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BRE5_CAEEL
ID   BRE5_CAEEL              Reviewed;         322 AA.
AC   Q95US5;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Beta-1,3-galactosyltransferase bre-5;
DE            EC=2.4.1.-;
DE   AltName: Full=Bacillus thuringiensis toxin-resistant protein 5;
DE            Short=Bt toxin-resistant protein 5;
GN   Name=bre-5 {ECO:0000312|EMBL:AAK72094.1}; ORFNames=T12G3.8;
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:AAK72094.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, MUTAGENESIS OF
RP   ARG-97, AND DISRUPTION PHENOTYPE.
RX   PubMed=11486087; DOI=10.1126/science.1062441;
RA   Griffitts J.S., Whitacre J.L., Stevens D.E., Aroian R.V.;
RT   "Bt toxin resistance from loss of a putative carbohydrate-modifying
RT   enzyme.";
RL   Science 293:860-864(2001).
RN   [2] {ECO:0000305, ECO:0000312|EMBL:CAD27607.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {ECO:0000312|EMBL:CAD27607.1};
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] {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).
RN   [4] {ECO:0000305}
RP   FUNCTION.
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   [5]
RP   FUNCTION.
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 mannose groups of
CC       carbohydrate substrates. Required for susceptibility to pore-forming
CC       crystal toxins in conjunction with bre-1, bre-2, bre-3, and bre-4.
CC       Involved in resistance to the nematotoxic C.cinerea galectin Cgl2
CC       (PubMed:20062796). {ECO:0000269|PubMed:10924467,
CC       ECO:0000269|PubMed:11486087, ECO:0000269|PubMed:12944392,
CC       ECO:0000269|PubMed:20062796}.
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000269|PubMed:11486087}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000255,
CC       ECO:0000305}; Single-pass type II membrane protein {ECO:0000255,
CC       ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in the gut.
CC       {ECO:0000269|PubMed:11486087}.
CC   -!- DISRUPTION PHENOTYPE: Worms exhibit resistance to the Cry5B and Cry14A
CC       toxins produced by Bacillus thuringiensis. This is thought to be due to
CC       mutants having reduced population of glycolipids which are targeted by
CC       the Cry proteins. {ECO:0000269|PubMed:10924467,
CC       ECO:0000269|PubMed:11486087}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC       {ECO:0000255}.
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DR   EMBL; AY038065; AAK72094.1; -; mRNA.
DR   EMBL; Z68752; CAD27607.1; -; Genomic_DNA.
DR   RefSeq; NP_001255612.1; NM_001268683.1.
DR   AlphaFoldDB; Q95US5; -.
DR   SMR; Q95US5; -.
DR   STRING; 6239.T12G3.8a; -.
DR   CAZy; GT31; Glycosyltransferase Family 31.
DR   PaxDb; Q95US5; -.
DR   PRIDE; Q95US5; -.
DR   EnsemblMetazoa; T12G3.8a.1; T12G3.8a.1; WBGene00000270.
DR   GeneID; 178142; -.
DR   KEGG; cel:CELE_T12G3.8; -.
DR   UCSC; T12G3.8; c. elegans.
DR   CTD; 178142; -.
DR   WormBase; T12G3.8a; CE30354; WBGene00000270; bre-5.
DR   eggNOG; KOG2287; Eukaryota.
DR   GeneTree; ENSGT00940000173583; -.
DR   InParanoid; Q95US5; -.
DR   OMA; ILLVDYC; -.
DR   OrthoDB; 1037602at2759; -.
DR   PhylomeDB; Q95US5; -.
DR   Reactome; R-CEL-9037629; Lewis blood group biosynthesis.
DR   SignaLink; Q95US5; -.
DR   UniPathway; UPA00378; -.
DR   PRO; PR:Q95US5; -.
DR   Proteomes; UP000001940; Chromosome IV.
DR   Bgee; WBGene00000270; Expressed in adult organism and 3 other tissues.
DR   ExpressionAtlas; Q95US5; baseline and differential.
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; IDA:UniProtKB.
DR   GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0008194; F:UDP-glycosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0016051; P:carbohydrate biosynthetic process; IMP:WormBase.
DR   GO; GO:0045747; P:positive regulation of Notch signaling pathway; IGI:WormBase.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   GO; GO:0042661; P:regulation of mesodermal cell fate specification; IMP:UniProtKB.
DR   GO; GO:0009636; P:response to toxic substance; IMP:WormBase.
DR   InterPro; IPR002659; Glyco_trans_31.
DR   PANTHER; PTHR11214; PTHR11214; 1.
DR   Pfam; PF01762; Galactosyl_T; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Glycosyltransferase; Golgi apparatus; Insecticide resistance;
KW   Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..322
FT                   /note="Beta-1,3-galactosyltransferase bre-5"
FT                   /id="PRO_0000324668"
FT   TOPO_DOM        1..16
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        17..37
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        38..322
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        150
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         97
FT                   /note="R->K: In ye107; resistant to Bacillus thuringiensis
FT                   crystal5B toxin."
FT                   /evidence="ECO:0000269|PubMed:11486087"
SQ   SEQUENCE   322 AA;  37587 MW;  8250B4F26CBDAB2B CRC64;
     MFLCVRILKR KYHELSSFQK LLIFTITIFL LWVLGVVDKF RETSFGDFSW PLETRNLQLR
     SKFTKYPQCK FSGNGQKIII IIIKSSAKNG PMRESVRKTW GVFRMIDGVE VMPIFIVGRV
     ENMEIMRRID VESEKYKDIL AISDIDSYRN NTLKLFGAID YAANPNQCSS PDFTFLVDDD
     YLVHIPNLVK FAKTKQKEEL VYEGFVFDTS PFRLKIHKHS ISLNEYPFSR YPPYVSAGAV
     FLTSETIARF RNSIRKLKMF PFDDVFTGIL AKTVNVAATH NENFIFWCRR VSQKEWDDGV
     IAVHGYARKD LEYEYSQLNG FE
 
 
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