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   24-JAN-2024, entry version 125.
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}.
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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   GlyCosmos; Q99NB2; 1 site, No reported glycans.
DR   GlyGen; Q99NB2; 1 site.
DR   PhosphoSitePlus; Q99NB2; -.
DR   PaxDb; 10116-ENSRNOP00000067153; -.
DR   Ensembl; ENSRNOT00000071848.3; ENSRNOP00000067153.1; ENSRNOG00000046258.3.
DR   Ensembl; ENSRNOT00000093901.1; ENSRNOP00000085318.1; ENSRNOG00000046258.3.
DR   Ensembl; ENSRNOT00000103393.1; ENSRNOP00000079466.1; ENSRNOG00000046258.3.
DR   Ensembl; ENSRNOT00000106647.1; ENSRNOP00000086439.1; ENSRNOG00000046258.3.
DR   Ensembl; ENSRNOT00055007942; ENSRNOP00055005978; ENSRNOG00055004977.
DR   Ensembl; ENSRNOT00055007946; ENSRNOP00055005980; ENSRNOG00055004977.
DR   Ensembl; ENSRNOT00055007949; ENSRNOP00055005982; ENSRNOG00055004977.
DR   Ensembl; ENSRNOT00060020532; ENSRNOP00060016169; ENSRNOG00060012104.
DR   Ensembl; ENSRNOT00060020538; ENSRNOP00060016173; ENSRNOG00060012104.
DR   Ensembl; ENSRNOT00060020543; ENSRNOP00060016178; ENSRNOG00060012104.
DR   Ensembl; ENSRNOT00065004984; ENSRNOP00065003527; ENSRNOG00065003492.
DR   Ensembl; ENSRNOT00065004986; ENSRNOP00065003529; ENSRNOG00065003492.
DR   Ensembl; ENSRNOT00065004987; ENSRNOP00065003530; ENSRNOG00065003492.
DR   GeneID; 116740; -.
DR   KEGG; rno:116740; -.
DR   AGR; RGD:70955; -.
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; NTYSCKA; -.
DR   OrthoDB; 532757at2759; -.
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 cell types or tissues.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0008457; F:beta-galactosyl-N-acetylglucosaminylgalactosylglucosyl-ceramide beta-1,3-acetylglucosaminyltransferase activity; ISO:RGD.
DR   GO; GO:0047256; F:lactosylceramide 1,3-N-acetyl-beta-D-glucosaminyltransferase activity; IEA:UniProtKB-EC.
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:0006493; P:protein O-linked glycosylation; IBA:GO_Central.
DR   Gene3D; 3.90.550.50; -; 1.
DR   InterPro; IPR002659; Glyco_trans_31.
DR   PANTHER; PTHR11214; BETA-1,3-N-ACETYLGLUCOSAMINYLTRANSFERASE; 1.
DR   PANTHER; PTHR11214:SF21; LACTOSYLCERAMIDE 1,3-N-ACETYL-BETA-D-GLUCOSAMINYLTRANSFERASE; 1.
DR   Pfam; PF01762; Galactosyl_T; 1.
DR   Genevisible; Q99NB2; RN.
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
//