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P58158 (B3GA3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length335 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 335335Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 3
PRO_0000195177

Regions

Topological domain1 – 77Cytoplasmic Potential
Transmembrane8 – 2821Helical; Signal-anchor for type II membrane protein; Potential
Topological domain29 – 335307Lumenal Potential
Nucleotide binding82 – 843UDP-glucuronate binding By similarity
Nucleotide binding194 – 1963UDP-glucuronate binding By similarity
Nucleotide binding308 – 3103UDP-glucuronate binding By similarity
Region243 – 25210Interaction with galactose moiety of substrate glycoprotein By similarity

Sites

Active site2811Proton donor/acceptor By similarity
Metal binding1961Manganese By similarity
Binding site1131UDP-glucuronate By similarity
Binding site1561UDP-glucuronate By similarity
Binding site1611UDP-glucuronate By similarity
Site2271Interaction with galactose moiety of substrate glycoprotein By similarity
Site3181Interaction with galactose moiety of substrate glycoprotein By similarity

Amino acid modifications

Glycosylation3001N-linked (GlcNAc...) Potential
Disulfide bond33Interchain By similarity

Sequences

Sequence LengthMass (Da)Tools
P58158 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 906EED2AB672F1EC

FASTA33537,067
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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.
RefSeqNP_077218.1. NM_024256.2.
UniGeneMm.259.

3D structure databases

ProteinModelPortalP58158.
SMRP58158. Positions 76-335.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000093962.

Protein family/group databases

CAZyGT43. Glycosyltransferase Family 43.

PTM databases

PhosphoSiteP58158.

Proteomic databases

PaxDbP58158.
PRIDEP58158.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000096243; ENSMUSP00000093962; ENSMUSG00000071649.
GeneID72727.
KEGGmmu:72727.
UCSCuc008gob.1. mouse.

Organism-specific databases

CTD26229.
MGIMGI:1919977. B3gat3.

Phylogenomic databases

eggNOGNOG310844.
GeneTreeENSGT00390000017640.
HOGENOMHOG000261693.
HOVERGENHBG050650.
InParanoidP58158.
KOK10158.
OMAFPMDMAG.
OrthoDBEOG7QG44X.
PhylomeDBP58158.
TreeFamTF313522.

Enzyme and pathway databases

UniPathwayUPA00378.

Gene expression databases

BgeeP58158.
GenevestigatorP58158.

Family and domain databases

InterProIPR005027. Glyco_trans_43.
[Graphical view]
PANTHERPTHR10896. PTHR10896. 1 hit.
PfamPF03360. Glyco_transf_43. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio336810.
PROP58158.
SOURCESearch...

Entry information

Entry nameB3GA3_MOUSE
AccessionPrimary (citable) accession number: P58158
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: June 1, 2001
Last modified: April 16, 2014
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot