B3GN5_HUMAN
ID B3GN5_HUMAN Reviewed; 378 AA.
AC Q9BYG0; D3DNS5; Q59FE3; Q7L9Z5; Q8WWP9;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Lactosylceramide 1,3-N-acetyl-beta-D-glucosaminyltransferase {ECO:0000305};
DE EC=2.4.1.206 {ECO:0000269|PubMed:11283017};
DE AltName: Full=Lactotriaosylceramide synthase;
DE Short=Lc(3)Cer synthase;
DE Short=Lc3 synthase;
DE AltName: Full=UDP-GlcNAc:beta-Gal beta-1,3-N-acetylglucosaminyltransferase 5;
DE Short=BGnT-5;
DE Short=Beta-1,3-Gn-T5;
DE Short=Beta-1,3-N-acetylglucosaminyltransferase 5;
DE Short=Beta3Gn-T5;
GN Name=B3GNT5 {ECO:0000312|HGNC:HGNC:15684};
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], CATALYTIC ACTIVITY, TISSUE SPECIFICITY,
RP INDUCTION, AND FUNCTION.
RX PubMed=11283017; DOI=10.1074/jbc.m011369200;
RA Togayachi A., Akashima T., Ookubo R., Kudo T., Nishihara S., Iwasaki H.,
RA Natsume A., Mio H., Inokuchi J., Irimura T., Sasaki K., Narimatsu H.;
RT "Molecular cloning and characterization of UDP-GlcNAc:lactosylceramide beta
RT 1,3-N-acetylglucosaminyltransferase (beta 3Gn-T5), an essential enzyme for
RT the expression of HNK-1 and Lewis X epitopes on glycolipids.";
RL J. Biol. Chem. 276:22032-22040(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=11384981; DOI=10.1074/jbc.m102979200;
RA Henion T.R., Zhou D., Wolfer D.P., Jungalwala F.B., Hennet T.;
RT "Cloning of a mouse beta 1,3 N-acetylglucosaminyltransferase GlcNAc(beta
RT 1,3)Gal(beta 1,4)Glc-ceramide synthase gene encoding the key regulator of
RT lacto-series glycolipid biosynthesis.";
RL J. Biol. Chem. 276:30261-30269(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Bennett E.P.;
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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: Beta-1,3-N-acetylglucosaminyltransferase that plays a key
CC role in the synthesis of lacto- or neolacto-series carbohydrate chains
CC on glycolipids, notably by participating in biosynthesis of HNK-1 and
CC Lewis X carbohydrate structures. Has strong activity toward
CC lactosylceramide (LacCer) and neolactotetraosylceramide (nLc(4)Cer;
CC paragloboside), resulting in the synthesis of Lc(3)Cer and
CC neolactopentaosylceramide (nLc(5)Cer), respectively. Probably plays a
CC central role in regulating neolacto-series glycolipid synthesis during
CC embryonic development. {ECO:0000269|PubMed:11283017,
CC ECO:0000269|PubMed:11384981}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-Cer(d18:1(4E)) + UDP-N-
CC acetyl-alpha-D-glucosamine = a beta-D-GlcNAc-(1->3)-beta-D-Gal-
CC (1->4)-beta-D-Glc-(1<->1)-Cer(d18:1(4E)) + H(+) + UDP;
CC Xref=Rhea:RHEA:13905, ChEBI:CHEBI:15378, ChEBI:CHEBI:17103,
CC ChEBI:CHEBI:17950, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223;
CC EC=2.4.1.206; Evidence={ECO:0000269|PubMed:11283017,
CC ECO:0000269|PubMed:11384981};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13906;
CC Evidence={ECO:0000269|PubMed:11283017, ECO:0000269|PubMed:11384981};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a neolactoside nLc4Cer(d18:1(4E)) + UDP-N-acetyl-alpha-D-
CC glucosamine = a neolactoside IV(3)-beta-GlcNAc-nLc4Cer(d18:1(4E)) +
CC H(+) + UDP; Xref=Rhea:RHEA:23004, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17006, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:142448; Evidence={ECO:0000269|PubMed:11283017};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23005;
CC Evidence={ECO:0000269|PubMed:11283017};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- INTERACTION:
CC Q9BYG0; Q9UHG0: DCDC2; NbExp=3; IntAct=EBI-3923833, EBI-10303987;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in lung, colon,
CC placenta, testis, pituitary gland and cerebellum. Weakly expressed in
CC brain, liver, spleen, lymph node and thymus.
CC {ECO:0000269|PubMed:11283017}.
CC -!- INDUCTION: Up-regulated by stimulation with retinoic acid and down-
CC regulated with 12-O-tetradecanoylphorbol-13-acetate (TPA).
CC {ECO:0000269|PubMed:11283017}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD92754.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=Beta1,3-
CC N-acetylglucosaminyltransferase 5;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_538";
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DR EMBL; AB045278; BAB40940.1; -; mRNA.
DR EMBL; AF368169; AAK53403.1; -; mRNA.
DR EMBL; AJ304505; CAC83093.1; -; mRNA.
DR EMBL; AB209517; BAD92754.1; ALT_FRAME; mRNA.
DR EMBL; CH471052; EAW78333.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78334.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78335.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78336.1; -; Genomic_DNA.
DR EMBL; BC028058; AAH28058.1; -; mRNA.
DR CCDS; CCDS3244.1; -.
DR RefSeq; NP_114436.1; NM_032047.4.
DR RefSeq; XP_005247880.1; XM_005247823.4.
DR RefSeq; XP_005247881.1; XM_005247824.3.
DR RefSeq; XP_005247882.1; XM_005247825.3.
DR RefSeq; XP_011511527.1; XM_011513225.2.
