B3G5A_DANRE
ID B3G5A_DANRE Reviewed; 379 AA.
AC Q7T3S5;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 112.
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=b3gnt5a; Synonyms=b3gnt5;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=14579371; DOI=10.1002/dvdy.10372;
RA Cao Y., Zhao J., Wang Y., Meng A.;
RT "Expression of zebrafish Lc3 synthase gene in embryonic lens requires
RT hedgehog signaling.";
RL Dev. Dyn. 228:308-312(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) 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 -!- DEVELOPMENTAL STAGE: Expressed in 2 distinct phases during the
CC embryogenesis. The early phase extends from late blastulation to the
CC completion of epiboly, during which the expression occurs in the
CC superficial layer of the embryos. The second phase of expression starts
CC during mid-segmentation and persists until day 3, during which the
CC expression occurs prominently in the developing lens.
CC {ECO:0000269|PubMed:14579371}.
CC -!- INDUCTION: Hedgehog signaling is required for expression in embryonic
CC lens. {ECO:0000269|PubMed:14579371}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC {ECO:0000305}.
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DR EMBL; AY292460; AAP42946.1; -; mRNA.
DR EMBL; BC075943; AAH75943.1; -; mRNA.
DR RefSeq; NP_942577.1; NM_198876.1.
DR AlphaFoldDB; Q7T3S5; -.
DR SMR; Q7T3S5; -.
DR STRING; 7955.ENSDARP00000117098; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR PaxDb; Q7T3S5; -.
DR Ensembl; ENSDART00000132365; ENSDARP00000117098; ENSDARG00000018971.
DR Ensembl; ENSDART00000191497; ENSDARP00000146890; ENSDARG00000018971.
DR GeneID; 336526; -.
DR KEGG; dre:336526; -.
DR CTD; 336526; -.
DR ZFIN; ZDB-GENE-030131-8470; b3gnt5a.
DR eggNOG; KOG2287; Eukaryota.
DR GeneTree; ENSGT00940000159676; -.
DR HOGENOM; CLU_036849_2_4_1; -.
DR InParanoid; Q7T3S5; -.
DR OMA; IYNKMIT; -.
DR OrthoDB; 1037602at2759; -.
DR PhylomeDB; Q7T3S5; -.
DR TreeFam; TF318639; -.
DR BRENDA; 2.4.1.206; 928.
DR Reactome; R-DRE-913709; O-linked glycosylation of mucins.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q7T3S5; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 11.
DR Bgee; ENSDARG00000018971; Expressed in granulocyte and 21 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..379
FT /note="Lactosylceramide 1,3-N-acetyl-beta-D-
FT glucosaminyltransferase A"
FT /id="PRO_0000289213"
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..379
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 277
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 379 AA; 43600 MW; 9438972318CCA25B CRC64;
MFMNCRRVKK WHFLQLLSMC CVMSVLMVCW EHVDHHVVSH VKSYSYRYLI NSYDFINKSL
SVSPEEAARF GSFPYLLDRR DVCKNKDVLL LLFVKSSPGN FKRRQAIRST WGNESYISQE
LGVVVKVVFA MGVRPDRSGH KTMQRELRKE HMAHHDLIQQ DFLDTFHNLT VKLLLQFRWT
HENCAHAHFL MSADDDVFIH VPNLVHYLQE LKSQNVRNLW VGHVHRGAPP VRKRDSKYYM
PFDMYQWSSY PDYTAGAGYV VSGDVAAKIY QATQSLNASM YIDDVFMGIC AIAAGVSPQE
HVYFSGEGKT PYHPCIYEKM ITSHGHEGDI RYLWKAATGP QVEGISSGLL GKLYCAAVKM
TLLCKPYFTN TYSCMAAFT
