ID B3GN5_PIG Reviewed; 377 AA.
AC Q864U8;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 24-JAN-2024, entry version 99.
DE RecName: Full=Lactosylceramide 1,3-N-acetyl-beta-D-glucosaminyltransferase;
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;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Small intestine;
RX PubMed=16130451; DOI=10.1111/j.1439-0388.2005.00490.x;
RA Python P., Jorg H., Neuenschwander S., Asai-Coakwell M., Hagger C.,
RA Burgi E., Bertschinger H.U., Stranzinger G., Vogeli P.;
RT "Inheritance of the F4ab, F4ac and F4ad E. coli receptors in swine and
RT examination of four candidate genes for F4acR.";
RL J. Anim. Breed. Genet. 122:5-14(2005).
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; AY253338; AAO92023.1; -; mRNA.
DR RefSeq; NP_999492.1; NM_214327.1.
DR RefSeq; XP_005670075.1; XM_005670018.2.
DR RefSeq; XP_013837686.1; XM_013982232.1.
DR RefSeq; XP_013837687.1; XM_013982233.1.
DR RefSeq; XP_013837688.1; XM_013982234.1.
DR RefSeq; XP_013837689.1; XM_013982235.1.
DR RefSeq; XP_013837690.1; XM_013982236.1.
DR RefSeq; XP_013837691.1; XM_013982237.1.
DR AlphaFoldDB; Q864U8; -.
DR SMR; Q864U8; -.
DR STRING; 9823.ENSSSCP00000051412; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR GlyCosmos; Q864U8; 2 sites, No reported glycans.
DR PaxDb; 9823-ENSSSCP00000023905; -.
DR Ensembl; ENSSSCT00000030536.2; ENSSSCP00000023905.1; ENSSSCG00000024393.4.
DR Ensembl; ENSSSCT00000040962.1; ENSSSCP00000051412.1; ENSSSCG00000024393.4.
DR Ensembl; ENSSSCT00000053206.1; ENSSSCP00000043405.1; ENSSSCG00000024393.4.
DR Ensembl; ENSSSCT00000067752.1; ENSSSCP00000068897.1; ENSSSCG00000024393.4.
DR Ensembl; ENSSSCT00005040685.1; ENSSSCP00005024891.1; ENSSSCG00005025642.1.
DR Ensembl; ENSSSCT00005040711.1; ENSSSCP00005024908.1; ENSSSCG00005025642.1.
DR Ensembl; ENSSSCT00005040722.1; ENSSSCP00005024917.1; ENSSSCG00005025642.1.
DR Ensembl; ENSSSCT00015030812.1; ENSSSCP00015012195.1; ENSSSCG00015023174.1.
DR Ensembl; ENSSSCT00015030861.1; ENSSSCP00015012214.1; ENSSSCG00015023174.1.
DR Ensembl; ENSSSCT00015030976.1; ENSSSCP00015012261.1; ENSSSCG00015023174.1.
DR Ensembl; ENSSSCT00015031019.1; ENSSSCP00015012274.1; ENSSSCG00015023174.1.
DR Ensembl; ENSSSCT00025051345.1; ENSSSCP00025021908.1; ENSSSCG00025037728.1.
DR Ensembl; ENSSSCT00025051355.1; ENSSSCP00025021914.1; ENSSSCG00025037728.1.
DR Ensembl; ENSSSCT00025051367.1; ENSSSCP00025021918.1; ENSSSCG00025037728.1.
DR Ensembl; ENSSSCT00025051373.1; ENSSSCP00025021920.1; ENSSSCG00025037728.1.
DR Ensembl; ENSSSCT00030051330.1; ENSSSCP00030023364.1; ENSSSCG00030036904.1.
DR Ensembl; ENSSSCT00030051373.1; ENSSSCP00030023388.1; ENSSSCG00030036904.1.
DR Ensembl; ENSSSCT00030051391.1; ENSSSCP00030023397.1; ENSSSCG00030036904.1.
DR Ensembl; ENSSSCT00030051407.1; ENSSSCP00030023407.1; ENSSSCG00030036904.1.
DR Ensembl; ENSSSCT00035098954.1; ENSSSCP00035041843.1; ENSSSCG00035073064.1.
DR Ensembl; ENSSSCT00035098963.1; ENSSSCP00035041850.1; ENSSSCG00035073064.1.
DR Ensembl; ENSSSCT00035098971.1; ENSSSCP00035041852.1; ENSSSCG00035073064.1.
DR Ensembl; ENSSSCT00035098978.1; ENSSSCP00035041858.1; ENSSSCG00035073064.1.
DR Ensembl; ENSSSCT00040056034.1; ENSSSCP00040023295.1; ENSSSCG00040041893.1.
DR Ensembl; ENSSSCT00040056129.1; ENSSSCP00040023340.1; ENSSSCG00040041893.1.
DR Ensembl; ENSSSCT00040056165.1; ENSSSCP00040023356.1; ENSSSCG00040041893.1.
DR Ensembl; ENSSSCT00040056203.1; ENSSSCP00040023374.1; ENSSSCG00040041893.1.
DR Ensembl; ENSSSCT00045036520.1; ENSSSCP00045025426.1; ENSSSCG00045021347.1.
