B3GN5_MOUSE
ID B3GN5_MOUSE Reviewed; 376 AA.
AC Q8BGY6; Q810C6; Q923K7;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Lactosylceramide 1,3-N-acetyl-beta-D-glucosaminyltransferase {ECO:0000305};
DE EC=2.4.1.206 {ECO:0000269|PubMed:11384981};
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|MGI:MGI:2137302};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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], ENZYME ACTIVITY, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, 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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head, Spinal ganglion, and Wolffian duct;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; 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. Plays a central
CC role in regulating neolacto-series glycolipid synthesis during
CC embryonic development. {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:11384981};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13906;
CC Evidence={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:11384981};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23005;
CC Evidence={ECO:0000269|PubMed:11384981};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in adult spleen, placenta and
CC cerebellar Purkinje cells where it colocalized with HNK-1. Expressed at
CC lower level in brain, lung, thymus and muscle.
CC {ECO:0000269|PubMed:11384981}.
CC -!- DEVELOPMENTAL STAGE: Mainly expressed during embryonic development.
CC Expressed in most tissues at embryonic day 11 with elevated expression
CC in the developing central nervous system.
CC {ECO:0000269|PubMed:11384981}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC {ECO:0000305}.
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DR EMBL; AB059620; BAC66698.1; -; mRNA.
DR EMBL; AY029203; AAK31579.1; -; mRNA.
DR EMBL; AK032911; BAC28082.1; -; mRNA.
DR EMBL; AK048010; BAC33213.1; -; mRNA.
DR EMBL; AK083839; BAC39037.1; -; mRNA.
DR EMBL; BC063076; AAH63076.1; -; mRNA.
DR CCDS; CCDS28040.1; -.
DR RefSeq; NP_001152879.1; NM_001159407.1.
DR RefSeq; NP_001152880.1; NM_001159408.1.
DR RefSeq; NP_473393.2; NM_054052.3.
DR RefSeq; XP_006521769.1; XM_006521706.3.
DR AlphaFoldDB; Q8BGY6; -.
DR SMR; Q8BGY6; -.
DR STRING; 10090.ENSMUSP00000078712; -.
DR SwissLipids; SLP:000000767; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR GlyGen; Q8BGY6; 1 site.
DR iPTMnet; Q8BGY6; -.
DR PhosphoSitePlus; Q8BGY6; -.
DR MaxQB; Q8BGY6; -.
DR PaxDb; Q8BGY6; -.
DR PRIDE; Q8BGY6; -.
DR ProteomicsDB; 265190; -.
DR Antibodypedia; 2643; 134 antibodies from 22 providers.
DR DNASU; 108105; -.
DR Ensembl; ENSMUST00000079780; ENSMUSP00000078712; ENSMUSG00000022686.
DR Ensembl; ENSMUST00000119468; ENSMUSP00000113145; ENSMUSG00000022686.
DR Ensembl; ENSMUST00000121344; ENSMUSP00000112624; ENSMUSG00000022686.
DR Ensembl; ENSMUST00000164397; ENSMUSP00000126157; ENSMUSG00000022686.
DR GeneID; 108105; -.
DR KEGG; mmu:108105; -.
DR UCSC; uc007ypc.2; mouse.
DR CTD; 84002; -.
DR MGI; MGI:2137302; B3gnt5.
DR VEuPathDB; HostDB:ENSMUSG00000022686; -.
DR eggNOG; KOG2287; Eukaryota.
DR GeneTree; ENSGT00940000159676; -.
DR HOGENOM; CLU_036849_2_4_1; -.
DR InParanoid; Q8BGY6; -.
DR OMA; FNTYPCK; -.
DR OrthoDB; 1037602at2759; -.
DR PhylomeDB; Q8BGY6; -.
DR TreeFam; TF318639; -.
DR BRENDA; 2.4.1.206; 3474.
DR Reactome; R-MMU-913709; O-linked glycosylation of mucins.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 108105; 2 hits in 75 CRISPR screens.
DR ChiTaRS; B3gnt5; mouse.
DR PRO; PR:Q8BGY6; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q8BGY6; protein.
DR Bgee; ENSMUSG00000022686; Expressed in epithelium of lens and 163 other tissues.
DR Genevisible; Q8BGY6; MM.
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; ISS: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:0007420; P:brain development; IBA:GO_Central.
DR GO; GO:0007417; P:central nervous system development; ISS:UniProtKB.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; TAS:MGI.
DR InterPro; IPR002659; Glyco_trans_31.
DR PANTHER; PTHR11214; PTHR11214; 1.
DR Pfam; PF01762; Galactosyl_T; 1.
PE 2: Evidence at transcript level;
KW Developmental protein; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Lipid metabolism; Membrane; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..376
FT /note="Lactosylceramide 1,3-N-acetyl-beta-D-
FT glucosaminyltransferase"
FT /id="PRO_0000289210"
FT TOPO_DOM 1..13
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 14..34
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..376
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 181..184
FT /note="CPHA -> VHMP (in Ref. 2; AAK31579)"
FT /evidence="ECO:0000305"
FT CONFLICT 241
FT /note="M -> V (in Ref. 2; AAK31579)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 376 AA; 43914 MW; 6204E7AA5D12F52F CRC64;
MRLFVSRRVK RWKIFHFFVT CFILSFMVFW SPINNYIMSH MKSYSYRYLV NSYGFVNNSL
SLKHSSVQPH YPYLINHREK CQAQDVLLLL FIKTAPENYG RRSAIRKTWG NENYVQSQLN
ANIKILFALG TPGPLKGKEL QKRLIGEDQV YKDIIQQDFI DSFHNLTSKF LLQFSWANTF
CPHAKFLMTA DDDIFIHMPN LIEYLQGLEQ IGVRDFWIGH VHRGGPPVRD KSSKYYVPYE
MYKWPAYPDY TAGAAYVVSR DVAAKIYEAS QTLNSSMYID DVFMGLCANK VGILPQDHVF
FSGEGKIPYH PCIYEKMMTS HGHLQDLQDL WIEATHPKVK NISKGFFGQI YCRLIKIVLL
CRLTYRNSYP CWAAFA
