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Q3UP75 (UD3A1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 69. 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 3A1

Short name=UDPGT 3A1
EC=2.4.1.17
Gene names
Name:Ugt3a1
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 3A1
PRO_0000299151

Regions

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

Amino acid modifications

Glycosylation701N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict3011G → D in AAH25940. Ref.2
Sequence conflict4451Q → N in AAH25940. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q3UP75 [UniParc].

Last modified October 11, 2005. Version 1.
Checksum: 8DE48C64EEFFDFCF

FASTA52359,698
        10         20         30         40         50         60 
MAAHRSWLLV SFFLLEVLLL EAAKILTIST LSASHYILMN RVSQILQGGG HDVIKLLYEG 

        70         80         90        100        110        120 
GDIPDFRKEN SSYQVINWRL PEDQQKTFEN RWHRLIDEYA YGRSKYHTLL KIHQYFADLC 

       130        140        150        160        170        180 
SHLLSRKDIM ELLQKENFDL VLLDSMDLCS FLIVEKLGKR FVSFLPFQFS YMDFGLPNAP 

       190        200        210        220        230        240 
LSYAPVYGSG LTDQMDFWGR VKNILMFFHF TKKRRDIFSQ YGNTVQEHFA EGSQPVLSDL 

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

       310        320        330        340        350        360 
GSVVSMIQSK EIIKEMNSAF AHLPQGVLWT CKSSHWPKDV SLAPNVKIMD WLPQIDLLAH 

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

       430        440        450        460        470        480 
LLTMKEVIED QRYKTAAMAS KVIRQSHPLT PAQRLVGWID HILQTGGAAH LKPYAFQQPW 

       490        500        510        520 
HEQYMLDVFL FLLGLTLGTL WLSVKVLVAV TRYLSISRKV KQA 

« 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: 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: 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
AK143745 mRNA. Translation: BAE25522.1.
BC025940 mRNA. Translation: AAH25940.1.
CCDSCCDS27374.1.
RefSeqNP_997099.2. NM_207216.2.
UniGeneMm.482274.

3D structure databases

ProteinModelPortalQ3UP75.
SMRQ3UP75. Positions 277-438.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-1863680.
STRING10090.ENSMUSP00000022861.

Protein family/group databases

CAZyGT1. Glycosyltransferase Family 1.

PTM databases

PhosphoSiteQ3UP75.

Proteomic databases

MaxQBQ3UP75.
PaxDbQ3UP75.
PRIDEQ3UP75.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000022861; ENSMUSP00000022861; ENSMUSG00000072664.
GeneID105887.
KEGGmmu:105887.
UCSCuc007vfk.2. mouse.

Organism-specific databases

CTD133688.
MGIMGI:2146055. Ugt3a1.

Phylogenomic databases

eggNOGCOG1819.
GeneTreeENSGT00560000076760.
HOGENOMHOG000220831.
HOVERGENHBG106370.
InParanoidQ3UP75.
OMASIMETIQ.
OrthoDBEOG7GBFWS.
PhylomeDBQ3UP75.
TreeFamTF315472.

Gene expression databases

ArrayExpressQ3UP75.
BgeeQ3UP75.
GenevestigatorQ3UP75.

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

NextBio357954.
PROQ3UP75.
SOURCESearch...

Entry information

Entry nameUD3A1_MOUSE
AccessionPrimary (citable) accession number: Q3UP75
Secondary accession number(s): Q8R0Y5
Entry history
Integrated into UniProtKB/Swiss-Prot: August 21, 2007
Last sequence update: October 11, 2005
Last modified: July 9, 2014
This is version 69 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