P58158 (B3GA3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 3
EC=2.4.1.135

Alternative name(s):
Beta-1,3-glucuronyltransferase 3
Glucuronosyltransferase I
Short name=GlcAT-I
UDP-GlcUA:Gal beta-1,3-Gal-R glucuronyltransferase
Short name=GlcUAT-I

Gene names

Name:

B3gat3

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	335 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Glycosaminoglycans biosynthesis. Involved in forming the linkage tetrasaccharide present in heparan sulfate and chondroitin sulfate. Transfers a glucuronic acid moiety from the uridine diphosphate-glucuronic acid (UDP-GlcUA) to the common linkage region trisaccharide Gal-beta-1,3-Gal-beta-1,4-Xyl covalently bound to a Ser residue at the glycosaminylglycan attachment site of proteoglycans. Can also play a role in the biosynthesis of l2/HNK-1 carbohydrate epitope on glycoproteins By similarity.
Catalytic activity	UDP-glucuronate + 3-beta-D-galactosyl-4-beta-D-galactosyl-O-beta-D-xylosylprotein = UDP + 3-beta-D-glucuronosyl-3-beta-D-galactosyl-4-beta-D-galactosyl-O-beta-D-xylosylprotein.
Cofactor	Manganese By similarity.
Pathway	Protein modification; protein glycosylation.
Subunit structure	Homodimer; disulfide-linked By similarity.
Subcellular location	Golgi apparatus membrane; Single-pass type II membrane protein By similarity.
Tissue specificity	Expressed in heart, aorta, bone, and also in osteoblasts. Ref.2
Post-translational modification	N-glycosylated By similarity.
Sequence similarities	Belongs to the glycosyltransferase 43 family.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Domain	Signal-anchor Transmembrane Transmembrane helix
Ligand	Manganese Metal-binding
Molecular function	Transferase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	heparan sulfate proteoglycan biosynthetic process Inferred from sequence orthology PubMed 11731273. Source: MGI protein glycosylation Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell cis-Golgi network Inferred from electronic annotation. Source: Compara integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase activity Inferred from electronic annotation. Source: EC metal 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 – 335	335	Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 3		PRO_0000195177
Regions
	Topological domain	1 – 7	7	Cytoplasmic Potential
	Transmembrane	8 – 28	21	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	29 – 335	307	Lumenal Potential
	Nucleotide binding	82 – 84	3	UDP-glucuronate binding By similarity
	Nucleotide binding	194 – 196	3	UDP-glucuronate binding By similarity
	Nucleotide binding	308 – 310	3	UDP-glucuronate binding By similarity
	Region	243 – 252	10	Interaction with galactose moiety of substrate glycoprotein By similarity
Sites
	Active site	281	1	Proton donor/acceptor By similarity
	Metal binding	196	1	Manganese By similarity
	Binding site	113	1	UDP-glucuronate By similarity
	Binding site	156	1	UDP-glucuronate By similarity
	Binding site	161	1	UDP-glucuronate By similarity
	Site	227	1	Interaction with galactose moiety of substrate glycoprotein By similarity
	Site	318	1	Interaction with galactose moiety of substrate glycoprotein By similarity
Amino acid modifications
	Glycosylation	300	1	N-linked (GlcNAc...) Potential
	Disulfide bond	33		Interchain By similarity

Sequences

	Sequence		Length	Mass (Da)
	P58158 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 906EED2AB672F1EC	FASTA	335	37,067
	10 20 30 40 50 60 MKLKLKNVFL AYFLVSIAGL LYALVQLGQP CDCLPPLRAA AEQLRQKDLR ISQLQADLRR 70 80 90 100 110 120 PPPVPAQPPE PEALPTIYVI TPTYARLVQK AELVRLSQTL SLVPRLHWLL VEDAESPTPL 130 140 150 160 170 180 VSGLLAASGL LFTHLAVLTP KAQRLREGEP GWVRPRGVEQ RNKALDWLRG KGGAVGGEKD 190 200 210 220 230 240 PPPPGTQGVV YFADDDNTYS RELFKEMRWT RGVSVWPVGL VGGLRFEGPQ VQDGRVVGFH 250 260 270 280 290 300 TAWEPNRPFP LDMAGFAVAL PLLLAKPNAQ FDATAPRGHL ESSLLSHLVD PKDLEPRAAN 310 320 330 CTQVLVWHTR TEKPKMKQEE QLQRQGQGSD PAIEV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Eye and Mammary tumor.
[2]	"Faulty initiation of proteoglycan synthesis causes cardiac and joint defects." Baasanjav S., Al-Gazali L., Hashiguchi T., Mizumoto S., Fischer B., Horn D., Seelow D., Ali B.R., Aziz S.A., Langer R., Saleh A.A., Becker C., Nurnberg G., Cantagrel V., Gleeson J.G., Gomez D., Michel J.B., Stricker S. , Lindner T.H., Nurnberg P., Sugahara K., Mundlos S., Hoffmann K. Am. J. Hum. Genet. 89:15-27(2011) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BC002103 mRNA. Translation: AAH02103.1. BC004038 mRNA. Translation: AAH04038.1. BC012930 mRNA. Translation: AAH12930.1.
IPI	IPI00116744.
RefSeq	NP_077218.1. NM_024256.2.
UniGene	Mm.259.
3D structure databases
ProteinModelPortal	P58158.
SMR	P58158. Positions 76-335.
ModBase	Search...
Protein-protein interaction databases
STRING	10090.ENSMUSP00000093962.
Protein family/group databases
CAZy	GT43. Glycosyltransferase Family 43.
PTM databases
PhosphoSite	P58158.
Proteomic databases
PaxDb	P58158.
PRIDE	P58158.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000096243; ENSMUSP00000093962; ENSMUSG00000071649.
GeneID	72727.
KEGG	mmu:72727.
UCSC	uc008gob.1. mouse.
Organism-specific databases
CTD	26229.
MGI	MGI:1919977. B3gat3.
Phylogenomic databases
eggNOG	NOG310844.
GeneTree	ENSGT00390000017640.
HOGENOM	HOG000261693.
HOVERGEN	HBG050650.
InParanoid	P58158.
KO	K10158.
OMA	FHTAWEP.
OrthoDB	EOG42NJ0R.
Enzyme and pathway databases
UniPathway	UPA00378.
Gene expression databases
Bgee	P58158.
Genevestigator	P58158.
GermOnline	ENSMUSG00000071649. Mus musculus.
Family and domain databases
InterPro	IPR005027. Glyco_trans_43. [Graphical view]
PANTHER	PTHR10896. PTHR10896. 1 hit.
Pfam	PF03360. Glyco_transf_43. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	336810.
SOURCE	Search...

Entry information

Entry name

B3GA3_MOUSE

Accession

Primary (citable) accession number: P58158

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 2001
Last sequence update:	June 1, 2001
Last modified:	April 3, 2013
This is version 112 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program