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Q8BWQ1 (UD2A3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
UDP-glucuronosyltransferase 2A3

Short name=UDPGT 2A3
EC=2.4.1.17
Gene names
Name:Ugt2a3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

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

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.

Ontologies

Keywords
   Cellular componentMembrane
   DomainSignal
Transmembrane
Transmembrane helix
   Molecular functionGlycosyltransferase
Transferase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular glucuronidation

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionglucuronosyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

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 – 51421Helical; Potential
Topological domain515 – 53420Cytoplasmic Potential

Amino acid modifications

Modified residue1351N6-succinyllysine Ref.4
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

Sequences

Sequence LengthMass (Da)Tools
Q8BWQ1 [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

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[4]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-135, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK008601 mRNA. Translation: BAB25770.1.
AK050327 mRNA. Translation: BAC34191.1.
BC025795 mRNA. Translation: AAH25795.1.
CCDSCCDS19387.1.
RefSeqNP_082370.2. NM_028094.3.
UniGeneMm.482739.

3D structure databases

ProteinModelPortalQ8BWQ1.
SMRQ8BWQ1. Positions 285-446.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ8BWQ1. 2 interactions.
MINTMINT-4118511.

Protein family/group databases

CAZyGT1. Glycosyltransferase Family 1.

PTM databases

PhosphoSiteQ8BWQ1.

Proteomic databases

MaxQBQ8BWQ1.
PaxDbQ8BWQ1.
PRIDEQ8BWQ1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000031195; ENSMUSP00000031195; ENSMUSG00000035780.
GeneID72094.
KEGGmmu:72094.
UCSCuc008xyh.2. mouse.

Organism-specific databases

CTD79799.
MGIMGI:1919344. Ugt2a3.

Phylogenomic databases

eggNOGCOG1819.
GeneTreeENSGT00640000091260.
HOGENOMHOG000220831.
HOVERGENHBG004033.
InParanoidQ8BWQ1.
KOK00699.
OMAPSIIIDQ.
OrthoDBEOG7GBFWS.
PhylomeDBQ8BWQ1.
TreeFamTF315472.

Gene expression databases

BgeeQ8BWQ1.
GenevestigatorQ8BWQ1.

Family and domain databases

InterProIPR002213. UDP_glucos_trans.
[Graphical view]
PANTHERPTHR11926. PTHR11926. 1 hit.
PfamPF00201. UDPGT. 1 hit.
[Graphical view]
PROSITEPS00375. UDPGT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSUGT2A3. mouse.
NextBio335422.
PROQ8BWQ1.
SOURCESearch...

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: July 9, 2014
This is version 92 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

MGD cross-references

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