ID   B3G5B_XENLA             Reviewed;         377 AA.
AC   Q6DE15;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Lactosylceramide 1,3-N-acetyl-beta-D-glucosaminyltransferase B;
DE            EC=2.4.1.206 {ECO:0000250|UniProtKB:Q8BGY6};
DE   AltName: Full=Lactotriaosylceramide synthase B;
DE            Short=Lc(3)Cer synthase B;
DE            Short=Lc3 synthase B;
DE   AltName: Full=UDP-GlcNAc:beta-Gal beta-1,3-N-acetylglucosaminyltransferase 5B;
DE            Short=BGnT-5B;
DE            Short=Beta-1,3-Gn-T5B;
DE            Short=Beta-1,3-N-acetylglucosaminyltransferase 5B;
DE            Short=Beta3Gn-T5B;
GN   Name=b3gnt5-b;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUL-2004) 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}.
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DR   EMBL; BC077332; AAH77332.1; -; mRNA.
DR   RefSeq; NP_001086705.1; NM_001093236.1.
DR   AlphaFoldDB; Q6DE15; -.
DR   SMR; Q6DE15; -.
DR   CAZy; GT31; Glycosyltransferase Family 31.
DR   PRIDE; Q6DE15; -.
DR   DNASU; 446540; -.
DR   GeneID; 446540; -.
DR   KEGG; xla:446540; -.
DR   CTD; 446540; -.
DR   Xenbase; XB-GENE-6255936; b3gnt5.S.
DR   OrthoDB; 1037602at2759; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000186698; Chromosome 5S.
DR   Bgee; 446540; Expressed in egg cell and 19 other tissues.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
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; IEA:RHEA.
DR   GO; GO:0047256; F:lactosylceramide 1,3-N-acetyl-beta-D-glucosaminyltransferase activity; IEA:UniProtKB-EC.
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; Membrane;
KW   Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..377
FT                   /note="Lactosylceramide 1,3-N-acetyl-beta-D-
FT                   glucosaminyltransferase B"
FT                   /id="PRO_0000289216"
FT   TOPO_DOM        1..13
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        14..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;  43295 MW;  DC4D36670DFC049D CRC64;
     MLISARRLRR CQSLQLLASC FVLSLMALLV QEDNSLVNHV KSYSYRYLIN SYNFVNDSLS
     VPRDRSDGAA GYRYLINNRH KCLNEDVLLL LFVKTAPENR RRRNAIRKTW GNEDYIRSRY
     AANIKVVFAL GVERDPVKSH HTQQDLVNEN KRFKDLIQQD FSDTFHNLTL KLLLQFGWVN
     SFCPSAKFIM SADDDIFVHT PNLVTYLKSL PIETQDFWIG RVHRGSPPIR SKASKYYVPY
     EMYPWSSYPD YTAGAAYVVS RDVAAKVYEA SQTLNTSLYI DDVFMGICAN KMGVVPQYHV
     YFSGEGKSPY HPCIYNKMMT SHGHLGDLDY LWRQATDSNV KSLSSGFLGN VYCKIVNIML
     LCKIGYVDTY PCSAAWS