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Reviewed, UniProtKB/Swiss-Prot Q9CW73 (B3GA1_MOUSE)

Last modified June 16, 2009. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 1
    EC=2.4.1.135
Alternative name(s):
    Beta-1,3-glucuronyltransferase 1
    Glucuronosyltransferase-P
      Short name=GlcAT-P
    UDP-GlcUA:glycoprotein beta-1,3-glucuronyltransferase
      Short name=GlcUAT-P
Gene names
Name: B3gat1
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length334 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Involved in the biosynthesis of L2/HNK-1 carbohydrate epitope on glycoproteins. Can also play a role in glycosaminoglycan biosynthesis. Substrates include asialo-orosomucoid (ASOR), asialo-fetuin, and asialo-neural cell adhesion molecule. Requires sphingomyelin for activity: stearoyl-sphingomyelin was the most effective, followed by palmitoyl-sphingomyelin and lignoceroyl-sphingomyelin. Activity was demonstrated only for sphingomyelin with a saturated fatty acid and not for that with an unsaturated fatty acid, regardless of the length of the acyl group 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 Potential.

Subcellular location

Golgi apparatus membrane; Single-pass type II membrane protein By similarity.

Sequence similarities

Belongs to the glycosyltransferase 43 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 334334Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 1
PRO_0000195168

Regions

Topological domain1 – 66Cytoplasmic Potential
Transmembrane7 – 2721Signal-anchor for type II membrane protein Potential
Topological domain28 – 334307Lumenal Potential

Sites

Active site2841Proton acceptor By similarity
Metal binding1971Manganese By similarity

Amino acid modifications

Glycosylation1401N-linked (GlcNAc...) Potential
Glycosylation1841N-linked (GlcNAc...) Potential
Glycosylation3031N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict1211G → E in BAB22514. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9CW73-1 [UniParc].

Last modified April 26, 2005. Version 2.
Checksum: 6BDAF9F6DA80A40C

FASTA33438,165
        10         20         30         40         50         60 
MPKRRDILAI VLIVLPWTLL ITVWHQSSLA PLLAVHKDEG SDPRHEAPPG ADPREYCMSD 

        70         80         90        100        110        120 
RDIVEVVRTE YVYTRPPPWS DTLPTIHVVT PTYSRPVQKA ELTRMANTLL HVPNLHWLVV 

       130        140        150        160        170        180 
GDAPRRTPLT ARLLRDTGLN YTHLHVETPR NYKLRGDARD PRIPRGTMQR NLALRWLRET 

       190        200        210        220        230        240 
FPRNSTQPGV VYFADDDNTY SLELFEEMRS TRRVSVWPVA FVGGLRYEAP RVNGAGKVVG 

       250        260        270        280        290        300 
WKTVFDPHRP FAIDMAGFAV NLRLILQRSQ AYFKLRGVKG GYQESSLLRE LVTLNDLEPK 

       310        320        330 
AANCTKILVW HTRTEKPVLV NEGKKGFTDP SVEI 

« Hide

References

[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Brain and Retina.
+Additional computationally mapped references.

Cross-references

Sequence databases

AK003020 mRNA. Translation: BAB22514.1.
AK044599 mRNA. Translation: BAC31996.1. Different initiation.
IPIIPI00405708.
UniGeneMm.218788

3D structure databases

HSSPHSSP built from PDB template 1KWS based on UniProtKB O94766.
SMRQ9CW73. Positions 83-334.
ModBaseSearch...

Protein family/group databases

CAZyGT43. Glycosyltransferase Family 43.

Genome annotation databases

EnsemblENSMUSG00000045994. Mus musculus. [Contig view]

Organism-specific databases

MGIMGI:1924148. B3gat1.

Phylogenomic databases

HOVERGENQ9CW73.

Enzyme and pathway databases

BRENDA2.4.1.135. 244.

Gene expression databases

ArrayExpressQ9CW73.
BgeeQ9CW73.
GermOnlineENSMUSG00000045994. Mus musculus.

Family and domain databases

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

Other Resources

SOURCESearch...

Entry information

Entry nameB3GA1_MOUSE
AccessionPrimary (citable) accession number: Q9CW73
Secondary accession number(s): Q8BXN8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: April 26, 2005
Last modified: June 16, 2009
This is version 68 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents