B3GN5_RAT
ID B3GN5_RAT Reviewed; 377 AA.
AC Q99NB2;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Lactosylceramide 1,3-N-acetyl-beta-D-glucosaminyltransferase {ECO:0000305};
DE EC=2.4.1.206 {ECO:0000250|UniProtKB:Q8BGY6};
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|RGD:70955};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 100-344.
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).
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:0000250|UniProtKB:Q9BYG0}.
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:0000250|UniProtKB:Q9BYG0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13906;
CC Evidence={ECO:0000250|UniProtKB:Q9BYG0};
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:0000250|UniProtKB:Q9BYG0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23005;
CC Evidence={ECO:0000250|UniProtKB:Q9BYG0};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AABR03079736; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB045279; BAB40941.1; -; mRNA.
DR RefSeq; NP_446384.1; NM_053932.1.
DR AlphaFoldDB; Q99NB2; -.
DR SMR; Q99NB2; -.
DR STRING; 10116.ENSRNOP00000067153; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR GlyGen; Q99NB2; 1 site.
DR PaxDb; Q99NB2; -.
DR Ensembl; ENSRNOT00000071848; ENSRNOP00000067153; ENSRNOG00000046258.
DR Ensembl; ENSRNOT00000093901; ENSRNOP00000085318; ENSRNOG00000046258.
DR Ensembl; ENSRNOT00000103393; ENSRNOP00000079466; ENSRNOG00000046258.
DR Ensembl; ENSRNOT00000106647; ENSRNOP00000086439; ENSRNOG00000046258.
DR GeneID; 116740; -.
DR KEGG; rno:116740; -.
DR CTD; 84002; -.
DR RGD; 70955; B3gnt5.
DR eggNOG; KOG2287; Eukaryota.
DR GeneTree; ENSGT00940000159676; -.
DR HOGENOM; CLU_036849_2_4_1; -.
DR InParanoid; Q99NB2; -.
DR OMA; IYNKMIT; -.
DR OrthoDB; 1037602at2759; -.
DR PhylomeDB; Q99NB2; -.
DR TreeFam; TF318639; -.
DR BRENDA; 2.4.1.206; 5301.
DR Reactome; R-RNO-913709; O-linked glycosylation of mucins.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q99NB2; -.
DR Proteomes; UP000002494; Chromosome 11.
DR Bgee; ENSRNOG00000046258; Expressed in spleen and 9 other tissues.
DR Genevisible; Q99NB2; RN.
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; ISO:RGD.
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; IEP:RGD.
DR GO; GO:0007417; P:central nervous system development; ISO:RGD.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
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..377
FT /note="Lactosylceramide 1,3-N-acetyl-beta-D-
FT glucosaminyltransferase"
FT /id="PRO_0000289212"
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..377
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 377 AA; 44131 MW; EC57827D7BFB5CF9 CRC64;
MRVFVSSRRV KRWQFFHLFA ICFILSFMVF WGPINNYIMS HMKSYSYRYL INSYDFVNDS
LSLKHSSVQP HHPYLINHRE KCQAQDVLLL LFIKTAPENY ERRSAIRKTW GNENYVQSQL
NANIKILFAL GTPHPLKGKE LQKRLIWEDQ VYHDIIQQDF TDSFHNLTFK FLLQFGWANT
FCPHARFLMT ADDDIFIHMP NLIEYLQGLE QVGVRDFWIG HVHRGGPPVR DKSSKYYVPY
EMYKWPAYPD YTAGAAYVVS NDVAAKIYEA SQTLNSSMYI DDVFMGLCAN KVGVVPQDHV
FFSGEGKIPY HPCIYEKMIT SHGHSQDLQD LWVEATDPKV KDISKGFFGQ IYCRLIKIVL
LCRLTYRNSY PCRAAFA
