B3GN6_HUMAN
ID B3GN6_HUMAN Reviewed; 384 AA.
AC Q6ZMB0; E9PKS1; Q6ZSC5; Q8TAZ4; Q8TDX1;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Acetylgalactosaminyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase;
DE EC=2.4.1.147 {ECO:0000269|PubMed:7655172};
DE AltName: Full=Core 3 synthase;
DE AltName: Full=UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 6;
DE Short=BGnT-6;
DE Short=Beta-1,3-Gn-T6;
DE Short=Beta-1,3-N-acetylglucosaminyltransferase 6;
DE Short=Beta3Gn-T6;
GN Name=B3GNT6;
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).
RX PubMed=11821425; DOI=10.1074/jbc.m112457200;
RA Iwai T., Inaba N., Naundorf A., Zhang Y., Gotoh M., Iwasaki H., Kudo T.,
RA Togayachi A., Ishizuka Y., Nakanishi H., Narimatsu H.;
RT "Molecular cloning and characterization of a novel UDP-GlcNAc:GalNAc-
RT peptide beta1,3-N-acetylglucosaminyltransferase (beta 3Gn-T6), an enzyme
RT synthesizing the core 3 structure of O-glycans.";
RL J. Biol. Chem. 277:12802-12809(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Ileal mucosa;
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 GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Pancreas;
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 [5]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE
RP SPECIFICITY.
RX PubMed=7655172; DOI=10.1093/glycob/5.3.351;
RA Vavasseur F., Yang J.M., Dole K., Paulsen H., Brockhausen I.;
RT "Synthesis of O-glycan core 3: characterization of UDP-GlcNAc: GalNAc-R
RT beta 3-N-acetyl-glucosaminyltransferase activity from colonic mucosal
RT tissues and lack of the activity in human cancer cell lines.";
RL Glycobiology 5:351-357(1995).
RN [6]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15755813; DOI=10.1073/pnas.0407983102;
RA Iwai T., Kudo T., Kawamoto R., Kubota T., Togayachi A., Hiruma T.,
RA Okada T., Kawamoto T., Morozumi K., Narimatsu H.;
RT "Core 3 synthase is down-regulated in colon carcinoma and profoundly
RT suppresses the metastatic potential of carcinoma cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:4572-4577(2005).
CC -!- FUNCTION: Beta-1,3-N-acetylglucosaminyltransferase that synthesizes the
CC core 3 structure of the O-glycan, an important precursor in the
CC biosynthesis of mucin-type glycoproteins. Plays an important role in
CC the synthesis of mucin-type O-glycans in digestive organs.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-[N-acetyl-alpha-D-galactosaminyl]-L-threonyl-[protein] +
CC UDP-N-acetyl-alpha-D-glucosamine = 3-O-[N-acetyl-beta-D-glucosaminyl-
CC (1->3)-N-acetyl-alpha-D-galactosaminyl]-L-threonyl-[protein] + H(+) +
CC UDP; Xref=Rhea:RHEA:46880, Rhea:RHEA-COMP:11689, Rhea:RHEA-
CC COMP:11692, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:87075, ChEBI:CHEBI:87080; EC=2.4.1.147;
CC Evidence={ECO:0000269|PubMed:7655172};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-[N-acetyl-alpha-D-galactosaminyl]-L-seryl-[protein] + UDP-
CC N-acetyl-alpha-D-glucosamine = 3-O-[N-acetyl-beta-D-glucosaminyl-
CC (1->3)-N-acetyl-alpha-D-galactosaminyl]-L-seryl-[protein] + H(+) +
CC UDP; Xref=Rhea:RHEA:46884, Rhea:RHEA-COMP:11691, Rhea:RHEA-
CC COMP:12788, ChEBI:CHEBI:15378, ChEBI:CHEBI:53604, ChEBI:CHEBI:57705,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:87079; EC=2.4.1.147;
CC Evidence={ECO:0000269|PubMed:7655172};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.3 mM for GalNAc-alpha-Bn {ECO:0000269|PubMed:7655172};
CC Vmax=4.5 nmol/h/mg enzyme with GalNAc-alpha-Bn as substrate
CC {ECO:0000269|PubMed:7655172};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:15755813}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:15755813}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6ZMB0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6ZMB0-2; Sequence=VSP_025963, VSP_025964;
CC Name=3;
CC IsoId=Q6ZMB0-3; Sequence=VSP_047091;
CC -!- TISSUE SPECIFICITY: Present in stomach and colon (at protein level).
