BRE2_CAEEL
ID BRE2_CAEEL Reviewed; 359 AA.
AC Q6QMT2; Q9U2K3;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Beta-1,3-galactosyltransferase bre-2;
DE EC=2.4.1.-;
DE AltName: Full=Bacillus thuringiensis toxin-resistant protein 2;
DE Short=Bt toxin-resistant protein 2;
GN Name=bre-2 {ECO:0000312|EMBL:AAS21306.1}; ORFNames=Y39E4B.9;
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:AAS21306.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), FUNCTION, MUTAGENESIS OF ARG-106,
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 [2] {ECO:0000305, ECO:0000312|EMBL:CAP16292.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:CAP16292.1};
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 [3]
RP FUNCTION, AND MUTAGENESIS OF ARG-106.
RX PubMed=20062796; DOI=10.1371/journal.ppat.1000717;
RA Butschi A., Titz A., Waelti M.A., Olieric V., Paschinger K., Noebauer K.,
RA Guo X., Seeberger P.H., Wilson I.B., Aebi M., Hengartner M.O., Kuenzler M.;
RT "Caenorhabditis elegans N-glycan core beta-galactoside confers sensitivity
RT towards nematotoxic fungal galectin CGL2.";
RL PLoS Pathog. 6:E1000717-E1000717(2010).
CC -!- FUNCTION: Transfers N-acetylgalactosamine onto carbohydrate substrates
CC (By similarity). Involved in susceptibility to pore-forming crystal
CC toxins in conjunction with bre-1, bre-3, bre-4, and bre-5
CC (PubMed:12944392). Involved in resistance to the nematotoxic C.cinerea
CC galectin Cgl2 (PubMed:20062796). {ECO:0000250|UniProtKB:Q95US5,
CC ECO:0000269|PubMed:12944392, ECO:0000269|PubMed:20062796}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:Q9Y5Z6}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000255,
CC ECO:0000305}; Single-pass type II membrane protein {ECO:0000255,
CC ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=b {ECO:0000269|PubMed:12944392};
CC IsoId=Q6QMT2-1; Sequence=Displayed;
CC Name=a {ECO:0000269|PubMed:9851916};
CC IsoId=Q6QMT2-2; Sequence=VSP_052711, VSP_052712;
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:12944392}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC {ECO:0000255}.
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DR EMBL; AY533304; AAS21306.1; -; mRNA.
DR EMBL; AL110487; CAB54430.2; -; Genomic_DNA.
DR EMBL; AL110487; CAP16292.1; -; Genomic_DNA.
DR RefSeq; NP_001122728.1; NM_001129256.1.
DR RefSeq; NP_499715.2; NM_067314.2. [Q6QMT2-2]
DR AlphaFoldDB; Q6QMT2; -.
DR SMR; Q6QMT2; -.
DR STRING; 6239.Y39E4B.9c; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR PaxDb; Q6QMT2; -.
DR EnsemblMetazoa; Y39E4B.9a.1; Y39E4B.9a.1; WBGene00000267. [Q6QMT2-2]
DR EnsemblMetazoa; Y39E4B.9a.2; Y39E4B.9a.2; WBGene00000267. [Q6QMT2-2]
DR EnsemblMetazoa; Y39E4B.9b.1; Y39E4B.9b.1; WBGene00000267. [Q6QMT2-1]
DR GeneID; 189753; -.
DR UCSC; Y39E4B.9b; c. elegans. [Q6QMT2-1]
DR CTD; 189753; -.
DR WormBase; Y39E4B.9a; CE36339; WBGene00000267; bre-2. [Q6QMT2-2]
DR WormBase; Y39E4B.9b; CE21720; WBGene00000267; bre-2. [Q6QMT2-1]
DR eggNOG; KOG2287; Eukaryota.
DR GeneTree; ENSGT00940000161798; -.
DR HOGENOM; CLU_045590_0_0_1; -.
DR InParanoid; Q6QMT2; -.
DR PhylomeDB; Q6QMT2; -.
DR Reactome; R-CEL-1660662; Glycosphingolipid metabolism.
DR Reactome; R-CEL-9037629; Lewis blood group biosynthesis.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q6QMT2; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00000267; Expressed in larva and 3 other tissues.
DR ExpressionAtlas; Q6QMT2; baseline.
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:0008375; F:acetylglucosaminyltransferase activity; ISS:UniProtKB.
DR GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR GO; GO:0009636; P:response to toxic substance; IMP:UniProtKB.
DR InterPro; IPR002659; Glyco_trans_31.
DR PANTHER; PTHR11214; PTHR11214; 1.
DR Pfam; PF01762; Galactosyl_T; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Insecticide resistance; Membrane; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..359
FT /note="Beta-1,3-galactosyltransferase bre-2"
FT /id="PRO_0000324667"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..29
FT /note="Helical; Signal-anchor for type II membrane protein"
FT TOPO_DOM 30..359
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 282..304
FT /note="DVFITGLLAGDVGIKKNQLPFMY -> KLLKMCSLLACLPATLGSKKINFHL
FT CI (in isoform a)"
FT /evidence="ECO:0000303|PubMed:9851916"
FT /id="VSP_052711"
FT VAR_SEQ 305..359
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000303|PubMed:9851916"
FT /id="VSP_052712"
FT MUTAGEN 106
FT /note="R->Q: In ye31; resistant to Bacillus thuringiensis
FT crystal5B toxin. Susceptible to C.cinerea galectin Cgl2."
FT /evidence="ECO:0000269|PubMed:12944392,
FT ECO:0000269|PubMed:20062796"
SQ SEQUENCE 359 AA; 41370 MW; 14C2C7CAF2AEF025 CRC64;
MRQSRRASSR VNRLVVIFII VASGFLLLYK NTQQFTQIDR ECIQDEWQEN NNLGNTIDDG
SNFRIAFTDI QQNYTWLHLP NFLENSEILM IVSSNCDNFA RRNILRKTWM NPENSQIIGD
GRMKALFLVG INGADEKLNA VVLEEAKVFG DMIVIDLEDN YLNLSYKTIS LLLYSISKTK
SPNLIGKIDE DVLFYPDQLT PLINDKTINT STFSIYGEKY EAGVAVNHGE DNAKWQISKN
SFKCSVYPSY LSGPTYFLTR KAAKRIVEAT KHRKFISVDV EDVFITGLLA GDVGIKKNQL
PFMYMIEEAT NDRESYEILA WHTKKRDQQY IEAFESLKLN RCKSCRKSKN PDLEELKEK
