BRE4_CAEEL
ID BRE4_CAEEL Reviewed; 383 AA.
AC Q9GUM2; W6SB74;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Beta-1,4-N-acetylgalactosaminyltransferase bre-4;
DE EC=2.4.1.-;
DE AltName: Full=Bacillus thuringiensis toxin-resistant protein 4;
DE Short=Bt toxin-resistant protein 4;
DE AltName: Full=Beta-4-GalNAcT;
GN Name=bre-4 {ECO:0000312|WormBase:Y73E7A.7a}; ORFNames=Y73E7A.7;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAM95168.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, AND PATHWAY.
RX PubMed=12167666; DOI=10.1074/jbc.m206112200;
RA Kawar Z.S., Van Die I., Cummings R.D.;
RT "Molecular cloning and enzymatic characterization of a UDP-
RT GalNAc:GlcNAc(beta)-R beta1,4-N-acetylgalactosaminyltransferase from
RT Caenorhabditis elegans.";
RL J. Biol. Chem. 277:34924-34932(2002).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAS21308.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, MUTAGENESIS OF GLY-260,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=12944392; DOI=10.1074/jbc.m308142200;
RA Griffitts J.S., Huffman D.L., Whitacre J.L., Barrows B.D., Marroquin L.D.,
RA Mueller R., Brown J.R., Hennet T., Esko J.D., Aroian R.V.;
RT "Resistance to a bacterial toxin is mediated by removal of a conserved
RT glycosylation pathway required for toxin-host interactions.";
RL J. Biol. Chem. 278:45594-45602(2003).
RN [3] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [4] {ECO:0000305}
RP IDENTIFICATION, FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=10924467; DOI=10.1093/genetics/155.4.1693;
RA Marroquin L.D., Elyassnia D., Griffitts J.S., Feitelson J.S., Aroian R.V.;
RT "Bacillus thuringiensis (Bt) toxin susceptibility and isolation of
RT resistance mutants in the nematode Caenorhabditis elegans.";
RL Genetics 155:1693-1699(2000).
CC -!- FUNCTION: Catalyzes the transfer of galactose onto proteins or lipids.
CC Required for susceptibility to pore-forming crystal toxins in
CC conjunction with bre-1, bre-2, bre-3 and bre-5.
CC {ECO:0000269|PubMed:10924467, ECO:0000269|PubMed:12167666,
CC ECO:0000269|PubMed:12944392}.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P08037};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:12167666, ECO:0000269|PubMed:12944392}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type II
CC membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=Q9GUM2-1; Sequence=Displayed;
CC Name=b;
CC IsoId=Q9GUM2-2; Sequence=VSP_054965;
CC -!- DISRUPTION PHENOTYPE: Worms exhibit resistance to the Cry5B toxin
CC produced by Bacillus thuringiensis. This is thought to be due to
CC mutants having reduced population of glycolipids which are targeted by
CC the Cry5B protein. {ECO:0000269|PubMed:10924467,
CC ECO:0000269|PubMed:12944392}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 7 family. {ECO:0000255}.
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DR EMBL; AY130767; AAM95168.1; -; mRNA.
DR EMBL; AY533306; AAS21308.1; -; mRNA.
DR EMBL; FO081821; CCD73531.1; -; Genomic_DNA.
DR EMBL; FO081821; CDM63463.1; -; Genomic_DNA.
DR RefSeq; NP_001293407.1; NM_001306478.1.
DR RefSeq; NP_490872.1; NM_058471.1. [Q9GUM2-1]
DR AlphaFoldDB; Q9GUM2; -.
DR SMR; Q9GUM2; -.
DR BioGRID; 55247; 1.
DR STRING; 6239.Y73E7A.7; -.
DR CAZy; GT7; Glycosyltransferase Family 7.
DR EPD; Q9GUM2; -.
DR PaxDb; Q9GUM2; -.
DR PeptideAtlas; Q9GUM2; -.
