ID   BRE2_CAEBR              Reviewed;         365 AA.
AC   A8Y3H3;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 67.
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-2.1 {ECO:0000312|WormBase:CBG22997};
GN   Synonyms=bre-2 {ECO:0000250|UniProtKB:Q60MT2};
GN   ORFNames=CBG22997 {ECO:0000312|WormBase:CBG22997};
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
CC   -!- FUNCTION: Transfers N-acetylgalactosamine onto carbohydrate substrates.
CC       Involved in susceptibility to pore-forming crystal toxins in
CC       conjunction with bre-1, bre-3, bre-4, and bre-5. Involved in resistance
CC       to the nematotoxic C.cinerea galectin Cgl2.
CC       {ECO:0000250|UniProtKB:Q6QMT2, ECO:0000250|UniProtKB:Q95US5}.
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000250|UniProtKB:Q95US5}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000255,
CC       ECO:0000305}; Single-pass type II membrane protein {ECO:0000255,
CC       ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC       {ECO:0000255}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; HE600964; CAP39442.3; -; Genomic_DNA.
DR   RefSeq; XP_002643077.1; XM_002643031.1.
DR   AlphaFoldDB; A8Y3H3; -.
DR   SMR; A8Y3H3; -.
DR   STRING; 6238.CBG22997; -.
DR   EnsemblMetazoa; CBG22997.1; CBG22997.1; WBGene00041433.
DR   GeneID; 8585071; -.
DR   KEGG; cbr:CBG_22997; -.
DR   CTD; 8585071; -.
DR   WormBase; CBG22997; CBP12305; WBGene00041433; Cbr-bre-2.1.
DR   eggNOG; KOG2287; Eukaryota.
DR   HOGENOM; CLU_045590_0_0_1; -.
DR   InParanoid; A8Y3H3; -.
DR   OMA; THHDILQ; -.
DR   OrthoDB; 1037602at2759; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000008549; Chromosome III.
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:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0016758; F:hexosyltransferase activity; IEA:InterPro.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR002659; Glyco_trans_31.
DR   PANTHER; PTHR11214; PTHR11214; 1.
DR   Pfam; PF01762; Galactosyl_T; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Glycosyltransferase; Golgi apparatus; Insecticide resistance;
KW   Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..365
FT                   /note="Beta-1,3-galactosyltransferase bre-2"
FT                   /id="PRO_0000324666"
FT   TOPO_DOM        1..8
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        9..29
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT   TOPO_DOM        30..365
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        50
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        54
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        61
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        212
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   365 AA;  42164 MW;  6230B891C60B85DE CRC64;
     MRQNRRASMI VNRILITLIV LVSLSFLFLR AGPKFSEADR ACIQDEWQEN KSLNVSSEIN
     NETYQIVFAD VQKEFKWIFL PKEISGNPDI LMIVSSNRDN FARRNVIRKS WMNSDKNKIV
     AEKRMKILFL VGVNSENEKE NTVVLKEAEV FGDIIVVDLE DNYQNLPYKS LTILLYGQSK
     TAESVKLIGK IDEDVIFYPD QLTPLINDGT INMSISAIYG EKWNAGVEVS NKDETNKWFI
     PKYSFKCQLL PSYLSGPFYL TTRKAAERIL KSTKHRKFIS VEDVFITGLL AGDVGVEKKQ
     LPSMYMYDET TTDTAKAEIL AWHNFKNNAE FLESWENLRL SRCKACRKSR NFRGSRSQLD
     EERNQ