B4GT5_HUMAN
ID B4GT5_HUMAN Reviewed; 388 AA.
AC O43286; E1P625; Q2M394; Q9UJQ8; U6C5D7;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Beta-1,4-galactosyltransferase 5;
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:0000303|PubMed:9435216};
DE AltName: Full=Glucosylceramide beta-1,4-galactosyltransferase;
DE EC=2.4.1.274 {ECO:0000269|PubMed:24498430};
DE AltName: Full=Lactosylceramide synthase {ECO:0000303|PubMed:24498430};
DE Short=LacCer synthase {ECO:0000303|PubMed:24498430};
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 {ECO:0000312|HGNC:HGNC:928};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Mammary tumor;
RX PubMed=9435216; DOI=10.1073/pnas.95.2.472;
RA Sato T., Furukawa K., Bakker H., van den Eijnden D.H., van Die I.;
RT "Molecular cloning of a human cDNA encoding beta-1,4-galactosyltransferase
RT with 37% identity to mammalian UDP-Gal:GlcNAc beta-1,4-
RT galactosyltransferase.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:472-477(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9597550; DOI=10.1093/glycob/8.5.517;
RA Lo N.-W., Shaper J.H., Pevsner J., Shaper N.L.;
RT "The expanding beta 4-galactosyltransferase gene family: messages from the
RT databanks.";
RL Glycobiology 8:517-526(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum, and Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 4-382, AND FUNCTION AS GLUCOSYLCERAMIDE
RP BETA-1,4-GALACTOSYLTRANSFERASE.
RC TISSUE=Brain;
RX PubMed=24498430; DOI=10.1371/journal.pone.0088124;
RA Yamaji T., Hanada K.;
RT "Establishment of HeLa cell mutants deficient in sphingolipid-related genes
RT using TALENs.";
RL PLoS ONE 9:E88124-E88124(2014).
RN [7]
RP REVIEW.
RX PubMed=10580128; DOI=10.1016/s0304-4165(99)00168-3;
RA Amado M., Almeida R., Schwientek T., Clausen H.;
RT "Identification and characterization of large galactosyltransferase gene
RT families: galactosyltransferases for all functions.";
RL Biochim. Biophys. Acta 1473:35-53(1999).
RN [8]
RP INDUCTION.
RX PubMed=29415997; DOI=10.1038/s41419-017-0239-5;
RA Li S.F., Zhu C.S., Wang Y.M., Xie X.X., Xiao L.L., Zhang Z.C., Tang Q.Q.,
RA Li X.;
RT "Downregulation of beta1,4-galactosyltransferase 5 improves insulin
RT resistance by promoting adipocyte commitment and reducing inflammation.";
RL Cell Death Dis. 9:196-196(2018).
CC -!- FUNCTION: Catalyzes the synthesis of lactosylceramide (LacCer) via the
CC transfer of galactose from UDP-galactose to glucosylceramide (GlcCer)
CC (PubMed:24498430). LacCer is the starting point in the biosynthesis of
CC all gangliosides (membrane-bound glycosphingolipids) which play pivotal
CC roles in the CNS including neuronal maturation and axonal and myelin
CC formation (By similarity). Plays a role in the glycosylation of BMPR1A
CC and regulation of its protein stability (By similarity). Essential for
CC extraembryonic development during early embryogenesis (By similarity).
CC {ECO:0000250|UniProtKB:Q9JMK0, ECO:0000269|PubMed:24498430}.
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:0000269|PubMed:24498430};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31496;
CC Evidence={ECO:0000305|PubMed:24498430};
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 -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:9435216}.
CC -!- INDUCTION: Up-regulated in subcutaneous adipose tissue during obesity
CC and diabetes. {ECO:0000269|PubMed:29415997}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 7 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=Beta-1,4-
CC galactosyltransferase 5;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_440";
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DR EMBL; AB004550; BAA25006.1; -; mRNA.
DR EMBL; AF038663; AAC39736.1; -; mRNA.
DR EMBL; AL035683; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL162615; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW75653.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75654.1; -; Genomic_DNA.
DR EMBL; BC074821; AAH74821.1; -; mRNA.
DR EMBL; BC074873; AAH74873.1; -; mRNA.
DR EMBL; BC104987; AAI04988.1; -; mRNA.
DR EMBL; BC112265; AAI12266.1; -; mRNA.
DR EMBL; AB871482; BAO04294.2; -; mRNA.
DR CCDS; CCDS13420.1; -.
DR RefSeq; NP_004767.1; NM_004776.3.
DR AlphaFoldDB; O43286; -.
DR SMR; O43286; -.
DR BioGRID; 114743; 113.
DR IntAct; O43286; 18.
DR STRING; 9606.ENSP00000360776; -.
DR CAZy; GT7; Glycosyltransferase Family 7.
DR GlyGen; O43286; 8 sites.
DR iPTMnet; O43286; -.
DR PhosphoSitePlus; O43286; -.
DR SwissPalm; O43286; -.
DR BioMuta; B4GALT5; -.
DR EPD; O43286; -.
DR jPOST; O43286; -.
DR MassIVE; O43286; -.
DR MaxQB; O43286; -.
DR PaxDb; O43286; -.
DR PeptideAtlas; O43286; -.
DR PRIDE; O43286; -.
DR ProteomicsDB; 48857; -.
DR Antibodypedia; 28497; 176 antibodies from 26 providers.
DR DNASU; 9334; -.
DR Ensembl; ENST00000371711.4; ENSP00000360776.4; ENSG00000158470.5.
DR GeneID; 9334; -.
DR KEGG; hsa:9334; -.
