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Acetylgalactosaminyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase (EC 2.4.1.147) (Core 3 synthase) (UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 6) (BGnT-6) (Beta-1,3-Gn-T6) (Beta-1,3-N-acetylglucosaminyltransferase 6) (Beta3Gn-T6)

 B3GN6_HUMAN             Reviewed;         384 AA.
Q6ZMB0; E9PKS1; Q6ZSC5; Q8TAZ4; Q8TDX1;
29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
29-MAY-2007, sequence version 2.
27-SEP-2017, entry version 99.
RecName: Full=Acetylgalactosaminyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase;
EC=2.4.1.147 {ECO:0000269|PubMed:7655172};
AltName: Full=Core 3 synthase;
AltName: Full=UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 6;
Short=BGnT-6;
Short=Beta-1,3-Gn-T6;
Short=Beta-1,3-N-acetylglucosaminyltransferase 6;
Short=Beta3Gn-T6;
Name=B3GNT6;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=11821425; DOI=10.1074/jbc.M112457200;
Iwai T., Inaba N., Naundorf A., Zhang Y., Gotoh M., Iwasaki H.,
Kudo T., Togayachi A., Ishizuka Y., Nakanishi H., Narimatsu H.;
"Molecular cloning and characterization of a novel UDP-GlcNAc:GalNAc-
peptide beta1,3-N-acetylglucosaminyltransferase (beta 3Gn-T6), an
enzyme synthesizing the core 3 structure of O-glycans.";
J. Biol. Chem. 277:12802-12809(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Ileal mucosa;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Pancreas;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE
SPECIFICITY.
PubMed=7655172; DOI=10.1093/glycob/5.3.351;
Vavasseur F., Yang J.M., Dole K., Paulsen H., Brockhausen I.;
"Synthesis of O-glycan core 3: characterization of UDP-GlcNAc: GalNAc-
R beta 3-N-acetyl-glucosaminyltransferase activity from colonic
mucosal tissues and lack of the activity in human cancer cell lines.";
Glycobiology 5:351-357(1995).
[6]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=15755813; DOI=10.1073/pnas.0407983102;
Iwai T., Kudo T., Kawamoto R., Kubota T., Togayachi A., Hiruma T.,
Okada T., Kawamoto T., Morozumi K., Narimatsu H.;
"Core 3 synthase is down-regulated in colon carcinoma and profoundly
suppresses the metastatic potential of carcinoma cells.";
Proc. Natl. Acad. Sci. U.S.A. 102:4572-4577(2005).
-!- FUNCTION: Beta-1,3-N-acetylglucosaminyltransferase that
synthesizes the core 3 structure of the O-glycan, an important
precursor in the biosynthesis of mucin-type glycoproteins. Plays
an important role in the synthesis of mucin-type O-glycans in
digestive organs.
-!- CATALYTIC ACTIVITY: UDP-N-acetyl-alpha-D-glucosamine + O(3)-(N-
acetyl-alpha-D-galactosaminyl)-L-threonyl/L-seryl-[protein] = UDP
+ O(3)-(N-acetyl-beta-D-glucosaminyl-(1->3)-N-acetyl-alpha-D-
galactosaminyl)-L-threonyl/L-seryl-[protein].
{ECO:0000269|PubMed:7655172}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=3.3 mM for GalNAc-alpha-Bn {ECO:0000269|PubMed:7655172};
Vmax=4.5 nmol/h/mg enzyme with GalNAc-alpha-Bn as substrate
{ECO:0000269|PubMed:7655172};
-!- PATHWAY: Protein modification; protein glycosylation.
-!- SUBCELLULAR LOCATION: Golgi apparatus membrane
{ECO:0000269|PubMed:15755813}; Single-pass type II membrane
protein {ECO:0000269|PubMed:15755813}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q6ZMB0-1; Sequence=Displayed;
Name=2;
IsoId=Q6ZMB0-2; Sequence=VSP_025963, VSP_025964;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q6ZMB0-3; Sequence=VSP_047091;
Note=Gene prediction based on EST data.;
-!- TISSUE SPECIFICITY: Present in stomach and colon (at protein
level). Restricted in the stomach, colon and small intestine,
where core 3 structure is present. {ECO:0000269|PubMed:15755813}.
-!- INDUCTION: Down-regulated in gastric and colorectal carcinomas,
suggesting that it may be used as a marker for distinguishing
between benign adenomas and premalignant lesions (at protein
level).
-!- MISCELLANEOUS: Injection into nude mice significantly suppress
lung metastasis, indicating that the core structures of O-glycans
are profoundly involved in the metastatic capacity of cancer
cells.
-!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/B3GNT6ID44427ch11q13.html";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AB073740; BAB88882.1; -; mRNA.
EMBL; AK127544; BAC87028.1; -; mRNA.
EMBL; AK172863; BAD18819.1; -; mRNA.
