B3GN8_HUMAN
ID B3GN8_HUMAN Reviewed; 397 AA.
AC Q7Z7M8;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 8;
DE Short=BGnT-8;
DE Short=Beta-1,3-Gn-T8;
DE Short=Beta-1,3-N-acetylglucosaminyltransferase 8;
DE Short=Beta3Gn-T8;
DE EC=2.4.1.-;
GN Name=B3GNT8 {ECO:0000312|EMBL:BAD86525.1};
GN Synonyms=B3GALT7 {ECO:0000303|PubMed:15486459},
GN BGALT15 {ECO:0000312|EMBL:AAP34405.1};
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] {ECO:0000305, ECO:0000312|EMBL:AAP34405.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Lung {ECO:0000269|PubMed:15486459};
RX PubMed=15486459; DOI=10.1023/b:glyc.0000045098.78968.4c;
RA Huang C., Zhou J., Wu S., Shan Y., Teng S., Yu L.;
RT "Cloning and tissue distribution of the human B3GALT7 gene, a member of the
RT beta1,3-Glycosyltransferase family.";
RL Glycoconj. J. 21:267-273(2004).
RN [2] {ECO:0000305, ECO:0000312|EMBL:BAD86525.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND
RP ENZYME ACTIVITY.
RC TISSUE=Colon cancer {ECO:0000312|EMBL:BAD86525.1};
RX PubMed=15620693; DOI=10.1016/j.febslet.2004.11.037;
RA Ishida H., Togayachi A., Sakai T., Iwai T., Hiruma T., Sato T., Okubo R.,
RA Inaba N., Kudo T., Gotoh M., Shoda J., Tanaka N., Narimatsu H.;
RT "A novel beta1,3-N-acetylglucosaminyltransferase (beta3Gn-T8), which
RT synthesizes poly-N-acetyllactosamine, is dramatically upregulated in colon
RT cancer.";
RL FEBS Lett. 579:71-78(2005).
RN [3] {ECO:0000312|EMBL:CAD11601.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Bennett E.P.;
RT "Beta1,3 GlcNAc-Transferase-T7, core 3 synthase.";
RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305}
RP FUNCTION, INTERACTION WITH B3GNT2, AND ENZYME ACTIVITY.
RX PubMed=15917431; DOI=10.1093/glycob/cwi082;
RA Seko A., Yamashita K.;
RT "Characterization of a novel galactose beta1,3-N-
RT acetylglucosaminyltransferase (beta3Gn-T8): the complex formation of
RT beta3Gn-T2 and beta3Gn-T8 enhances enzymatic activity.";
RL Glycobiology 15:943-951(2005).
RN [5]
RP INTERACTION WITH B3GNT2, AND MUTAGENESIS OF GLN-246.
RX PubMed=18826941; DOI=10.1074/jbc.m806933200;
RA Seko A., Yamashita K.;
RT "Activation of beta1,3-N-acetylglucosaminyltransferase-2 (beta3Gn-T2) by
RT beta3Gn-T8. Possible involvement of beta3Gn-T8 in increasing poly-N-
RT acetyllactosamine chains in differentiated HL-60 cells.";
RL J. Biol. Chem. 283:33094-33100(2008).
CC -!- FUNCTION: Beta-1,3-N-acetylglucosaminyltransferase that plays a role in
CC the elongation of specific branch structures of multiantennary N-
CC glycans. Has strong activity towards tetraantennary N-glycans and 2,6
CC triantennary glycans. {ECO:0000269|PubMed:15620693,
CC ECO:0000269|PubMed:15917431}.
CC -!- PATHWAY: Protein modification; protein glycosylation. {ECO:0000305}.
CC -!- SUBUNIT: Interacts with B3GNT2; this interaction greatly increases
CC B3GNT2 catalytic activity, independently of B3GNT8 enzymatic activity.
CC {ECO:0000269|PubMed:15917431, ECO:0000269|PubMed:18826941}.
CC -!- INTERACTION:
CC Q7Z7M8; Q9NY97: B3GNT2; NbExp=2; IntAct=EBI-20593091, EBI-3922389;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q9NY97}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q9NY97}.
CC -!- TISSUE SPECIFICITY: Highly expressed in small intestine, pancreas,
CC spleen, bone marrow, lung, throat, and ileum, and weakly in fetal
CC brain, cerebellum, heart, liver, tongue, breast, uteri, and testis. Not
CC detected in colon. Differentially expressed in human tumor cell lines.
CC {ECO:0000269|PubMed:15486459, ECO:0000269|PubMed:15620693}.
CC -!- INDUCTION: Up-regulated in colon cancer. {ECO:0000269|PubMed:15620693}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC {ECO:0000255}.
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DR EMBL; AY277592; AAP34405.1; -; mRNA.
DR EMBL; AB175895; BAD86525.1; -; mRNA.
DR EMBL; AJ419172; CAD11601.1; -; mRNA.
DR CCDS; CCDS12582.1; -.
DR RefSeq; NP_940942.1; NM_198540.2.