CC Restricted in the stomach, colon and small intestine, where core 3
CC structure is present. {ECO:0000269|PubMed:15755813}.
CC -!- INDUCTION: Down-regulated in gastric and colorectal carcinomas,
CC suggesting that it may be used as a marker for distinguishing between
CC benign adenomas and premalignant lesions (at protein level).
CC -!- MISCELLANEOUS: Injection into nude mice significantly suppress lung
CC metastasis, indicating that the core structures of O-glycans are
CC profoundly involved in the metastatic capacity of cancer cells.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/B3GNT6ID44427ch11q13.html";
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DR EMBL; AB073740; BAB88882.1; -; mRNA.
DR EMBL; AK127544; BAC87028.1; -; mRNA.
DR EMBL; AK172863; BAD18819.1; -; mRNA.
DR EMBL; AP000752; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC025357; AAH25357.1; -; mRNA.
DR EMBL; BC103908; AAI03909.1; -; mRNA.
DR EMBL; BC103909; AAI03910.1; -; mRNA.
DR EMBL; BC103910; AAI03911.1; -; mRNA.
DR CCDS; CCDS53681.1; -. [Q6ZMB0-1]
DR RefSeq; NP_619651.3; NM_138706.4. [Q6ZMB0-1]
DR AlphaFoldDB; Q6ZMB0; -.
DR SMR; Q6ZMB0; -.
DR STRING; 9606.ENSP00000484640; -.
DR ChEMBL; CHEMBL2321631; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR GlyGen; Q6ZMB0; 3 sites.
DR iPTMnet; Q6ZMB0; -.
DR PhosphoSitePlus; Q6ZMB0; -.
DR BioMuta; B3GNT6; -.
DR DMDM; 152033628; -.
DR jPOST; Q6ZMB0; -.
DR MassIVE; Q6ZMB0; -.
DR PaxDb; Q6ZMB0; -.
DR PeptideAtlas; Q6ZMB0; -.
DR PRIDE; Q6ZMB0; -.
DR ProteomicsDB; 21560; -.
DR ProteomicsDB; 67861; -. [Q6ZMB0-1]
DR ProteomicsDB; 67862; -. [Q6ZMB0-2]
DR Antibodypedia; 31219; 102 antibodies from 24 providers.
DR DNASU; 192134; -.
DR Ensembl; ENST00000622824.1; ENSP00000484640.1; ENSG00000198488.10. [Q6ZMB0-1]
DR GeneID; 192134; -.
DR KEGG; hsa:192134; -.
DR MANE-Select; ENST00000622824.1; ENSP00000484640.1; NM_138706.5; NP_619651.3.
DR UCSC; uc031xwa.2; human. [Q6ZMB0-1]
DR CTD; 192134; -.
DR DisGeNET; 192134; -.
DR GeneCards; B3GNT6; -.
DR HGNC; HGNC:24141; B3GNT6.
DR HPA; ENSG00000198488; Group enriched (intestine, salivary gland, stomach).
DR MIM; 615315; gene.
DR neXtProt; NX_Q6ZMB0; -.
DR OpenTargets; ENSG00000198488; -.
DR PharmGKB; PA164741288; -.
DR VEuPathDB; HostDB:ENSG00000198488; -.
DR eggNOG; KOG2287; Eukaryota.
DR GeneTree; ENSGT00940000163174; -.
