B4GT5_PIG
ID B4GT5_PIG Reviewed; 388 AA.
AC A0A1S6M251; A0A287B5B9;
DT 16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2019, sequence version 2.
DT 03-AUG-2022, entry version 22.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION (MICROBIAL INFECTION), SUBCELLULAR
RP LOCATION, INTERACTION WITH PORCINE REPRODUCTIVE AND RESPIRATORY SYNDROME
RP VIRUS GP5 (MICROBIAL INFECTION), AND INDUCTION (MICROBIAL INFECTION).
RC TISSUE=Alveolar macrophage;
RX PubMed=29546034; DOI=10.3389/fcimb.2018.00048;
RA Zhang L., Ren J., Shi P., Lu D., Zhao C., Su Y., Zhang L., Huang J.;
RT "The immunological regulation roles of porcine beta-1, 4
RT Galactosyltransferase V (B4GALT5) in PRRSV Infection.";
RL Front. Cell. Infect. Microbiol. 8:48-48(2018).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) 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). 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}.
CC -!- FUNCTION: (Microbial infection) May play a role in the glycosylation of
CC porcine reproductive and respiratory syndrome virus GP5 protein and may
CC be involved in the regulation of viral proliferation.
CC {ECO:0000269|PubMed:29546034}.
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 -!- SUBUNIT: (Microbial infection) Interacts with porcine reproductive and
CC respiratory syndrome virus GP5. {ECO:0000269|PubMed:29546034}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000250|UniProtKB:P15291}; Single-pass type II membrane protein.
CC Golgi apparatus {ECO:0000269|PubMed:29546034}. Note=Trans cisternae of
CC Golgi stack. {ECO:0000250|UniProtKB:P15291}.
CC -!- INDUCTION: (Microbial infection) Up-regulated in response to porcine
CC reproductive and respiratory syndrome viral infection.
CC {ECO:0000269|PubMed:29546034}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 7 family. {ECO:0000305}.
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DR EMBL; KY565579; AQU14360.1; -; mRNA.
DR EMBL; AEMK02000106; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003134538.1; XM_003134490.4.
DR AlphaFoldDB; A0A1S6M251; -.
DR SMR; A0A1S6M251; -.
DR STRING; 9823.ENSSSCP00000007952; -.
DR Ensembl; ENSSSCT00000008169; ENSSSCP00000007952; ENSSSCG00000007465.
DR Ensembl; ENSSSCT00025106169; ENSSSCP00025047608; ENSSSCG00025076572.
DR Ensembl; ENSSSCT00035034067; ENSSSCP00035013457; ENSSSCG00035025847.
DR Ensembl; ENSSSCT00045006200; ENSSSCP00045004194; ENSSSCG00045003733.
DR Ensembl; ENSSSCT00055050054; ENSSSCP00055039991; ENSSSCG00055025271.
DR Ensembl; ENSSSCT00070034393; ENSSSCP00070028732; ENSSSCG00070017416.
DR GeneID; 100522653; -.
DR KEGG; ssc:100522653; -.
DR CTD; 9334; -.
DR VGNC; VGNC:96499; B4GALT5.
DR eggNOG; KOG3916; Eukaryota.
DR GeneTree; ENSGT00940000158019; -.
DR OrthoDB; 1201618at2759; -.
DR BRENDA; 2.4.1.274; 6170.
DR Reactome; R-SSC-2022854; Keratan sulfate biosynthesis.
DR Reactome; R-SSC-913709; O-linked glycosylation of mucins.
DR Reactome; R-SSC-975577; N-Glycan antennae elongation.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000008227; Chromosome 17.
DR Proteomes; UP000314985; Chromosome 17.
DR Bgee; ENSSSCG00000007465; Expressed in caecum and 42 other tissues.
DR ExpressionAtlas; A0A1S6M251; baseline and differential.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
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:0003945; F:N-acetyllactosamine synthase activity; IEA:Ensembl.
DR GO; GO:0008489; F:UDP-galactose:glucosylceramide beta-1,4-galactosyltransferase activity; ISS: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; IDA:UniProtKB.
DR GO; GO:0042551; P:neuron maturation; ISS:UniProtKB.
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_0000446108"
FT TOPO_DOM 1..14
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
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:0000305"
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 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 CONFLICT 57
FT /note="M -> T (in Ref. 1; AQU14360)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 388 AA; 45046 MW; 853112C7163502C1 CRC64;
MRVRRGLLRL PRRSLLAALF FFSLSSSLLY FVYVAPGIVN TYLFMMQAQG ILIRDNMRTI
GAQVYEQVVR SAYAKRNSSV NDSDYPLDLN HSETFLQTTT FLPEDFTYFA NHTCPERLPS
MKGPIDINMS EIGMDTIHEL FSKDPAIKLG GHWKPSDCVP RWKVAILIPF RNRHEHLPVL
LRHLIPMLQR QRLQFAFYVV EQVGTQPFNR AMLFNVGFQE AMKDLDWDCL VFHDVDHIPE
NDRNYYGCGQ MPRHFATKLD KYMYLLPYNE FFGGVSGLTV EQFRKINGFP NAFWGWGGED
DDLWNRVQNA GYSVSRPEGD TGKYKSIPYH HRGEVQFLGR YALLRKSKER QGLDGLNNLN
YFANITYDAL YKNITVNLTP ELAQVTEY
