B4GT5_DANRE
ID B4GT5_DANRE Reviewed; 381 AA.
AC Q3YL68; B3DJV1;
DT 16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2019, sequence version 2.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Beta-1,4-galactosyltransferase 5 {ECO:0000305};
DE Short=Beta-1,4-GalTase 5;
DE Short=Beta4Gal-T5;
DE Short=b4Gal-T5;
DE EC=2.4.1.-;
DE AltName: Full=Beta-1,4-GalT II {ECO:0000250|UniProtKB:O43286};
DE AltName: Full=Glucosylceramide beta-1,4-galactosyltransferase;
DE EC=2.4.1.274 {ECO:0000250|UniProtKB:O43286};
DE AltName: Full=Lactosylceramide synthase {ECO:0000250|UniProtKB:O43286};
DE Short=LacCer synthase {ECO:0000250|UniProtKB:O43286};
DE AltName: Full=UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 5;
DE AltName: Full=UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 5;
GN Name=b4galt5;
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], FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=16672343; DOI=10.1242/dev.02378;
RA Machingo Q.J., Fritz A., Shur B.D.;
RT "A beta1,4-galactosyltransferase is required for Bmp2-dependent patterning
RT of the dorsoventral axis during zebrafish embryogenesis.";
RL Development 133:2233-2241(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the synthesis of lactosylceramide (LacCer) via the
CC transfer of galactose from UDP-galactose to glucosylceramide (GlcCer)
CC (By similarity). Required for proper patterning of the dorsoventral
CC axis during embryogenesis through the regulation of BMP signaling
CC (PubMed:16672343). Plays a role in proteoglycan glycosylation that is
CC required for BMP-dependent specification of the dorsoventral axis
CC (PubMed:16672343). {ECO:0000250|UniProtKB:Q9JMK0,
CC ECO:0000269|PubMed:16672343}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine + UDP-alpha-D-
CC galactose = a beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-Cer(d18:1(4E)) +
CC H(+) + UDP; Xref=Rhea:RHEA:31495, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17950, ChEBI:CHEBI:22801, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:66914; EC=2.4.1.274;
CC Evidence={ECO:0000250|UniProtKB:Q9JMK0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31496;
CC Evidence={ECO:0000250|UniProtKB:Q9JMK0};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q9UBX8};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- PATHWAY: Sphingolipid metabolism.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000250|UniProtKB:P15291}; Single-pass type II membrane protein.
CC Golgi apparatus {ECO:0000250|UniProtKB:A0A1S6M251}. Note=Trans
CC cisternae of Golgi stack. {ECO:0000250|UniProtKB:P15291}.
CC -!- DEVELOPMENTAL STAGE: Expressed by the early epiboly stage and reaches a
CC steady state level of expression by mid-somitogenesis
CC (PubMed:16672343). Shows widespread expression throughout the embryo
CC during the first 24 hours of development, with enhanced expression
CC within several structures at the 20-somite stage (PubMed:16672343).
CC {ECO:0000269|PubMed:16672343}.
CC -!- DISRUPTION PHENOTYPE: Morpholino knockdown results in dorsalized
CC embryos which have ventrally expanded chordin expression and reduced
CC activation of the Bmp-dependent transcription factors smad1/5/8
CC (PubMed:16672343). Proteoglycans exhibits defective glycosylation and a
CC greatly reduced affinity for bmp2 (PubMed:16672343).
CC {ECO:0000269|PubMed:16672343}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 7 family. {ECO:0000305}.
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DR EMBL; DQ104219; AAZ80090.1; -; mRNA.
DR EMBL; FP017154; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; FP017188; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC163615; AAI63615.1; -; mRNA.
DR RefSeq; NP_001038797.1; NM_001045332.1.
DR AlphaFoldDB; Q3YL68; -.
DR SMR; Q3YL68; -.
DR STRING; 7955.ENSDARP00000055098; -.
DR CAZy; GT7; Glycosyltransferase Family 7.
DR Ensembl; ENSDART00000055099; ENSDARP00000055098; ENSDARG00000037815.
DR GeneID; 724080; -.
DR KEGG; dre:724080; -.
DR CTD; 9334; -.
DR ZFIN; ZDB-GENE-060628-3; b4galt5.
DR eggNOG; KOG3916; Eukaryota.
DR GeneTree; ENSGT00940000158138; -.
