ID   B3G5A_XENLA             Reviewed;         377 AA.
AC   Q5HZL5;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Lactosylceramide 1,3-N-acetyl-beta-D-glucosaminyltransferase A;
DE            EC=2.4.1.206 {ECO:0000250|UniProtKB:Q8BGY6};
DE   AltName: Full=Lactotriaosylceramide synthase A;
DE            Short=Lc(3)Cer synthase A;
DE            Short=Lc3 synthase A;
DE   AltName: Full=UDP-GlcNAc:beta-Gal beta-1,3-N-acetylglucosaminyltransferase 5A;
DE            Short=BGnT-5A;
DE            Short=Beta-1,3-Gn-T5A;
DE            Short=Beta-1,3-N-acetylglucosaminyltransferase 5A;
DE            Short=Beta3Gn-T5A;
GN   Name=b3gnt5-a;
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=Egg;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JAN-2005) 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; BC088967; AAH88967.1; -; mRNA.
DR   RefSeq; NP_001088982.1; NM_001095513.1.
DR   AlphaFoldDB; Q5HZL5; -.
DR   SMR; Q5HZL5; -.
DR   CAZy; GT31; Glycosyltransferase Family 31.
DR   DNASU; 496364; -.
DR   GeneID; 496364; -.
DR   KEGG; xla:496364; -.
DR   CTD; 496364; -.
DR   Xenbase; XB-GENE-955716; b3gnt5.L.
DR   OMA; FNTYPCK; -.
DR   OrthoDB; 1037602at2759; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000186698; Chromosome 5L.
DR   Bgee; 496364; 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 A"
FT                   /id="PRO_0000289215"
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;  43635 MW;  681E1E08AC0FD59B CRC64;
     MLISARRLRR CQFLQLLASC FVLSLMALLV QEDNSLISHV KSYSYRYLIN SYDFVNVSLS
     IPRDRLDGAA SYRYLLNNRH ICLNEDVLLL LFVKTAPENR RRRDAIRNTW GNEDFIRSQY
     DANIKVVFAL GAEGDPVKSR EIQQDLVNEN KRFKDLIQQD FSDTFHNLTL KLLLQFGWVN
     SFCPSAKFIM SADDDIFVHT PNLVSYLKSL PIETQDFWIG RVHRGSPPIR RKTSKYYVPY
     EMYPWSSYPD YTAGAAYVVS RDVAAKVYEA SQTLNTSLYI DDVFMGICAN KMGLVPQYHV
     FFSGEGKSPY HPCIYNKMMT SHGHLDDLDY LWRQAIDPNV KSISSGFWGN LYCRFVNIML
     LCRISYVDTY PCSAAWS