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Q8JZZ0 (UD3A2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 82. 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 3A2

Short name=UDPGT 3A2
EC=2.4.1.17
Gene names
Name:Ugt3a2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length523 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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 kidney, while it is expressed at low levels in liver. Not detected in other tissues examined. Ref.3

Sequence similarities

Belongs to the UDP-glycosyltransferase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 523501UDP-glucuronosyltransferase 3A2
PRO_0000299154

Regions

Topological domain23 – 487465Extracellular Potential
Transmembrane488 – 50821Helical; Potential
Topological domain509 – 52315Cytoplasmic Potential

Amino acid modifications

Glycosylation521N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict1211S → G in BAE25548. Ref.1
Sequence conflict3441P → S in AAH34837. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q8JZZ0 [UniParc].

Last modified August 21, 2007. Version 2.
Checksum: BC7BD6ADF197ADD9

FASTA52359,673
        10         20         30         40         50         60 
MAAHRRWLLM SFLFLEVILL EAAKILTIST LSASHYIVIS RVSQVLHEGG HNVTKLLYES 

        70         80         90        100        110        120 
ANIPDFRKEK PSYQVINWRP PEDQEKKFAD LRHRLTEEIT YGRSKHHTLL KIHQYFGDLC 

       130        140        150        160        170        180 
SQLLSRKDIM DFLKNENFDL VLLDSMDLCS LLIVEKLGKR FVSFLPFQFS YMDFGLPSAP 

       190        200        210        220        230        240 
LSYAPVYGSG LTDQMDFWGR VKNFLMFLDF SMKQREILSQ YDSTIQEHFV EGSQPVLSDL 

       250        260        270        280        290        300 
LLKAELWFVN SDFALDFARP LFPNTVYVGG LLDKPVQPIP QDLENFISQF GDSGFVLVAL 

       310        320        330        340        350        360 
GSIVSMIQSK EIIKEMNSAF AHLPQGVLWT CKTSHWPKDV SLAPNVKIMD WLPQTDLLAH 

       370        380        390        400        410        420 
PSIRLFVTHG GMNSVMEAVH HGVPMVGIPF FFDQPENMVR VEAKNLGVSI QLQTLKAESF 

       430        440        450        460        470        480 
ALTMKKIIED KRYKSAAMAS KIIRHSHPLT PAQRLLGWID HILQTGGAAH LKPYAFQQPW 

       490        500        510        520 
HEQYMLDVFL FLLGLMLGTL WLSVKVLVAV TRYLSIATKV KEA 

« 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 Spleen.
[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: Kidney and 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK050128 mRNA. Translation: BAC34080.1.
AK143815 mRNA. Translation: BAE25548.1.
BC022134 mRNA. Translation: AAH22134.1.
BC024453 mRNA. Translation: AAH24453.1.
BC034837 mRNA. Translation: AAH34837.1.
RefSeqNP_659094.1. NM_144845.3.
UniGeneMm.422853.

3D structure databases

ProteinModelPortalQ8JZZ0.
SMRQ8JZZ0. Positions 230-462.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ8JZZ0. 2 interactions.
MINTMINT-4116696.

Protein family/group databases

CAZyGT1. Glycosyltransferase Family 1.

PTM databases

PhosphoSiteQ8JZZ0.

Proteomic databases

PaxDbQ8JZZ0.
PRIDEQ8JZZ0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000072403; ENSMUSP00000072236; ENSMUSG00000049152.
GeneID223337.
KEGGmmu:223337.
UCSCuc007vfl.1. mouse.

Organism-specific databases

CTD167127.
MGIMGI:2145969. Ugt3a2.

Phylogenomic databases

eggNOGCOG1819.
GeneTreeENSGT00560000076760.
HOGENOMHOG000220831.
HOVERGENHBG106370.
InParanoidQ8JZZ0.
OMAQYDSTIQ.
OrthoDBEOG7GBFWS.
PhylomeDBQ8JZZ0.
TreeFamTF315472.

Gene expression databases

BgeeQ8JZZ0.
CleanExMM_UGT3A2.
GenevestigatorQ8JZZ0.

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

NextBio376697.
PROQ8JZZ0.
SOURCESearch...

Entry information

Entry nameUD3A2_MOUSE
AccessionPrimary (citable) accession number: Q8JZZ0
Secondary accession number(s): A1A4B4, Q3UP49, Q8VC11
Entry history
Integrated into UniProtKB/Swiss-Prot: August 21, 2007
Last sequence update: August 21, 2007
Last modified: April 16, 2014
This is version 82 of the entry and version 2 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