Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Lactosylceramide 1,3-N-acetyl-beta-D-glucosaminyltransferase

Gene

B3gnt5

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Beta-1,3-N-acetylglucosaminyltransferase that plays a key role in the synthesis of lacto- or neolacto-series carbohydrate chains on glycolipids, notably by participating in biosynthesis of HNK-1 and Lewis X carbohydrate structures. Has strong activity toward lactosylceramide (LacCer) and neolactotetraosylceramide (nLc4Cer; paragloboside), resulting in the synthesis of Lc3Cer and neolactopentaosylceramide (nLc5Cer), respectively. Plays a central role in regulating neolacto-series glycolipid synthesis during embryonic development.

Catalytic activityi

UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide = UDP + N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide.1 Publication

Pathwayi: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Glycosyltransferase, Transferase

Enzyme and pathway databases

BRENDAi2.4.1.206. 3474.
ReactomeiR-MMU-913709. O-linked glycosylation of mucins.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT31. Glycosyltransferase Family 31.

Chemistry

SwissLipidsiSLP:000000767.

Names & Taxonomyi

Protein namesi
Recommended name:
Lactosylceramide 1,3-N-acetyl-beta-D-glucosaminyltransferase (EC:2.4.1.206)
Alternative name(s):
Lactotriaosylceramide synthase
Short name:
Lc(3)Cer synthase
Short name:
Lc3 synthase
UDP-GlcNAc:beta-Gal beta-1,3-N-acetylglucosaminyltransferase 5
Short name:
BGnT-5
Short name:
Beta-1,3-Gn-T5
Short name:
Beta-1,3-N-acetylglucosaminyltransferase 5
Short name:
Beta3Gn-T5
Gene namesi
Name:B3gnt5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 16

Organism-specific databases

MGIiMGI:2137302. B3gnt5.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1313CytoplasmicSequence analysisAdd
BLAST
Transmembranei14 – 3421Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini35 – 376342LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 376376Lactosylceramide 1,3-N-acetyl-beta-D-glucosaminyltransferasePRO_0000289210Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi57 – 571N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ8BGY6.
PaxDbiQ8BGY6.
PRIDEiQ8BGY6.

Expressioni

Tissue specificityi

Highly expressed in adult spleen, placenta and cerebellar Purkinje cells where it colocalized with HNK-1. Expressed at lower level in brain, lung, thymus and muscle.1 Publication

Developmental stagei

Mainly expressed during embryonic development. Expressed in most tissues at embryonic day 11 with elevated expression in the developing central nervous system.1 Publication

Gene expression databases

BgeeiQ8BGY6.
GenevisibleiQ8BGY6. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000078712.

Structurei

3D structure databases

ProteinModelPortaliQ8BGY6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyltransferase 31 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2287. Eukaryota.
ENOG410ZZ1B. LUCA.
GeneTreeiENSGT00760000118879.
HOGENOMiHOG000064519.
HOVERGENiHBG101684.
InParanoidiQ8BGY6.
KOiK03766.
OMAiTWGNEKY.
OrthoDBiEOG7C2R1D.
PhylomeDBiQ8BGY6.
TreeFamiTF318639.

Family and domain databases

InterProiIPR002659. Glyco_trans_31.
[Graphical view]
PANTHERiPTHR11214. PTHR11214. 1 hit.
PfamiPF01762. Galactosyl_T. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8BGY6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLFVSRRVK RWKIFHFFVT CFILSFMVFW SPINNYIMSH MKSYSYRYLV
60 70 80 90 100
NSYGFVNNSL SLKHSSVQPH YPYLINHREK CQAQDVLLLL FIKTAPENYG
110 120 130 140 150
RRSAIRKTWG NENYVQSQLN ANIKILFALG TPGPLKGKEL QKRLIGEDQV
160 170 180 190 200
YKDIIQQDFI DSFHNLTSKF LLQFSWANTF CPHAKFLMTA DDDIFIHMPN
210 220 230 240 250
LIEYLQGLEQ IGVRDFWIGH VHRGGPPVRD KSSKYYVPYE MYKWPAYPDY
260 270 280 290 300
TAGAAYVVSR DVAAKIYEAS QTLNSSMYID DVFMGLCANK VGILPQDHVF
310 320 330 340 350
FSGEGKIPYH PCIYEKMMTS HGHLQDLQDL WIEATHPKVK NISKGFFGQI
360 370
YCRLIKIVLL CRLTYRNSYP CWAAFA
Length:376
Mass (Da):43,914
Last modified:March 1, 2003 - v1
Checksum:i6204E7AA5D12F52F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti181 – 1844CPHA → VHMP in AAK31579 (PubMed:11384981).Curated
Sequence conflicti241 – 2411M → V in AAK31579 (PubMed:11384981).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB059620 mRNA. Translation: BAC66698.1.
AY029203 mRNA. Translation: AAK31579.1.
AK032911 mRNA. Translation: BAC28082.1.
AK048010 mRNA. Translation: BAC33213.1.
AK083839 mRNA. Translation: BAC39037.1.
BC063076 mRNA. Translation: AAH63076.1.
CCDSiCCDS28040.1.
RefSeqiNP_001152879.1. NM_001159407.1.
NP_001152880.1. NM_001159408.1.
NP_473393.2. NM_054052.3.
XP_006521769.1. XM_006521706.2.
XP_011244105.1. XM_011245803.1.
UniGeneiMm.33935.