DR RefSeq; XP_011525236.1; XM_011526934.2.
DR AlphaFoldDB; Q7Z7M8; -.
DR SMR; Q7Z7M8; -.
DR BioGRID; 131936; 53.
DR IntAct; Q7Z7M8; 2.
DR STRING; 9606.ENSP00000312700; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR GlyGen; Q7Z7M8; 1 site.
DR iPTMnet; Q7Z7M8; -.
DR PhosphoSitePlus; Q7Z7M8; -.
DR BioMuta; B3GNT8; -.
DR DMDM; 74713777; -.
DR CPTAC; CPTAC-1233; -.
DR jPOST; Q7Z7M8; -.
DR MassIVE; Q7Z7M8; -.
DR PaxDb; Q7Z7M8; -.
DR PeptideAtlas; Q7Z7M8; -.
DR PRIDE; Q7Z7M8; -.
DR ProteomicsDB; 69570; -.
DR Antibodypedia; 70706; 11 antibodies from 8 providers.
DR DNASU; 374907; -.
DR Ensembl; ENST00000321702.2; ENSP00000312700.1; ENSG00000177191.3.
DR Ensembl; ENST00000691102.1; ENSP00000510371.1; ENSG00000177191.3.
DR GeneID; 374907; -.
DR KEGG; hsa:374907; -.
DR MANE-Select; ENST00000691102.1; ENSP00000510371.1; NM_001385648.2; NP_001372577.1.
DR UCSC; uc002oqs.3; human.
DR CTD; 374907; -.
DR DisGeNET; 374907; -.
DR GeneCards; B3GNT8; -.
DR HGNC; HGNC:24139; B3GNT8.
DR HPA; ENSG00000177191; Tissue enhanced (esophagus, vagina).
DR MIM; 615357; gene.
DR neXtProt; NX_Q7Z7M8; -.
DR OpenTargets; ENSG00000177191; -.
DR PharmGKB; PA134910679; -.
DR VEuPathDB; HostDB:ENSG00000177191; -.
DR eggNOG; KOG2287; Eukaryota.
DR GeneTree; ENSGT00940000161895; -.
DR HOGENOM; CLU_036849_5_0_1; -.
DR InParanoid; Q7Z7M8; -.
DR OMA; WESHRYS; -.
DR OrthoDB; 640360at2759; -.
DR PhylomeDB; Q7Z7M8; -.
DR TreeFam; TF318639; -.
DR PathwayCommons; Q7Z7M8; -.
DR Reactome; R-HSA-913709; O-linked glycosylation of mucins.
DR SignaLink; Q7Z7M8; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 374907; 14 hits in 1065 CRISPR screens.
DR GenomeRNAi; 374907; -.
DR Pharos; Q7Z7M8; Tbio.
DR PRO; PR:Q7Z7M8; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q7Z7M8; protein.
DR Bgee; ENSG00000177191; Expressed in lower esophagus mucosa and 127 other tissues.
DR Genevisible; Q7Z7M8; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
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:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0016262; F:protein N-acetylglucosaminyltransferase activity; IDA:HGNC-UCL.
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:0016266; P:O-glycan processing; TAS:Reactome.
DR GO; GO:0030311; P:poly-N-acetyllactosamine biosynthetic process; IDA:HGNC-UCL.
DR InterPro; IPR002659; Glyco_trans_31.
DR PANTHER; PTHR11214; PTHR11214; 1.
DR Pfam; PF01762; Galactosyl_T; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Glycosyltransferase; Golgi apparatus; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..397
FT /note="UDP-GlcNAc:betaGal beta-1,3-N-
FT acetylglucosaminyltransferase 8"
FT /id="PRO_0000306381"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..23
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 24..397
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 33..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..52
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 137
FT /note="S -> G (in dbSNP:rs284662)"
FT /id="VAR_049348"
FT MUTAGEN 246
FT /note="Q->A: Loss of enzymatic activity, no loss of B3GNT2-
FT binding and activation."
FT /evidence="ECO:0000269|PubMed:18826941"
SQ SEQUENCE 397 AA; 43396 MW; AC0CCE6880F46850 CRC64;
MRCPKCLLCL SALLTLLGLK VYIEWTSESR LSKAYPSPRG TPPSPTPANP EPTLPANLST
RLGQTIPLPF AYWNQQQWRL GSLPSGDSTE TGGCQAWGAA AATEIPDFAS YPKDLRRFLL
SAACRSFPQW LPGGGGSQVS SCSDTDVPYL LLAVKSEPGR FAERQAVRET WGSPAPGIRL
LFLLGSPVGE AGPDLDSLVA WESRRYSDLL LWDFLDVPFN QTLKDLLLLA WLGRHCPTVS
FVLRAQDDAF VHTPALLAHL RALPPASARS LYLGEVFTQA MPLRKPGGPF YVPESFFEGG
YPAYASGGGY VIAGRLAPWL LRAAARVAPF PFEDVYTGLC IRALGLVPQA HPGFLTAWPA
DRTADHCAFR NLLLVRPLGP QASIRLWKQL QDPRLQC