DR HOGENOM; CLU_044391_6_0_1; -.
DR OMA; LEVNMTE; -.
DR OrthoDB; 1201618at2759; -.
DR PhylomeDB; Q3YL68; -.
DR TreeFam; TF312834; -.
DR Reactome; R-DRE-2022854; Keratan sulfate biosynthesis.
DR Reactome; R-DRE-913709; O-linked glycosylation of mucins.
DR Reactome; R-DRE-975577; N-Glycan antennae elongation.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q3YL68; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 23.
DR Bgee; ENSDARG00000037815; Expressed in retina and 8 other tissues.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008378; F:galactosyltransferase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008489; F:UDP-galactose:glucosylceramide beta-1,4-galactosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0009950; P:dorsal/ventral axis specification; IMP:ZFIN.
DR GO; GO:0010706; P:ganglioside biosynthetic process via lactosylceramide; ISS:UniProtKB.
DR GO; GO:0009101; P:glycoprotein biosynthetic process; IBA:GO_Central.
DR GO; GO:0070085; P:glycosylation; IBA:GO_Central.
DR GO; GO:0048840; P:otolith development; IMP:ZFIN.
DR GO; GO:0030513; P:positive regulation of BMP signaling pathway; IMP:ZFIN.
DR GO; GO:0006486; P:protein glycosylation; ISS:UniProtKB.
DR GO; GO:0030166; P:proteoglycan biosynthetic process; IMP:ZFIN.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR003859; Galactosyl_T.
DR InterPro; IPR027791; Galactosyl_T_C.
DR InterPro; IPR027995; Galactosyl_T_N.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR19300; PTHR19300; 1.
DR Pfam; PF02709; Glyco_transf_7C; 1.
DR Pfam; PF13733; Glyco_transf_7N; 1.
DR PRINTS; PR02050; B14GALTRFASE.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Lipid biosynthesis; Lipid metabolism; Manganese; Membrane; Metal-binding;
KW Reference proteome; Signal-anchor; Sphingolipid metabolism; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..381
FT /note="Beta-1,4-galactosyltransferase 5"
FT /id="PRO_0000446109"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 12..32
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..381
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT BINDING 162..166
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250|UniProtKB:Q9UBV7"
FT BINDING 201..203
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250|UniProtKB:Q9UBV7"
FT BINDING 228..229
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250|UniProtKB:Q9UBV7"
FT BINDING 229
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q9UBV7"
FT BINDING 257
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250|UniProtKB:Q9UBV7"
FT BINDING 289
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250|UniProtKB:Q9UBV7"
FT BINDING 291..294
FT /ligand="N-acetyl-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:506227"
FT /evidence="ECO:0000250|UniProtKB:Q9UBV7"
FT BINDING 322..323
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250|UniProtKB:Q9UBV7"
FT BINDING 322
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q9UBV7"
FT BINDING 333
FT /ligand="N-acetyl-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:506227"
FT /evidence="ECO:0000250|UniProtKB:Q9UBV7"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 366
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 106..151
FT /evidence="ECO:0000250|UniProtKB:P15291"
FT DISULFID 222..241
FT /evidence="ECO:0000250|UniProtKB:P15291"
FT CONFLICT 76
FT /note="D -> E (in Ref. 1; AAZ80090)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 381 AA; 44335 MW; B86C17B99A31F533 CRC64;
MPTHLRFRRR SFLGLLFLFS LSTSALYFIY SAPGIVNEYL FMVQARGIQI RENVRNMGAQ
VLEQVVRSAY SINGTDYTYE FNFSETDASP TPFLPEGFTY KPEQVCPEKL PSMKGRLKVN
MSEIALDEVE KLLKLNDPGL SVGGHWKPHD CRPRWKVAIL VPFRNRHEHL PILFRHLIPA
LQRQRLQFGF YVIEQAGNEP FNRAMLFNVG FKEAMKDLNW DCVIFHDVDH ILENDRNYYG
CGEMPRHFAV KLNKYSYMLP YEEFFGGVSG LTVKQFKRIN GFPNAFWGWG GEDDDLWNRV
QFAGYKVSRP HGELGRYMSI PHHHRGEVQF LGRYKLLRRS KERQSLDGLN NLNYSPLVSR
RSLYTNVSVT LSRDLAPVAD Y