Genome annotation databases

EnsembliENSMUST00000079780; ENSMUSP00000078712; ENSMUSG00000022686.
ENSMUST00000119468; ENSMUSP00000113145; ENSMUSG00000022686.
ENSMUST00000121344; ENSMUSP00000112624; ENSMUSG00000022686.
ENSMUST00000164397; ENSMUSP00000126157; ENSMUSG00000022686.
GeneIDi108105.
KEGGimmu:108105.
UCSCiuc007ypc.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB059620 mRNA. Translation: BAC66698.1.
AY029203 mRNA. Translation: AAK31579.1.
AK032911 mRNA. Translation: BAC28082.1.
AK048010 mRNA. Translation: BAC33213.1.
AK083839 mRNA. Translation: BAC39037.1.
BC063076 mRNA. Translation: AAH63076.1.
CCDSiCCDS28040.1.
RefSeqiNP_001152879.1. NM_001159407.1.
NP_001152880.1. NM_001159408.1.
NP_473393.2. NM_054052.3.
XP_006521769.1. XM_006521706.2.
XP_011244105.1. XM_011245803.1.
UniGeneiMm.33935.

3D structure databases

ProteinModelPortaliQ8BGY6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000078712.

Chemistry

SwissLipidsiSLP:000000767.

Protein family/group databases

CAZyiGT31. Glycosyltransferase Family 31.

Proteomic databases

MaxQBiQ8BGY6.
PaxDbiQ8BGY6.
PRIDEiQ8BGY6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000079780; ENSMUSP00000078712; ENSMUSG00000022686.
ENSMUST00000119468; ENSMUSP00000113145; ENSMUSG00000022686.
ENSMUST00000121344; ENSMUSP00000112624; ENSMUSG00000022686.
ENSMUST00000164397; ENSMUSP00000126157; ENSMUSG00000022686.
GeneIDi108105.
KEGGimmu:108105.
UCSCiuc007ypc.2. mouse.

Organism-specific databases

CTDi84002.
MGIiMGI:2137302. B3gnt5.

Phylogenomic databases

eggNOGiKOG2287. Eukaryota.
ENOG410ZZ1B. LUCA.
GeneTreeiENSGT00760000118879.
HOGENOMiHOG000064519.
HOVERGENiHBG101684.
InParanoidiQ8BGY6.
KOiK03766.
OMAiTWGNEKY.
OrthoDBiEOG7C2R1D.
PhylomeDBiQ8BGY6.
TreeFamiTF318639.

Enzyme and pathway databases

UniPathwayiUPA00378.
BRENDAi2.4.1.206. 3474.
ReactomeiR-MMU-913709. O-linked glycosylation of mucins.

Miscellaneous databases

NextBioi360080.
PROiQ8BGY6.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BGY6.
GenevisibleiQ8BGY6. MM.

Family and domain databases

InterProiIPR002659. Glyco_trans_31.
[Graphical view]
PANTHERiPTHR11214. PTHR11214. 1 hit.
PfamiPF01762. Galactosyl_T. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and characterization of UDP-GlcNAc:lactosylceramide beta 1,3-N-acetylglucosaminyltransferase (beta 3Gn-T5), an essential enzyme for the expression of HNK-1 and Lewis X epitopes on glycolipids."
    Togayachi A., Akashima T., Ookubo R., Kudo T., Nishihara S., Iwasaki H., Natsume A., Mio H., Inokuchi J., Irimura T., Sasaki K., Narimatsu H.
    J. Biol. Chem. 276:22032-22040(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Cloning of a mouse beta 1,3 N-acetylglucosaminyltransferase GlcNAc(beta 1,3)Gal(beta 1,4)Glc-ceramide synthase gene encoding the key regulator of lacto-series glycolipid biosynthesis."
    Henion T.R., Zhou D., Wolfer D.P., Jungalwala F.B., Hennet T.
    J. Biol. Chem. 276:30261-30269(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Head, Spinal ganglion and Wolffian duct.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Brain.

Entry informationi

Entry nameiB3GN5_MOUSE
AccessioniPrimary (citable) accession number: Q8BGY6
Secondary accession number(s): Q810C6, Q923K7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: March 1, 2003
Last modified: February 17, 2016
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.