B3GN5_XENTR
ID B3GN5_XENTR Reviewed; 377 AA.
AC Q6P3P5; Q07G20;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 98.
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; ORFNames=TEgg092f15.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Egg;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
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. {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 -!- SEQUENCE CAUTION:
CC Sequence=CAL49301.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CR848570; CAL49301.1; ALT_INIT; mRNA.
DR EMBL; BC063912; AAH63912.1; -; mRNA.
DR EMBL; BC080164; AAH80164.1; -; mRNA.
DR RefSeq; NP_989240.1; NM_203909.1.
DR RefSeq; XP_017949312.1; XM_018093823.1.
DR RefSeq; XP_017949313.1; XM_018093824.1.
DR AlphaFoldDB; Q6P3P5; -.
DR SMR; Q6P3P5; -.
DR STRING; 8364.ENSXETP00000055015; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR PaxDb; Q6P3P5; -.
DR DNASU; 394849; -.
DR Ensembl; ENSXETT00000055015; ENSXETP00000055015; ENSXETG00000025974.
DR GeneID; 394849; -.
DR KEGG; xtr:394849; -.
DR CTD; 84002; -.
DR Xenbase; XB-GENE-955708; b3gnt5.
DR eggNOG; KOG2287; Eukaryota.
DR HOGENOM; CLU_036849_2_4_1; -.
DR InParanoid; Q6P3P5; -.
DR OMA; IYNKMIT; -.
DR OrthoDB; 1037602at2759; -.
DR PhylomeDB; Q6P3P5; -.
DR TreeFam; TF318639; -.
DR Reactome; R-XTR-913709; O-linked glycosylation of mucins.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000008143; Chromosome 5.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000025974; Expressed in egg cell and 15 other tissues.
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; IBA:GO_Central.
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; IBA:GO_Central.
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 Glycoprotein; Glycosyltransferase; Golgi apparatus; Lipid metabolism;
KW Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..377
FT /note="Lactosylceramide 1,3-N-acetyl-beta-D-
FT glucosaminyltransferase"
FT /id="PRO_0000289217"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..30
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 31..377
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 377 AA; 43330 MW; EA39668B455412AF CRC64;
MLISARRLRR CQFFQLLTSC FVLSLMALLV QEDNSLINHV KSYSYRYLIN SYDFVNDSLS
VPRDRPDGAP SYRYLINNRD KCQNEDVLLL LFVKTSPENR RRRNAIRKTW GNEDYIRSQY
AANIKVVFAL GIEADPVKSH QTQKDLVIEN KRFNDLIQQD FKDTFHNLTL KLLLQFGWVN
SYCPSAKFIM SADDDIFVHT PNLVSYLKSL PIETQDFWIG RVHRGSPPIR SKTSKYYVPY
EMYPWSSYPD YTAGAAYVVS KDVAAKVYEA SQTLNTSLYI DDVFMGICAN KMGVVPQYHV
YFAGEGKAPY HPCIYNKMIT SHGHLDDLDY LWRQATDPNV KSLSAGVLGG AYCKLVNIML
LCKLSYVDTY PCSAAWS
