus; IDA:BHF-UCL.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
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 Disulfide bond; Glycoprotein; Glycosyltransferase; Golgi apparatus; Lectin;
KW Manganese; Membrane; Metal-binding; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..622
FT /note="Polypeptide N-acetylgalactosaminyltransferase 6"
FT /id="PRO_0000059114"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..28
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..622
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 496..622
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REGION 176..285
FT /note="Catalytic subdomain A"
FT REGION 348..410
FT /note="Catalytic subdomain B"
FT BINDING 217
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 246
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 269
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 271
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 379
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 407
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 410
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 476
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 165..402
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 393..474
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 509..527
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 553..566
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 597..610
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT VARIANT 423
FT /note="V -> I (in dbSNP:rs747300)"
FT /id="VAR_019580"
FT CONFLICT 362
FT /note="S -> P (in Ref. 1; CAA69876)"
FT /evidence="ECO:0000305"
FT CONFLICT 454
FT /note="A -> T (in Ref. 2; BAC11118)"
FT /evidence="ECO:0000305"
FT CONFLICT 551
FT /note="Q -> R (in Ref. 2; BAC11118)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 622 AA; 71159 MW; 38E63FF2AFB486EF CRC64;
MRLLRRRHMP LRLAMVGCAF VLFLFLLHRD VSSREEATEK PWLKSLVSRK DHVLDLMLEA
MNNLRDSMPK LQIRAPEAQQ TLFSINQSCL PGFYTPAELK PFWERPPQDP NAPGADGKAF
QKSKWTPLET QEKEEGYKKH CFNAFASDRI SLQRSLGPDT RPPECVDQKF RRCPPLATTS
VIIVFHNEAW STLLRTVYSV LHTTPAILLK EIILVDDAST EEHLKEKLEQ YVKQLQVVRV
VRQEERKGLI TARLLGASVA QAEVLTFLDA HCECFHGWLE PLLARIAEDK TVVVSPDIVT
IDLNTFEFAK PVQRGRVHSR GNFDWSLTFG WETLPPHEKQ RRKDETYPIK SPTFAGGLFS
ISKSYFEHIG TYDNQMEIWG GENVEMSFRV WQCGGQLEII PCSVVGHVFR TKSPHTFPKG
TSVIARNQVR LAEVWMDSYK KIFYRRNLQA AKMAQEKSFG DISERLQLRE QLHCHNFSWY
LHNVYPEMFV PDLTPTFYGA IKNLGTNQCL DVGENNRGGK PLIMYSCHGL GGNQYFEYTT
QRDLRHNIAK QLCLHVSKGA LGLGSCHFTG KNSQVPKDEE WELAQDQLIR NSGSGTCLTS
QDKKPAMAPC NPSDPHQLWL FV
