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Q80X89 (UD2A1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 85. 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 2A1

Short name=UDPGT 2A1
EC=2.4.1.17
Gene names
Name:Ugt2a1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length528 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. Active on odorants and seems to be involved in olfaction; it could help clear lipophilic odorant molecules from the sensory epithelium.

Catalytic activity

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

Subcellular location

Cell membrane; Single-pass type I membrane protein Potential.

Sequence similarities

Belongs to the UDP-glycosyltransferase family.

Ontologies

Keywords
   Biological processOlfaction
Sensory transduction
   Cellular componentCell membrane
Membrane
   DomainSignal
Transmembrane
Transmembrane helix
   Molecular functionGlycosyltransferase
Transferase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processresponse to stimulus

Inferred from electronic annotation. Source: UniProtKB-KW

sensory perception of smell

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   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 – 2121 Potential
Chain22 – 528507UDP-glucuronosyltransferase 2A1
PRO_0000299143

Regions

Topological domain22 – 494473Extracellular Potential
Transmembrane495 – 51521Helical; Potential
Topological domain516 – 52813Cytoplasmic Potential

Amino acid modifications

Glycosylation491N-linked (GlcNAc...) Potential
Glycosylation3141N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict641Missing in AAG17003. Ref.1
Sequence conflict2081T → A in AAG17003. Ref.1
Sequence conflict5221G → R in AAG17003. Ref.1
Sequence conflict5271R → S in AAG17003. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q80X89 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: B53F1CB6680E2F95

FASTA52859,965
        10         20         30         40         50         60 
MLKNILLCSL QISLLGMSLG GNVLIWPMEG SHWLNVKIII DELLRKEHNV TVLVASGALF 

        70         80         90        100        110        120 
ITPSSISPSL TFEIYPVPFG KEKIESVIKD FVLTWLENRP SPSTIWTFYK EMAKVIEEFH 

       130        140        150        160        170        180 
LVSRGICDGV LKNEKLMSKL QKEKFEVLLS DPVFPCGDIV ALKLGIPFIY SLRFSPASTV 

       190        200        210        220        230        240 
EKHCGKVPFP PSYVPAILSE LTDQMSFTDR VRNFISYRMQ DYMFETLWKQ WDSYYTKALG 

       250        260        270        280        290        300 
RPTTLCETMG KAEIWLMRTY WDFEFPRPYL PNFEFVGGLH CKPAKPLPKE MEEFVQTSGE 

       310        320        330        340        350        360 
HGIVVFSLGS MVKNLTDEKA NLIASALAQI PQKVLWRYKG KIPDTLGSNT RLFDWIPQND 

       370        380        390        400        410        420 
LLGHPKTRAF ITHGGTNGIY EAIYHGIPMV GVPMFADQPD NIAHMKAKGA AVEVNMNTMT 

       430        440        450        460        470        480 
SSDLLNALRT VINEPSYKEN AMRLSRIHHD QPVKPLDRAV FWIEFVMRHK GAKHLRVAAH 

       490        500        510        520 
DLSWFQYHSL DVIGFLLACV ASAILLVAKC CLFIFQKVGK TGKKKKRD 

« Hide

References

« Hide 'large scale' references
[1]"Rat olfactory bulb and epithelium UDP-glucuronosyltransferase 2A1 (UGT2A1) expression: in situ mRNA localization and quantitative analysis."
Heydel J.-M., Leclerc S., Bernard P., Pelczar H., Gradinaru D., Magdalou J., Minn A., Artur Y., Goudonnet H.
Brain Res. Mol. Brain Res. 90:83-92(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
[2]"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: Head.
[3]"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].
Tissue: Olfactory epithelium.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF184901 mRNA. Translation: AAG17003.1.
AK140757 mRNA. Translation: BAE24468.1.
BC048926 mRNA. Translation: AAH48926.1.
CCDSCCDS39129.1.
RefSeqNP_444414.2. NM_053184.2.
UniGeneMm.26794.

3D structure databases

ProteinModelPortalQ80X89.
SMRQ80X89. Positions 223-446.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGT1. Glycosyltransferase Family 1.

PTM databases

PhosphoSiteQ80X89.

Proteomic databases

PaxDbQ80X89.
PRIDEQ80X89.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000147854; ENSMUSP00000114583; ENSMUSG00000029268.
GeneID94215.
KEGGmmu:94215.
UCSCuc008xyl.2. mouse.

Organism-specific databases

CTD10941.
MGIMGI:2149905. Ugt2a1.

Phylogenomic databases

eggNOGCOG1819.
GeneTreeENSGT00640000091260.
HOGENOMHOG000220831.
HOVERGENHBG004033.
KOK00699.
OMAARRQHAN.
PhylomeDBQ80X89.

Gene expression databases

BgeeQ80X89.
GenevestigatorQ80X89.

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

NextBio352183.
PROQ80X89.
SOURCESearch...

Entry information

Entry nameUD2A1_MOUSE
AccessionPrimary (citable) accession number: Q80X89
Secondary accession number(s): Q9ESE4
Entry history
Integrated into UniProtKB/Swiss-Prot: August 21, 2007
Last sequence update: June 1, 2003
Last modified: July 9, 2014
This is version 85 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