EMBL; AP000752; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC025357; AAH25357.1; -; mRNA.
EMBL; BC103908; AAI03909.1; -; mRNA.
EMBL; BC103909; AAI03910.1; -; mRNA.
EMBL; BC103910; AAI03911.1; -; mRNA.
CCDS; CCDS53681.1; -. [Q6ZMB0-1]
RefSeq; NP_619651.3; NM_138706.4. [Q6ZMB0-1]
UniGene; Hs.352622; -.
ProteinModelPortal; Q6ZMB0; -.
STRING; 9606.ENSP00000435352; -.
ChEMBL; CHEMBL2321631; -.
CAZy; GT31; Glycosyltransferase Family 31.
iPTMnet; Q6ZMB0; -.
PhosphoSitePlus; Q6ZMB0; -.
DMDM; 152033628; -.
PaxDb; Q6ZMB0; -.
PeptideAtlas; Q6ZMB0; -.
PRIDE; Q6ZMB0; -.
DNASU; 192134; -.
Ensembl; ENST00000622824; ENSP00000484640; ENSG00000198488. [Q6ZMB0-1]
GeneID; 192134; -.
KEGG; hsa:192134; -.
UCSC; uc031xwa.2; human. [Q6ZMB0-1]
CTD; 192134; -.
DisGeNET; 192134; -.
EuPathDB; HostDB:ENSG00000198488.10; -.
GeneCards; B3GNT6; -.
H-InvDB; HIX0026120; -.
HGNC; HGNC:24141; B3GNT6.
HPA; HPA012158; -.
HPA; HPA039805; -.
MIM; 615315; gene.
neXtProt; NX_Q6ZMB0; -.
OpenTargets; ENSG00000198488; -.
PharmGKB; PA164741288; -.
eggNOG; KOG2287; Eukaryota.
eggNOG; ENOG410ZZ1B; LUCA.
GeneTree; ENSGT00760000118879; -.
HOGENOM; HOG000232195; -.
HOVERGEN; HBG050653; -.
InParanoid; Q6ZMB0; -.
KO; K00739; -.
OMA; RFAPYEM; -.
OrthoDB; EOG091G0AXM; -.
PhylomeDB; Q6ZMB0; -.
TreeFam; TF318639; -.
BRENDA; 2.4.1.147; 2681.
Reactome; R-HSA-913709; O-linked glycosylation of mucins.
UniPathway; UPA00378; -.
GenomeRNAi; 192134; -.
PRO; PR:Q6ZMB0; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000198488; -.
CleanEx; HS_B3GNT6; -.
ExpressionAtlas; Q6ZMB0; baseline and differential.
Genevisible; Q6ZMB0; HS.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; NAS:UniProtKB.
GO; GO:0047224; F:acetylgalactosaminyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0047223; F:beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase activity; NAS:UniProtKB.
GO; GO:0008378; F:galactosyltransferase activity; IDA:UniProtKB.
GO; GO:0008499; F:UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase activity; TAS:Reactome.
GO; GO:0009101; P:glycoprotein biosynthetic process; NAS:UniProtKB.
GO; GO:0016266; P:O-glycan processing; TAS:Reactome.
GO; GO:0016269; P:O-glycan processing, core 3; NAS:UniProtKB.
InterPro; IPR002659; Glyco_trans_31.
PANTHER; PTHR11214; PTHR11214; 1.
Pfam; PF01762; Galactosyl_T; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Glycoprotein;
Glycosyltransferase; Golgi apparatus; Membrane; Reference proteome;
Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
CHAIN 1 384 Acetylgalactosaminyl-O-glycosyl-
glycoprotein beta-1,3-N-
acetylglucosaminyltransferase.
/FTId=PRO_0000289218.
TOPO_DOM 1 12 Cytoplasmic. {ECO:0000255}.
TRANSMEM 13 31 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 32 384 Lumenal. {ECO:0000255}.
CARBOHYD 73 73 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 77 77 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 196 196 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 25 147 ALQQWFLQAPRSPREERSPQEETPEGPTDAPAADEPPSELV
PGPPCVANASANATADFEQLPARIQDFLRYRHCRHFPLLWD
APAKCAGGRGVFLLLAVKSAPEHYERRELIRRTWGQERSYG
-> VLQRRRLPPVRPHGPGPARGRPPHPALPHRRRLH (in
isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_025963.
VAR_SEQ 289 319 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_025964.
VAR_SEQ 317 335 ERAGLAPSGHEGIRPFGVQ -> GARRPGAQRPRGHPGPSA
CS (in isoform 3). {ECO:0000305}.
/FTId=VSP_047091.
CONFLICT 164 164 D -> N (in Ref. 2; BAD18819).
{ECO:0000305}.
CONFLICT 191 191 A -> T (in Ref. 4; AAH25357).
{ECO:0000305}.
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


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