Reviewed, UniProtKB/Swiss-Prot Q9GUM2 (BRE4_CAEEL)

Names and origin

Protein names

Recommended name:
    Beta-1,4-N-acetylgalactosaminyltransferase bre-4
    EC=2.4.1.-
Alternative name(s):
    Beta-4-GalNAcT
    Bacillus thuringiensis toxin-resistant protein 4
      Short name=Bt toxin-resistant protein 4

Gene names

Name:	bre-4
ORF Names:	Y73E7A.7

Organism

Caenorhabditis elegans [Complete proteome]

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length	383 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the transfer of galactose onto proteins or lipids. Required for susceptibility to pore-forming crystal toxins in conjunction with bre-1, bre-2, bre-3 and bre-5. Ref.1 Ref.2 Ref.4
Cofactor	Manganese By similarity. UniProtKB P08037
Pathway	Protein modification; protein glycosylation. Ref.1 Ref.2
Subcellular location	Membrane; Single-pass type II membrane protein Potential.
Disruption phenotype	Worms exhibit resistance to the Cry5B toxin produced by Bacillus thuringiensis. This is thought to be due to mutants having reduced population of glycolipids which are targeted by the Cry5B protein. Ref.2 Ref.4
Sequence similarities	Belongs to the glycosyltransferase 7 family.

Ontologies

Keywords
Biological process	Insecticide resistance
Cellular component	Membrane
Domain	Signal-anchor Transmembrane
Ligand	Manganese Metal-binding
Molecular function	Glycosyltransferase Transferase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro formation of infection structure on or near host Ref.4 Inferred from mutant phenotype. Source: UniProtKB
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	acetylgalactosaminyltransferase activity Ref.1 Inferred from direct assay. Source: UniProtKB manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 383	383	Beta-1,4-N-acetylgalactosaminyltransferase bre-4		PRO_0000324671
Regions
	Topological domain	1 – 6	6	Cytoplasmic Potential
	Transmembrane	7 – 29	23	Signal-anchor for type II membrane protein Potential
	Topological domain	30 – 383	354	Extracellular Potential
Sites
	Metal binding	222	1	Manganese By similarity UniProtKB P08037
	Metal binding	315	1	Manganese By similarity UniProtKB P08037
Amino acid modifications
	Glycosylation	37	1	N-linked (GlcNAc...) Potential
	Glycosylation	71	1	N-linked (GlcNAc...) Potential
	Glycosylation	81	1	N-linked (GlcNAc...) Potential
	Glycosylation	97	1	N-linked (GlcNAc...) Potential
	Glycosylation	191	1	N-linked (GlcNAc...) Potential
	Disulfide bond	103 ↔ 144		By similarity UniProtKB P08037
	Disulfide bond	215 ↔ 234		By similarity UniProtKB P08037
Experimental info
	Mutagenesis	260	1	G → R in ye43; resistant to Bacillus thuringiensis crystal5B toxin. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9GUM2-1 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: ADEDFA4275B2CE81	FASTA	383	43,914
	10 20 30 40 50 60 MAFRHLAVAR LKSLLVLCAV LLLVHAMIYK IPSLYENLTI GSSTLIADVD AMEAVLGNTA 70 80 90 100 110 120 STSDDLLDTW NSTFSPISEV NQTSFMEDIR PILFPDNQTL QFCNQTPPHL VGPIRVFLDE 130 140 150 160 170 180 PDFKTLEKIY PDTHAGGHGM PKDCVARHRV AIIVPYRDRE AHLRIMLHNL HSLLAKQQLD 190 200 210 220 230 240 YAIFIVEQVA NQTFNRGKLM NVGYDVASRL YPWQCFIFHD VDLLPEDDRN LYTCPIQPRH 250 260 270 280 290 300 MSVAIDKFNY KLPYSAIFGG ISALTKDHLK KINGFSNDFW GWGGEDDDLA TRTSMAGLKV 310 320 330 340 350 360 SRYPTQIARY KMIKHSTEAT NPVNKCRYKI MGQTKRRWTR DGLSNLKYKL VNLELKPLYT 370 380 RAVVDLLEKD CRRELRRDFP TCF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and enzymatic characterization of a UDP-GalNAc:GlcNAc(beta)-R beta1,4-N-acetylgalactosaminyltransferase from Caenorhabditis elegans." Kawar Z.S., Van Die I., Cummings R.D. J. Biol. Chem. 277:34924-34932(2002) [PubMed: 12167666] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, PATHWAY.
[2]	"Resistance to a bacterial toxin is mediated by removal of a conserved glycosylation pathway required for toxin-host interactions." Griffitts J.S., Huffman D.L., Whitacre J.L., Barrows B.D., Marroquin L.D., Mueller R., Brown J.R., Hennet T., Esko J.D., Aroian R.V. J. Biol. Chem. 278:45594-45602(2003) [PubMed: 12944392] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, MUTAGENESIS OF GLY-260, DISRUPTION PHENOTYPE.
[3]	"Genome sequence of the nematode C. elegans: a platform for investigating biology." The C. elegans sequencing consortium Science 282:2012-2018(1998) [PubMed: 9851916] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bristol N2.
[4]	"Bacillus thuringiensis (Bt) toxin susceptibility and isolation of resistance mutants in the nematode Caenorhabditis elegans." Marroquin L.D., Elyassnia D., Griffitts J.S., Feitelson J.S., Aroian R.V. Genetics 155:1693-1699(2000) [PubMed: 10924467] [Abstract] Cited for: IDENTIFICATION, FUNCTION, DISRUPTION PHENOTYPE.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AY130767 mRNA. Translation: AAM95168.1. AY533306 mRNA. Translation: AAS21308.1. AC025727 Genomic DNA. Translation: AAG23384.1.
RefSeq	NP_490872.1.
UniGene	Cel.9283
3D structure databases
HSSP	HSSP built from PDB template 1O0R based on UniProtKB P08037.
ModBase	Search...
Protein family/group databases
CAZy	GT7. Glycosyltransferase Family 7.
Genome annotation databases
Ensembl	Y73E7A.7. Caenorhabditis elegans. [Contig view]
GeneID	190668.
KEGG	cel:Y73E7A.7.
NMPDR	fig|6239.3.peg.252.
Organism-specific databases
WormBase	WBGene00000269. bre-4.
WormPep	Y73E7A.7. CE26412. [WorfDB]
Phylogenomic databases
OMA	Q9GUM2. PHLVGPI.
Gene expression databases
ArrayExpress	Q9GUM2.
Family and domain databases
InterPro	IPR003859. Galactosyl_T_2. [Graphical view]
PANTHER	PTHR19300. Galactosyl_T_2. 1 hit.
Pfam	PF02709. Galactosyl_T_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	946570.

Entry information

Entry name

BRE4_CAEEL

Accession

Primary (citable) accession number: Q9GUM2

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 18, 2008
Last sequence update:	March 1, 2001
Last modified:	May 5, 2009
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Caenorhabditis annotation project