BRE4_CAEBR
ID BRE4_CAEBR Reviewed; 384 AA.
AC A8Y1P7;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 77.
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:0000250|UniProtKB:Q9GUM2}; ORFNames=CBG22165;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1] {ECO:0000312|EMBL:CAP38817.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000312|EMBL:CAP38817.1};
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: 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 and bre-3 (By similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P08037};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:Q9GUM2}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type II
CC membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 7 family. {ECO:0000255}.
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DR EMBL; HE601428; CAP38817.1; -; Genomic_DNA.
DR RefSeq; XP_002638938.1; XM_002638892.1.
DR AlphaFoldDB; A8Y1P7; -.
DR SMR; A8Y1P7; -.
DR STRING; 6238.CBG22165; -.
DR EnsemblMetazoa; CBG22165.1; CBG22165.1; WBGene00040787.
DR GeneID; 8580934; -.
DR KEGG; cbr:CBG_22165; -.
DR CTD; 8580934; -.
DR WormBase; CBG22165; CBP05300; WBGene00040787; Cbr-bre-4.
DR eggNOG; KOG3916; Eukaryota.
DR HOGENOM; CLU_044391_3_1_1; -.
DR InParanoid; A8Y1P7; -.
DR OMA; GPFNRAM; -.
DR OrthoDB; 1201618at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000008549; Chromosome I.
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:0033207; F:beta-1,4-N-acetylgalactosaminyltransferase activity; IBA:GO_Central.
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; IEA:EnsemblMetazoa.
DR GO; GO:0006486; P:protein glycosylation; IBA:GO_Central.
DR GO; GO:0009636; P:response to toxic substance; IEA:EnsemblMetazoa.
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 3: Inferred from homology;
KW Disulfide bond; Glycoprotein; Glycosyltransferase; Insecticide resistance;
KW Manganese; Membrane; Metal-binding; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..384
FT /note="Beta-1,4-N-acetylgalactosaminyltransferase bre-4"
FT /id="PRO_0000324670"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..35
FT /note="Helical; Signal-anchor for type II membrane protein"
FT TOPO_DOM 36..384
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT BINDING 223
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P08037"
FT BINDING 316
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 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 104..145
FT /evidence="ECO:0000250|UniProtKB:P08037"
FT DISULFID 216..235
FT /evidence="ECO:0000250|UniProtKB:P08037"
SQ SEQUENCE 384 AA; 43811 MW; 4F9EBC583A634B7C CRC64;
MAFRHLASAK LKTFFVLCAA LLLVHAMIYK VPSLYENFSI GSSTLIADVD AMEAVLGNTA
STSDDPFDVW NSTFSPISEV NQTAFMEDIR PILFGDANET RPHCNQTPPH LVGPIRVFLD
EPDFATLEKI YPETHPGGHG IPTECVARHR VAIIVPYRDR EAHLRIMLHN LHSLLAKQQL
DYAIFVVEQV ANQTFNRGKL MNVGYDVASR LYPWQCFIFH DVDLLPEDDR NLYTCPIQPR
HMSVAIDKFH YKLPYSAIFG GISALTQEHV KAINGFSNDF WGWGGEDDDL ATRTSQAGLK
VSRYPAQIAR YKMIKHSTEA TNPVNKCRYK IMGQTKRRWK TDGLSSLKYK LVKLELKPLY
TRAVVDLLEK ECRRELRRDF PTCF
