B3GT5_MOUSE
ID B3GT5_MOUSE Reviewed; 308 AA.
AC Q9JI67;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Beta-1,3-galactosyltransferase 5 {ECO:0000305};
DE Short=Beta-1,3-GalTase 5;
DE Short=Beta3Gal-T5;
DE Short=Beta3GalT5;
DE Short=b3Gal-T5;
DE EC=2.4.1.-;
DE AltName: Full=Beta-3-Gx-T5;
DE AltName: Full=Stage-specific embryonic antigen 3 synthase;
DE Short=SSEA-3 synthase;
DE AltName: Full=UDP-Gal:beta-GlcNAc beta-1,3-galactosyltransferase 5;
DE AltName: Full=UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase 5;
GN Name=B3galt5 {ECO:0000312|MGI:MGI:2136878}; Synonyms=B3gt5;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvJ;
RX PubMed=10837462; DOI=10.1074/jbc.c000263200;
RA Zhou D., Henion T.R., Jungalwala F.B., Berger E.G., Hennet T.;
RT "The beta1,3-galactosyltransferase beta3GalT-V is a stage-specific
RT embryonic antigen-3 (SSEA-3) synthase.";
RL J. Biol. Chem. 275:22631-22634(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
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).
CC -!- FUNCTION: Catalyzes the transfer of Gal to GlcNAc-based acceptors with
CC a preference for the core3 O-linked glycan GlcNAc(beta1,3)GalNAc
CC structure. Can use glycolipid LC3Cer as an efficient acceptor. Also
CC catalyzes the transfer of Gal to the terminal GalNAc unit of the
CC globoside GB4, thereby synthesizing the glycolipid GB5, also known as
CC the stage-specific embryonic antigen-3 (SSEA-3).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=globoside Gb4Cer (d18:1(4E)) + UDP-alpha-D-galactose =
CC globoside GalGb4Cer (d18:1(4E)) + H(+) + UDP; Xref=Rhea:RHEA:41996,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:18259, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:62571, ChEBI:CHEBI:66914;
CC Evidence={ECO:0000250|UniProtKB:Q9Y2C3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41997;
CC Evidence={ECO:0000250|UniProtKB:Q9Y2C3};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC pass type II membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in brain and kidney.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=b3GalT5;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_458";
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DR EMBL; AF254738; AAF86241.1; -; Genomic_DNA.
DR EMBL; BC057887; AAH57887.1; -; mRNA.
DR CCDS; CCDS28356.1; -.
DR RefSeq; NP_001116465.1; NM_001122993.1.
DR RefSeq; NP_149161.1; NM_033149.3.
DR RefSeq; XP_006523179.1; XM_006523116.3.
DR RefSeq; XP_006523180.1; XM_006523117.1.
DR RefSeq; XP_017172660.1; XM_017317171.1.
DR AlphaFoldDB; Q9JI67; -.
DR SMR; Q9JI67; -.
DR STRING; 10090.ENSMUSP00000109431; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR GlyGen; Q9JI67; 3 sites.
DR PhosphoSitePlus; Q9JI67; -.
DR MaxQB; Q9JI67; -.
DR PaxDb; Q9JI67; -.
DR PRIDE; Q9JI67; -.
DR ProteomicsDB; 277153; -.
DR Antibodypedia; 23457; 109 antibodies from 24 providers.
DR DNASU; 93961; -.
DR Ensembl; ENSMUST00000099497; ENSMUSP00000097096; ENSMUSG00000074892.
DR Ensembl; ENSMUST00000113800; ENSMUSP00000109431; ENSMUSG00000074892.
DR GeneID; 93961; -.
DR KEGG; mmu:93961; -.
DR UCSC; uc008acv.2; mouse.
DR CTD; 10317; -.
DR MGI; MGI:2136878; B3galt5.
DR VEuPathDB; HostDB:ENSMUSG00000074892; -.
DR eggNOG; KOG2287; Eukaryota.
DR GeneTree; ENSGT00940000160964; -.
DR HOGENOM; CLU_036849_2_4_1; -.
DR InParanoid; Q9JI67; -.
DR OMA; RFNKWFV; -.
DR OrthoDB; 1037602at2759; -.
DR PhylomeDB; Q9JI67; -.
DR TreeFam; TF318639; -.
DR Reactome; R-MMU-9037629; Lewis blood group biosynthesis.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 93961; 3 hits in 74 CRISPR screens.
DR ChiTaRS; B3galt5; mouse.
DR PRO; PR:Q9JI67; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q9JI67; protein.
DR Bgee; ENSMUSG00000074892; Expressed in left colon and 116 other tissues.
DR Genevisible; Q9JI67; MM.
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:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0008499; F:UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase activity; IBA:GO_Central.
DR GO; GO:0008194; F:UDP-glycosyltransferase activity; 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 GO; GO:0009617; P:response to bacterium; IEP:MGI.
DR InterPro; IPR002659; Glyco_trans_31.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR11214; PTHR11214; 1.
DR Pfam; PF01762; Galactosyl_T; 1.
DR SUPFAM; SSF53448; SSF53448; 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..308
FT /note="Beta-1,3-galactosyltransferase 5"
FT /id="PRO_0000219165"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..25
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 26..308
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 308 AA; 35964 MW; 789073A5178825B1 CRC64;
MAHMKTRLVY ASILMMGALC LYFSMDSFRE LPFVFKKSHG KFLQIPDIDC KQKPPFLVLL
VTSSHKQLAA RMAIRKTWGR ETSVQGQQVR TFFLLGTSDS TEEMDATTLE SEQHRDIIQK
DFKDAYFNLT LKTMMGMEWV YHFCPQTAYV MKTDSDMFVN VGYLTELLLK KNKTTRFFTG
YIKPHDFPIR QKFNKWFVSK FEYPWDRYPP FCSGTGYVFS SDVAIQVYNV SESVPFIKLE
DVFVGLCLAK LKIRPEELHT KQTFFPGGLR FSVCRFQKIV ACHFMKPQDL LTYWQALENS
KEQDCPAV