DR Ensembl; ENSSSCT00045036554.1; ENSSSCP00045025455.1; ENSSSCG00045021347.1.
DR Ensembl; ENSSSCT00045036584.1; ENSSSCP00045025469.1; ENSSSCG00045021347.1.
DR Ensembl; ENSSSCT00045036611.1; ENSSSCP00045025484.1; ENSSSCG00045021347.1.
DR Ensembl; ENSSSCT00050081803.1; ENSSSCP00050035125.1; ENSSSCG00050060042.1.
DR Ensembl; ENSSSCT00050081808.1; ENSSSCP00050035127.1; ENSSSCG00050060042.1.
DR Ensembl; ENSSSCT00050081809.1; ENSSSCP00050035128.1; ENSSSCG00050060042.1.
DR Ensembl; ENSSSCT00050081814.1; ENSSSCP00050035130.1; ENSSSCG00050060042.1.
DR Ensembl; ENSSSCT00055004738.1; ENSSSCP00055003665.1; ENSSSCG00055002483.1.
DR Ensembl; ENSSSCT00055004747.1; ENSSSCP00055003673.1; ENSSSCG00055002483.1.
DR Ensembl; ENSSSCT00055004750.1; ENSSSCP00055003675.1; ENSSSCG00055002483.1.
DR Ensembl; ENSSSCT00055004758.1; ENSSSCP00055003682.1; ENSSSCG00055002483.1.
DR Ensembl; ENSSSCT00060073825.1; ENSSSCP00060031827.1; ENSSSCG00060054230.1.
DR Ensembl; ENSSSCT00060073836.1; ENSSSCP00060031831.1; ENSSSCG00060054230.1.
DR Ensembl; ENSSSCT00060073843.1; ENSSSCP00060031835.1; ENSSSCG00060054230.1.
DR Ensembl; ENSSSCT00060073853.1; ENSSSCP00060031840.1; ENSSSCG00060054230.1.
DR Ensembl; ENSSSCT00065070200.1; ENSSSCP00065030589.1; ENSSSCG00065051251.1.
DR Ensembl; ENSSSCT00065070203.1; ENSSSCP00065030591.1; ENSSSCG00065051251.1.
DR Ensembl; ENSSSCT00065070210.1; ENSSSCP00065030596.1; ENSSSCG00065051251.1.
DR Ensembl; ENSSSCT00065070213.1; ENSSSCP00065030598.1; ENSSSCG00065051251.1.
DR Ensembl; ENSSSCT00070040372.1; ENSSSCP00070033857.1; ENSSSCG00070020341.1.
DR Ensembl; ENSSSCT00070040376.1; ENSSSCP00070033860.1; ENSSSCG00070020341.1.
DR Ensembl; ENSSSCT00070040377.1; ENSSSCP00070033861.1; ENSSSCG00070020341.1.
DR GeneID; 397599; -.
DR KEGG; ssc:397599; -.
DR CTD; 84002; -.
DR VGNC; VGNC:85726; B3GNT5.
DR eggNOG; KOG2287; Eukaryota.
DR GeneTree; ENSGT00940000159676; -.
DR HOGENOM; CLU_036849_2_4_1; -.
DR InParanoid; Q864U8; -.
DR OrthoDB; 532757at2759; -.
DR TreeFam; TF318639; -.
DR Reactome; R-SSC-913709; O-linked glycosylation of mucins.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000008227; Chromosome 13.
DR Proteomes; UP000314985; Chromosome 13.
DR Proteomes; UP000694570; Unplaced.
DR Proteomes; UP000694571; Unplaced.
DR Proteomes; UP000694720; Unplaced.
DR Proteomes; UP000694722; Unplaced.
DR Proteomes; UP000694723; Unplaced.
DR Proteomes; UP000694724; Unplaced.
DR Proteomes; UP000694725; Unplaced.
DR Proteomes; UP000694726; Unplaced.
DR Proteomes; UP000694727; Unplaced.
DR Proteomes; UP000694728; Unplaced.
DR Bgee; ENSSSCG00000024393; Expressed in epididymis and 41 other cell types or tissues.
DR ExpressionAtlas; Q864U8; baseline and differential.
DR Genevisible; Q864U8; SS.
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; ISS:UniProtKB.
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; ISS:UniProtKB.
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.
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_0000289211"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..32
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..377
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 377 AA; 43971 MW; F09DD970FE5DAC03 CRC64;
MFGSGRRVKK WQFIQIFATC FVLSLMFFWG PIDNHIVSHM KSYSYRYLIN SYDFVNDSLS
LKRSEDGTPR YQYLINHEEK CQAQDVLLLL FVKTAPENYN RRSAIRNTWG NEKYVQSQLN
ANIKTLFVLG TPSDPLMRER LQRRLVWEDH MYSDIIQQDF VDSFYNLTLK FLLQFKWANS
FCPHAKFLMT ADDDIFIHMP NLIEYLQSLE QMGVQDFWIG RVHHGAPPVR DKSSKYYVSY
DMYQWPAYPD YTAGAAYVIS GDVATKVYEA SQTLNSSLYI DDVFMGLCAN KIGLVPQSHA
FFSGEGKTPY HPCIYEKMMT SHGHVEDLQD LWKDATDPKV KMISKGFFGQ IYCRIIKIVL
LCKLTYLDTY PCRAAFA
//