DR EnsemblMetazoa; Y73E7A.7a.1; Y73E7A.7a.1; WBGene00000269. [Q9GUM2-1]
DR EnsemblMetazoa; Y73E7A.7a.2; Y73E7A.7a.2; WBGene00000269. [Q9GUM2-1]
DR EnsemblMetazoa; Y73E7A.7b.1; Y73E7A.7b.1; WBGene00000269. [Q9GUM2-2]
DR GeneID; 190668; -.
DR KEGG; cel:CELE_Y73E7A.7; -.
DR UCSC; Y73E7A.7; c. elegans. [Q9GUM2-1]
DR CTD; 190668; -.
DR WormBase; Y73E7A.7a; CE26412; WBGene00000269; bre-4. [Q9GUM2-1]
DR WormBase; Y73E7A.7b; CE49566; WBGene00000269; bre-4. [Q9GUM2-2]
DR eggNOG; KOG3916; Eukaryota.
DR GeneTree; ENSGT00940000163971; -.
DR HOGENOM; CLU_044391_3_1_1; -.
DR InParanoid; Q9GUM2; -.
DR OMA; YSCPEQP; -.
DR OrthoDB; 1201618at2759; -.
DR PhylomeDB; Q9GUM2; -.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR Reactome; R-CEL-913709; O-linked glycosylation of mucins.
DR Reactome; R-CEL-975577; N-Glycan antennae elongation.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q9GUM2; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00000269; Expressed in adult organism and 4 other tissues.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008376; F:acetylgalactosaminyltransferase activity; IDA:UniProtKB.
DR GO; GO:0033207; F:beta-1,4-N-acetylgalactosaminyltransferase activity; IDA:WormBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0070085; P:glycosylation; IBA:GO_Central.
DR GO; GO:0045747; P:positive regulation of Notch signaling pathway; IGI:WormBase.
DR GO; GO:0006486; P:protein glycosylation; IDA:WormBase.
DR GO; GO:0009636; P:response to toxic substance; IMP:WormBase.
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 Alternative splicing; Disulfide bond; Glycoprotein; Glycosyltransferase;
KW Insecticide resistance; Manganese; Membrane; Metal-binding;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..383
FT /note="Beta-1,4-N-acetylgalactosaminyltransferase bre-4"
FT /id="PRO_0000324671"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..29
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..383
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT BINDING 222
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P08037"
FT BINDING 315
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P08037"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 71
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 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 103..144
FT /evidence="ECO:0000250|UniProtKB:P08037"
FT DISULFID 215..234
FT /evidence="ECO:0000250|UniProtKB:P08037"
FT VAR_SEQ 1..165
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_054965"
FT MUTAGEN 260
FT /note="G->R: In ye43; resistant to Bacillus thuringiensis
FT crystal5B toxin."
FT /evidence="ECO:0000269|PubMed:12944392"
SQ SEQUENCE 383 AA; 43914 MW; ADEDFA4275B2CE81 CRC64;
MAFRHLAVAR LKSLLVLCAV LLLVHAMIYK IPSLYENLTI GSSTLIADVD AMEAVLGNTA
STSDDLLDTW NSTFSPISEV NQTSFMEDIR PILFPDNQTL QFCNQTPPHL VGPIRVFLDE
PDFKTLEKIY PDTHAGGHGM PKDCVARHRV AIIVPYRDRE AHLRIMLHNL HSLLAKQQLD
YAIFIVEQVA NQTFNRGKLM NVGYDVASRL YPWQCFIFHD VDLLPEDDRN LYTCPIQPRH
MSVAIDKFNY KLPYSAIFGG ISALTKDHLK KINGFSNDFW GWGGEDDDLA TRTSMAGLKV
SRYPTQIARY KMIKHSTEAT NPVNKCRYKI MGQTKRRWTR DGLSNLKYKL VNLELKPLYT
RAVVDLLEKD CRRELRRDFP TCF