DR HOGENOM; CLU_036849_5_1_1; -.
DR InParanoid; Q6ZMB0; -.
DR OMA; MWKALHN; -.
DR PhylomeDB; Q6ZMB0; -.
DR TreeFam; TF318639; -.
DR BRENDA; 2.4.1.147; 2681.
DR PathwayCommons; Q6ZMB0; -.
DR Reactome; R-HSA-913709; O-linked glycosylation of mucins.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 192134; 10 hits in 1059 CRISPR screens.
DR GenomeRNAi; 192134; -.
DR Pharos; Q6ZMB0; Tbio.
DR PRO; PR:Q6ZMB0; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q6ZMB0; protein.
DR Bgee; ENSG00000198488; Expressed in rectum and 64 other tissues.
DR ExpressionAtlas; Q6ZMB0; baseline and differential.
DR Genevisible; Q6ZMB0; HS.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; NAS:UniProtKB.
DR GO; GO:0106328; F:acetylgalactosaminyl-O-glycosyl-seryl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0106327; F:acetylgalactosaminyl-O-glycosyl-threonyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0047223; F:beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase activity; NAS:UniProtKB.
DR GO; GO:0008378; F:galactosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0008499; F:UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase activity; TAS:Reactome.
DR GO; GO:0008194; F:UDP-glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0009101; P:glycoprotein biosynthetic process; NAS:UniProtKB.
DR GO; GO:0016266; P:O-glycan processing; TAS:Reactome.
DR GO; GO:0016269; P:O-glycan processing, core 3; NAS:UniProtKB.
DR GO; GO:0030311; P:poly-N-acetyllactosamine biosynthetic process; IBA:GO_Central.
DR InterPro; IPR002659; Glyco_trans_31.
DR PANTHER; PTHR11214; PTHR11214; 1.
DR Pfam; PF01762; Galactosyl_T; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..384
FT /note="Acetylgalactosaminyl-O-glycosyl-glycoprotein beta-
FT 1,3-N-acetylglucosaminyltransferase"
FT /id="PRO_0000289218"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..31
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..384
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 34..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 25..147
FT /note="ALQQWFLQAPRSPREERSPQEETPEGPTDAPAADEPPSELVPGPPCVANASA
FT NATADFEQLPARIQDFLRYRHCRHFPLLWDAPAKCAGGRGVFLLLAVKSAPEHYERREL
FT IRRTWGQERSYG -> VLQRRRLPPVRPHGPGPARGRPPHPALPHRRRLH (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_025963"
FT VAR_SEQ 289..319
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_025964"
FT VAR_SEQ 317..335
FT /note="ERAGLAPSGHEGIRPFGVQ -> GARRPGAQRPRGHPGPSACS (in
FT isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_047091"
FT CONFLICT 164
FT /note="D -> N (in Ref. 2; BAD18819)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="A -> T (in Ref. 4; AAH25357)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 384 AA; 42748 MW; F76C4577D3008429 CRC64;
MAFPCRRSLT AKTLACLLVG VSFLALQQWF LQAPRSPREE RSPQEETPEG PTDAPAADEP
PSELVPGPPC VANASANATA DFEQLPARIQ DFLRYRHCRH FPLLWDAPAK CAGGRGVFLL
LAVKSAPEHY ERRELIRRTW GQERSYGGRP VRRLFLLGTP GPEDEARAER LAELVALEAR
EHGDVLQWAF ADTFLNLTLK HLHLLDWLAA RCPHARFLLS GDDDVFVHTA NVVRFLQAQP
PGRHLFSGQL MEGSVPIRDS WSKYFVPPQL FPGSAYPVYC SGGGFLLSGP TARALRAAAR
HTPLFPIDDA YMGMCLERAG LAPSGHEGIR PFGVQLPGAQ QSSFDPCMYR ELLLVHRFAP
YEMLLMWKAL HSPALSCDRG HRVS
