Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q8BWQ1 (UD2A3_MOUSE)

Last modified June 16, 2009. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

Hide | Top

Names and origin

Protein namesRecommended name:
    UDP-glucuronosyltransferase 2A3
      Short name=UDPGT 2A3
    EC=2.4.1.17
Gene names
Name: Ugt2a3
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Hide | Top

Protein attributes

Sequence length534 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

Hide | Top

General annotation (Comments)

Function

UDP-glucuronosyltransferases catalyze phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to increase water solubility and enhance excretion. They are of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds By similarity.

Catalytic activity

UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside.

Subcellular location

Membrane; Single-pass type I membrane protein Potential.

Tissue specificity

Highly expressed in liver, with lower levels in duodenum and jejunum. Ref.3

Sequence similarities

Belongs to the UDP-glycosyltransferase family.

Hide | Top

Ontologies

Keywords
   Cellular componentMembrane
   DomainSignal
Transmembrane
   Molecular functionGlycosyltransferase
Transferase
   PTMGlycoprotein
Gene Ontology (GO)
   Biological processmetabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionglucuronosyltransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 534516UDP-glucuronosyltransferase 2A3
PRO_0000299147

Regions

Topological domain19 – 493475Extracellular Potential
Transmembrane494 – 51421 Potential
Topological domain515 – 53420Cytoplasmic Potential

Amino acid modifications

Glycosylation1021N-linked (GlcNAc...) Potential
Glycosylation2041N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict2521K → E in BAB25770. Ref.1
Sequence conflict2841P → S in AAH25795. Ref.2
Sequence conflict3461T → I in BAB25770. Ref.1

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
Q8BWQ1-1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 3BF4F591395B1620

FASTA53461,119
        10         20         30         40         50         60 
MVSEKCVAAF FLLQLCWAGC GFCSKVLVWP CDMSHWLNLK TILEELGARG HEVTVLKYPS 

        70         80         90        100        110        120 
IIIDQSKRIP LHFENIPLLY EIETAENRLN EIANLAVNVI PNLSLWEAAK TLQDFFLQVT 

       130        140        150        160        170        180 
GDFESICRSV LYNQKFMDKL RDAQYDVVVI DPVVPCGELV AEVLQIPFVY TLRFSMGYYM 

       190        200        210        220        230        240 
EKHCGQLPIP LSYVPVVMSE LTDNMTFTER VKNMMFSLLF EYWLQQYDFA FWDQFYSETL 

       250        260        270        280        290        300 
GRPTTFCKTV GKADIWLIRT YWDVEFPRPY LPNFEFVGGL HCKPAKPLPK EMEEFVQSSG 

       310        320        330        340        350        360 
EHGVVVFSLG SMVKNLTEEK ANLIASVLAQ IPQKVLWRYS GKKPATLGSN TRLFNWIPQN 

       370        380        390        400        410        420 
DLLGHPKTKA FITHGGTNGI YEAIYHGVPM VGVPMLGDQP HNIAHMEAKG AALKVSISTM 

       430        440        450        460        470        480 
TSTDLLSAVR AVINEPSYKE NAMRLSRIHH DQPVKPLDRA VFWIEFVMRH KGAKHLRVAA 

       490        500        510        520        530 
HDLSWFQYHS LDVIGFLLLC VVTLTFIITK FCLFVCQKLY MKESKKMGNR KKKN

« Hide

Hide | Top

References

« Hide 'large scale' 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: Liver and Small intestine.
[2]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Liver.
[3]"Tissue- and gender-specific mRNA expression of UDP-glucuronosyltransferases (UGTs) in mice."
Buckley D.B., Klaassen C.D.
Drug Metab. Dispos. 35:121-127(2007) [PubMed: 17050650] [Abstract]
Cited for: TISSUE SPECIFICITY.

Hide | Top

Cross-references

Sequence databases

AK008601 mRNA. Translation: BAB25770.1.
AK050327 mRNA. Translation: BAC34191.1.
BC025795 mRNA. Translation: AAH25795.1.
IPIIPI00471231.
RefSeqNP_082370.1.
UniGeneMm.26794

3D structure databases

SMRQ8BWQ1. Positions 285-446.
ModBaseSearch...

Protein family/group databases

CAZyGT1. Glycosyltransferase Family 1.

Genome annotation databases

EnsemblENSMUSG00000035780. Mus musculus. [Contig view]
GeneID72094.
KEGGmmu:72094.

Organism-specific databases

MGIMGI:1919344. Ugt2a3.

Phylogenomic databases

HOGENOMQ8BWQ1.
HOVERGENQ8BWQ1.
OMAQ8BWQ1. VKNMMFS.

Enzyme and pathway databases

BRENDA2.4.1.17. 244.

Gene expression databases

ArrayExpressQ8BWQ1.
BgeeQ8BWQ1.

Family and domain databases

InterProIPR002213. UDP_glucos_trans.
[Graphical view]
PANTHERPTHR11926. UDP_glucos_trans. 1 hit.
PfamPF00201. UDPGT. 1 hit.
[Graphical view]
PROSITEPS00375. UDPGT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio335422.
SOURCESearch...

Hide | Top

Entry information

Entry nameUD2A3_MOUSE
AccessionPrimary (citable) accession number: Q8BWQ1
Secondary accession number(s): Q8R129, Q9D811
Entry history
Integrated into UniProtKB/Swiss-Prot: August 21, 2007
Last sequence update: March 1, 2003
Last modified: June 16, 2009
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Hide | Top

Relevant documents

MGD cross-references

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

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