ID   B3G5B_DANRE             Reviewed;         382 AA.
AC   Q5XJP0;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=b3gnt5b; ORFNames=zgc:101733;
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 [LARGE SCALE MRNA].
RC   TISSUE=Olfactory epithelium;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (OCT-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; BC083259; AAH83259.1; -; mRNA.
DR   AlphaFoldDB; Q5XJP0; -.
DR   SMR; Q5XJP0; -.
DR   STRING; 7955.ENSDARP00000123385; -.
DR   PaxDb; Q5XJP0; -.
DR   ZFIN; ZDB-GENE-041010-166; b3gnt5b.
DR   eggNOG; KOG2287; Eukaryota.
DR   InParanoid; Q5XJP0; -.
DR   UniPathway; UPA00378; -.
DR   PRO; PR:Q5XJP0; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
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: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..382
FT                   /note="Lactosylceramide 1,3-N-acetyl-beta-D-
FT                   glucosaminyltransferase B"
FT                   /id="PRO_0000289214"
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..382
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        57
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        112
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        276
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   382 AA;  44550 MW;  9055FC99BAB9FF1D CRC64;
     MAVLKMPRFK KYHLRLMITC FSTLLLMTYW EKIDNCVVTH VMSFSYRYLF NSFKFINSSF
     IVNPEDAIKY NHRYLINHQT KCDNKDILLL LFVKSSSENF ERRQAIRSTW GNETYIESTL
     GVTVKVLFAL GLHPIPEERG KLKEDLMFED QKYRDLIQQD FIDTFHNLTL KLLLQLGWKE
     TYCHHAQFLM SADDDVFVHT PNLILYLQGF GQSNTRDLWI GGVHRGSPPN RDKESKYYVS
     RDLYPWLSYP DYTPGSGYVL SRDVVSRIYQ ASLTINASFH IDDVFLGICA KMMDVSPTDH
     AFFSGEGKAP HHHCIYSLMM TSHGHVSDIH EMWRHARNAE DVLISSGLFR RLYCTAVKVR
     LLCVPFFSNS YPCKAAFFEE DT