ID   BRE3_CAEEL              Reviewed;         455 AA.
AC   Q03562;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2004, sequence version 2.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Beta-1,4-mannosyltransferase bre-3;
DE            EC=2.4.1.-;
DE   AltName: Full=Bacillus thuringiensis toxin-resistant protein 3;
DE            Short=Bt toxin-resistant protein 3;
GN   Name=bre-3; ORFNames=B0464.4;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC   STRAIN=Bristol N2;
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]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=7906398; DOI=10.1038/368032a0;
RA   Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA   Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA   Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA   Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA   Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA   Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA   Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA   Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA   Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA   Wilkinson-Sproat J., Wohldman P.;
RT   "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT   elegans.";
RL   Nature 368:32-38(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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]
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   [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: Glycosyltransferase with a proposed role in glycosphingolipid
CC       biosynthesis (PubMed:12944392, PubMed:10924467). Involved in
CC       susceptibility to pore-forming crystal toxins in conjunction with bre-
CC       1, bre-2, bre-4 and bre-5 (PubMed:12944392, PubMed:10924467). Involved
CC       in resistance to the nematotoxic C.cinerea galectin Cgl2
CC       (PubMed:20062796). Has a role in determining brood size
CC       (PubMed:12944392, PubMed:10924467). {ECO:0000269|PubMed:10924467,
CC       ECO:0000269|PubMed:12944392, ECO:0000269|PubMed:20062796}.
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12944392}. Note=In
CC       punctate structures throughout the cell.
CC   -!- TISSUE SPECIFICITY: Endothelial cells. {ECO:0000269|PubMed:12944392}.
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. Mutants also have reduced brood sizes at only 17% of
CC       wild-type N2. {ECO:0000269|PubMed:10924467,
CC       ECO:0000269|PubMed:12944392}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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DR   EMBL; AY533305; AAS21307.1; -; mRNA.
DR   EMBL; Z19152; CAA79538.2; -; Genomic_DNA.
DR   PIR; S28281; S28281.
DR   RefSeq; NP_499087.2; NM_066686.5.
DR   AlphaFoldDB; Q03562; -.
DR   STRING; 6239.B0464.4.1; -.
DR   CAZy; GT2; Glycosyltransferase Family 2.
DR   PaxDb; Q03562; -.
DR   PeptideAtlas; Q03562; -.
DR   EnsemblMetazoa; B0464.4a.1; B0464.4a.1; WBGene00000268.
DR   EnsemblMetazoa; B0464.4a.2; B0464.4a.2; WBGene00000268.
DR   EnsemblMetazoa; B0464.4a.3; B0464.4a.3; WBGene00000268.
DR   GeneID; 176332; -.
DR   KEGG; cel:CELE_B0464.4; -.
DR   UCSC; B0464.4.1; c. elegans.
DR   CTD; 176332; -.
DR   WormBase; B0464.4a; CE33592; WBGene00000268; bre-3.
DR   eggNOG; ENOG502QTGI; Eukaryota.
DR   GeneTree; ENSGT00520000061918; -.
DR   HOGENOM; CLU_044554_0_0_1; -.
DR   InParanoid; Q03562; -.
DR   OMA; DSDWIVH; -.
DR   OrthoDB; 801915at2759; -.
DR   PhylomeDB; Q03562; -.
DR   UniPathway; UPA00378; -.
DR   PRO; PR:Q03562; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00000268; Expressed in adult organism and 4 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0019187; F:beta-1,4-mannosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0016051; P:carbohydrate biosynthetic process; IMP:UniProtKB.
DR   GO; GO:0006688; P:glycosphingolipid biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009636; P:response to toxic substance; IMP:UniProtKB.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR027389; B_mannosylTrfase_Bre-3/Egh.
DR   InterPro; IPR001173; Glyco_trans_2-like.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR16779; PTHR16779; 1.
DR   Pfam; PF13632; Glyco_trans_2_3; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Glycosyltransferase; Insecticide resistance; Reference proteome;
KW   Transferase.
FT   CHAIN           1..455
FT                   /note="Beta-1,4-mannosyltransferase bre-3"
FT                   /id="PRO_0000059273"
SQ   SEQUENCE   455 AA;  51591 MW;  28A3605A22C38F04 CRC64;
     MNCEVKHALH CAVLVAWIVC FAYFCGVFTE PVEGSVPESP VASYGLIWTV CLYLLRFTAL
     LVLPQCLCNL GGLMMFNAFR EKVQLKAAPL LSPFVCFRVV TKGNFPLLVK ENIDTNMKTC
     FEAGMENFIF EVVTDKAINL PPNPRVREVV VPTVYKTKSG AKFKARALQY CLEDDVNILQ
     PTDWIVHLDE ETLLTTNAIC GILNFCEDGK HQFGQGVITY ANGDIVNWLT TLSDSFRVAD
     DMGKLRFQFK LFHKPLFGWK GSYVVTQVEA ERDVSYDHGM EGSIAEDCFF SMVAMKHGYS
     FDFIEGEMHE KSPFTMWDFL QQRKRWLQGI LLTVHSSKIA VVHKALLALS LYAWATMPLT
     SLQVFLCPLF PLPRCLPFDF LLSFVGALNL YMYIFGVVKS FSHKYRNSLL RLAMYLAGAL
     MTIPFNILIE NAAVLVGMFG RKDQFYIVNK DIQTV