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Protein

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

Gene

B3gnt5

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 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 (By similarity).By similarity

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.

Pathwayi

GO - Molecular functioni

  1. beta-galactosyl-N-acetylglucosaminylgalactosylglucosyl-ceramide beta-1,3-acetylglucosaminyltransferase activity Source: Ensembl
  2. galactosyltransferase activity Source: InterPro
  3. lactosylceramide 1,3-N-acetyl-beta-D-glucosaminyltransferase activity Source: UniProtKB-EC
  4. lipopolysaccharide N-acetylglucosaminyltransferase activity Source: Ensembl

GO - Biological processi

  1. central nervous system development Source: Ensembl
  2. protein glycosylation Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Glycosyltransferase, Transferase

Enzyme and pathway databases

BRENDAi2.4.1.206. 5301.
ReactomeiREACT_196259. O-linked glycosylation of mucins.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT31. Glycosyltransferase Family 31.

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 11

Organism-specific databases

RGDi70955. B3gnt5.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1414CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei15 – 3521Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini36 – 377342LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. Golgi membrane Source: UniProtKB-SubCell
  2. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 377377Lactosylceramide 1,3-N-acetyl-beta-D-glucosaminyltransferasePRO_0000289212Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi58 – 581N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PRIDEiQ99NB2.

Expressioni

Gene expression databases

GenevestigatoriQ99NB2.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000002616.

Structurei

3D structure databases

ProteinModelPortaliQ99NB2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyltransferase 31 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG253164.
GeneTreeiENSGT00760000118879.
HOGENOMiHOG000064519.
HOVERGENiHBG101684.
InParanoidiQ99NB2.
KOiK03766.
OMAiTWGNEKY.
OrthoDBiEOG7C2R1D.
PhylomeDBiQ99NB2.
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.

Q99NB2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRVFVSSRRV KRWQFFHLFA ICFILSFMVF WGPINNYIMS HMKSYSYRYL
60 70 80 90 100
INSYDFVNDS LSLKHSSVQP HHPYLINHRE KCQAQDVLLL LFIKTAPENY
110 120 130 140 150
ERRSAIRKTW GNENYVQSQL NANIKILFAL GTPHPLKGKE LQKRLIWEDQ
160 170 180 190 200
VYHDIIQQDF TDSFHNLTFK FLLQFGWANT FCPHARFLMT ADDDIFIHMP
210 220 230 240 250
NLIEYLQGLE QVGVRDFWIG HVHRGGPPVR DKSSKYYVPY EMYKWPAYPD
260 270 280 290 300
YTAGAAYVVS NDVAAKIYEA SQTLNSSMYI DDVFMGLCAN KVGVVPQDHV
310 320 330 340 350
FFSGEGKIPY HPCIYEKMIT SHGHSQDLQD LWVEATDPKV KDISKGFFGQ
360 370
IYCRLIKIVL LCRLTYRNSY PCRAAFA
Length:377
Mass (Da):44,131
Last modified:May 29, 2007 - v2
Checksum:iEC57827D7BFB5CF9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03079736 Genomic DNA. No translation available.
AB045279 mRNA. Translation: BAB40941.1.
RefSeqiNP_446384.1. NM_053932.1.
XP_008767071.1. XM_008768849.1.
UniGeneiRn.20376.

Genome annotation databases

EnsembliENSRNOT00000071848; ENSRNOP00000067153; ENSRNOG00000046258.
GeneIDi116740.
KEGGirno:116740.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03079736 Genomic DNA. No translation available.
AB045279 mRNA. Translation: BAB40941.1.
RefSeqiNP_446384.1. NM_053932.1.
XP_008767071.1. XM_008768849.1.
UniGeneiRn.20376.

3D structure databases

ProteinModelPortaliQ99NB2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000002616.

Protein family/group databases

CAZyiGT31. Glycosyltransferase Family 31.

Proteomic databases

PRIDEiQ99NB2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000071848; ENSRNOP00000067153; ENSRNOG00000046258.
GeneIDi116740.
KEGGirno:116740.

Organism-specific databases

CTDi84002.
RGDi70955. B3gnt5.

Phylogenomic databases

eggNOGiNOG253164.
GeneTreeiENSGT00760000118879.
HOGENOMiHOG000064519.
HOVERGENiHBG101684.
InParanoidiQ99NB2.
KOiK03766.
OMAiTWGNEKY.
OrthoDBiEOG7C2R1D.
PhylomeDBiQ99NB2.
TreeFamiTF318639.

Enzyme and pathway databases

UniPathwayiUPA00378.
BRENDAi2.4.1.206. 5301.
ReactomeiREACT_196259. O-linked glycosylation of mucins.

Miscellaneous databases

NextBioi619666.
PROiQ99NB2.

Gene expression databases

GenevestigatoriQ99NB2.

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. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  2. "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] OF 100-344.

Entry informationi

Entry nameiB3GN5_RAT
AccessioniPrimary (citable) accession number: Q99NB2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: May 29, 2007
Last modified: January 7, 2015
This is version 83 of the entry and version 2 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.