DR MANE-Select; ENST00000371711.4; ENSP00000360776.4; NM_004776.4; NP_004767.1.
DR UCSC; uc002xuu.5; human.
DR CTD; 9334; -.
DR DisGeNET; 9334; -.
DR GeneCards; B4GALT5; -.
DR HGNC; HGNC:928; B4GALT5.
DR HPA; ENSG00000158470; Low tissue specificity.
DR MIM; 604016; gene.
DR neXtProt; NX_O43286; -.
DR OpenTargets; ENSG00000158470; -.
DR PharmGKB; PA25227; -.
DR VEuPathDB; HostDB:ENSG00000158470; -.
DR eggNOG; KOG3916; Eukaryota.
DR GeneTree; ENSGT00940000158019; -.
DR HOGENOM; CLU_044391_6_0_1; -.
DR InParanoid; O43286; -.
DR OMA; MSEISMD; -.
DR OrthoDB; 1201618at2759; -.
DR PhylomeDB; O43286; -.
DR TreeFam; TF312834; -.
DR BRENDA; 2.4.1.274; 2681.
DR BRENDA; 2.4.1.38; 2681.
DR BRENDA; 2.4.1.90; 2681.
DR PathwayCommons; O43286; -.
DR Reactome; R-HSA-2022854; Keratan sulfate biosynthesis.
DR Reactome; R-HSA-913709; O-linked glycosylation of mucins.
DR Reactome; R-HSA-975577; N-Glycan antennae elongation.
DR SignaLink; O43286; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 9334; 21 hits in 1079 CRISPR screens.
DR ChiTaRS; B4GALT5; human.
DR GeneWiki; B4GALT5; -.
DR GenomeRNAi; 9334; -.
DR Pharos; O43286; Tbio.
DR PRO; PR:O43286; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; O43286; protein.
DR Bgee; ENSG00000158470; Expressed in nasal cavity epithelium and 207 other tissues.
DR Genevisible; O43286; HS.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
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:0003945; F:N-acetyllactosamine synthase activity; IEA:Ensembl.
DR GO; GO:0008489; F:UDP-galactose:glucosylceramide beta-1,4-galactosyltransferase activity; IMP:UniProtKB.
DR GO; GO:0022010; P:central nervous system myelination; ISS:UniProtKB.
DR GO; GO:0021955; P:central nervous system neuron axonogenesis; ISS:UniProtKB.
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:0042551; P:neuron maturation; ISS:UniProtKB.
DR GO; GO:0016266; P:O-glycan processing; TAS:Reactome.
DR GO; GO:0030311; P:poly-N-acetyllactosamine biosynthetic process; IEA:Ensembl.
DR GO; GO:0040019; P:positive regulation of embryonic development; ISS:UniProtKB.
DR GO; GO:0006486; P:protein glycosylation; ISS:UniProtKB.
DR GO; GO:0031647; P:regulation of protein stability; ISS:UniProtKB.
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 1: Evidence at protein 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..388
FT /note="Beta-1,4-galactosyltransferase 5"
FT /id="PRO_0000080545"
FT TOPO_DOM 1..14
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 15..35
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 36..388
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT BINDING 169..173
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250|UniProtKB:Q9UBV7"
FT BINDING 208..210
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250|UniProtKB:Q9UBV7"
FT BINDING 235..236
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250|UniProtKB:Q9UBV7"
FT BINDING 236
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q9UBV7"
FT BINDING 264
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250|UniProtKB:Q9UBV7"
FT BINDING 296
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250|UniProtKB:Q9UBV7"
FT BINDING 298..301
FT /ligand="N-acetyl-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:506227"
FT /evidence="ECO:0000250|UniProtKB:Q9UBV7"
FT BINDING 329..330
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250|UniProtKB:Q9UBV7"
FT BINDING 329
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q9UBV7"
FT BINDING 340
FT /ligand="N-acetyl-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:506227"
FT /evidence="ECO:0000250|UniProtKB:Q9UBV7"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 364
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 373
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 114..158
FT /evidence="ECO:0000250|UniProtKB:P15291"
FT DISULFID 229..248
FT /evidence="ECO:0000250|UniProtKB:P15291"
FT VARIANT 61
FT /note="G -> S (in dbSNP:rs2273086)"
FT /id="VAR_024468"
FT VARIANT 368
FT /note="D -> N (in dbSNP:rs235035)"
FT /id="VAR_054022"
FT VARIANT 371
FT /note="Y -> D (in dbSNP:rs35195217)"
FT /id="VAR_033538"
SQ SEQUENCE 388 AA; 45119 MW; A71F3F8999B6E13A CRC64;
MRARRGLLRL PRRSLLAALF FFSLSSSLLY FVYVAPGIVN TYLFMMQAQG ILIRDNVRTI
GAQVYEQVLR SAYAKRNSSV NDSDYPLDLN HSETFLQTTT FLPEDFTYFA NHTCPERLPS
MKGPIDINMS EIGMDYIHEL FSKDPTIKLG GHWKPSDCMP RWKVAILIPF RNRHEHLPVL
FRHLLPMLQR QRLQFAFYVV EQVGTQPFNR AMLFNVGFQE AMKDLDWDCL IFHDVDHIPE
SDRNYYGCGQ MPRHFATKLD KYMYLLPYTE FFGGVSGLTV EQFRKINGFP NAFWGWGGED
DDLWNRVQNA GYSVSRPEGD TGKYKSIPHH HRGEVQFLGR YALLRKSKER QGLDGLNNLN
YFANITYDAL YKNITVNLTP ELAQVNEY
