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Q99NB2 (B3GN5_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:B3gnt5
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length377 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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.

Catalytic activity

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.

Pathway

Protein modification; protein glycosylation.

Subcellular location

Golgi apparatus membrane; Single-pass type II membrane protein By similarity.

Sequence similarities

Belongs to the glycosyltransferase 31 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 377377Lactosylceramide 1,3-N-acetyl-beta-D-glucosaminyltransferase
PRO_0000289212

Regions

Topological domain1 – 1414Cytoplasmic Potential
Transmembrane15 – 3521Helical; Signal-anchor for type II membrane protein; Potential
Topological domain36 – 377342Lumenal Potential

Amino acid modifications

Glycosylation581N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q99NB2 [UniParc].

Last modified May 29, 2007. Version 2.
Checksum: EC57827D7BFB5CF9

FASTA37744,131
        10         20         30         40         50         60 
MRVFVSSRRV KRWQFFHLFA ICFILSFMVF WGPINNYIMS HMKSYSYRYL INSYDFVNDS 

        70         80         90        100        110        120 
LSLKHSSVQP HHPYLINHRE KCQAQDVLLL LFIKTAPENY ERRSAIRKTW GNENYVQSQL 

       130        140        150        160        170        180 
NANIKILFAL GTPHPLKGKE LQKRLIWEDQ VYHDIIQQDF TDSFHNLTFK FLLQFGWANT 

       190        200        210        220        230        240 
FCPHARFLMT ADDDIFIHMP NLIEYLQGLE QVGVRDFWIG HVHRGGPPVR DKSSKYYVPY 

       250        260        270        280        290        300 
EMYKWPAYPD YTAGAAYVVS NDVAAKIYEA SQTLNSSMYI DDVFMGLCAN KVGVVPQDHV 

       310        320        330        340        350        360 
FFSGEGKIPY HPCIYEKMIT SHGHSQDLQD LWVEATDPKV KDISKGFFGQ IYCRLIKIVL 

       370 
LCRLTYRNSY PCRAAFA

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AABR03079736 Genomic DNA. No translation available.
AB045279 mRNA. Translation: BAB40941.1.
IPIIPI00358604.
RefSeqNP_446384.1. NM_053932.1.
UniGeneRn.20376.

3D structure databases

ProteinModelPortalQ99NB2.
ModBaseSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000002616.

Protein family/group databases

CAZyGT31. Glycosyltransferase Family 31.

Proteomic databases

PRIDEQ99NB2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000071848; ENSRNOP00000067153; ENSRNOG00000046258.
GeneID116740.
KEGGrno:116740.

Organism-specific databases

CTD84002.
RGD70955. B3gnt5.

Phylogenomic databases

eggNOGNOG253164.
GeneTreeENSGT00670000097716.
HOGENOMHOG000064519.
HOVERGENHBG101684.
InParanoidQ99NB2.
KOK03766.
OMALCANKMG.
OrthoDBEOG4PNXH6.

Enzyme and pathway databases

BRENDA2.4.1.206. 5301.
UniPathwayUPA00378.

Gene expression databases

GenevestigatorQ99NB2.

Family and domain databases

InterProIPR002659. Glyco_trans_31.
[Graphical view]
PANTHERPTHR11214. PTHR11214. 1 hit.
PfamPF01762. Galactosyl_T. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio619666.

Entry information

Entry nameB3GN5_RAT
AccessionPrimary (citable) accession number: Q99NB2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: May 29, 2007
Last modified: April 3, 2013
This is version 72 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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