DR RefSeq; XP_011511528.1; XM_011513226.2.
DR RefSeq; XP_011511529.1; XM_011513227.2.
DR RefSeq; XP_011511530.1; XM_011513228.2.
DR RefSeq; XP_011511531.1; XM_011513229.2.
DR RefSeq; XP_016862798.1; XM_017007309.1.
DR AlphaFoldDB; Q9BYG0; -.
DR SMR; Q9BYG0; -.
DR BioGRID; 123846; 5.
DR IntAct; Q9BYG0; 2.
DR STRING; 9606.ENSP00000316173; -.
DR SwissLipids; SLP:000000768; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR GlyGen; Q9BYG0; 1 site.
DR PhosphoSitePlus; Q9BYG0; -.
DR BioMuta; B3GNT5; -.
DR DMDM; 74733473; -.
DR EPD; Q9BYG0; -.
DR MassIVE; Q9BYG0; -.
DR MaxQB; Q9BYG0; -.
DR PaxDb; Q9BYG0; -.
DR PeptideAtlas; Q9BYG0; -.
DR PRIDE; Q9BYG0; -.
DR ProteomicsDB; 79636; -.
DR Antibodypedia; 2643; 134 antibodies from 22 providers.
DR DNASU; 84002; -.
DR Ensembl; ENST00000326505.4; ENSP00000316173.3; ENSG00000176597.12.
DR Ensembl; ENST00000460419.1; ENSP00000420778.1; ENSG00000176597.12.
DR Ensembl; ENST00000465010.1; ENSP00000417868.1; ENSG00000176597.12.
DR GeneID; 84002; -.
DR KEGG; hsa:84002; -.
DR MANE-Select; ENST00000326505.4; ENSP00000316173.3; NM_032047.5; NP_114436.1.
DR UCSC; uc003flk.3; human.
DR CTD; 84002; -.
DR DisGeNET; 84002; -.
DR GeneCards; B3GNT5; -.
DR HGNC; HGNC:15684; B3GNT5.
DR HPA; ENSG00000176597; Tissue enhanced (bone).
DR MIM; 615333; gene.
DR neXtProt; NX_Q9BYG0; -.
DR OpenTargets; ENSG00000176597; -.
DR PharmGKB; PA25221; -.
DR VEuPathDB; HostDB:ENSG00000176597; -.
DR eggNOG; KOG2287; Eukaryota.
DR GeneTree; ENSGT00940000159676; -.
DR HOGENOM; CLU_036849_2_4_1; -.
DR InParanoid; Q9BYG0; -.
DR OMA; FNTYPCK; -.
DR PhylomeDB; Q9BYG0; -.
DR TreeFam; TF318639; -.
DR BioCyc; MetaCyc:ENSG00000176597-MON; -.
DR BRENDA; 2.4.1.206; 2681.
DR PathwayCommons; Q9BYG0; -.
DR Reactome; R-HSA-913709; O-linked glycosylation of mucins.
DR SignaLink; Q9BYG0; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 84002; 17 hits in 1071 CRISPR screens.
DR ChiTaRS; B3GNT5; human.
DR GenomeRNAi; 84002; -.
DR Pharos; Q9BYG0; Tbio.
DR PRO; PR:Q9BYG0; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9BYG0; protein.
DR Bgee; ENSG00000176597; Expressed in ileal mucosa and 167 other tissues.
DR ExpressionAtlas; Q9BYG0; baseline and differential.
DR Genevisible; Q9BYG0; 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:0008457; F:beta-galactosyl-N-acetylglucosaminylgalactosylglucosyl-ceramide beta-1,3-acetylglucosaminyltransferase activity; IDA:UniProtKB.
DR GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0047256; F:lactosylceramide 1,3-N-acetyl-beta-D-glucosaminyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008499; F:UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase activity; TAS:Reactome.
DR GO; GO:0007420; P:brain development; IBA:GO_Central.
DR GO; GO:0007417; P:central nervous system development; IDA:UniProtKB.
DR GO; GO:0009247; P:glycolipid biosynthetic process; TAS:UniProtKB.
DR GO; GO:0016266; P:O-glycan processing; TAS:Reactome.
DR GO; GO:0006486; P:protein glycosylation; TAS:UniProtKB.
DR InterPro; IPR002659; Glyco_trans_31.
DR PANTHER; PTHR11214; PTHR11214; 1.
DR Pfam; PF01762; Galactosyl_T; 1.
PE 1: Evidence at protein level;
KW Developmental protein; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Lipid metabolism; Membrane; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..378
FT /note="Lactosylceramide 1,3-N-acetyl-beta-D-
FT glucosaminyltransferase"
FT /id="PRO_0000289209"
FT TOPO_DOM 1..14
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 15..35
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 36..378
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 378 AA; 44053 MW; E19BA966A5E12CD2 CRC64;
MRMLVSGRRV KKWQLIIQLF ATCFLASLMF FWEPIDNHIV SHMKSYSYRY LINSYDFVND
TLSLKHTSAG PRYQYLINHK EKCQAQDVLL LLFVKTAPEN YDRRSGIRRT WGNENYVRSQ
LNANIKTLFA LGTPNPLEGE ELQRKLAWED QRYNDIIQQD FVDSFYNLTL KLLMQFSWAN
TYCPHAKFLM TADDDIFIHM PNLIEYLQSL EQIGVQDFWI GRVHRGAPPI RDKSSKYYVS
YEMYQWPAYP DYTAGAAYVI SGDVAAKVYE ASQTLNSSLY IDDVFMGLCA NKIGIVPQDH
VFFSGEGKTP YHPCIYEKMM TSHGHLEDLQ DLWKNATDPK VKTISKGFFG QIYCRLMKII
LLCKISYVDT YPCRAAFI
