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Q80X89

- UD2A1_MOUSE

UniProt

Q80X89 - UD2A1_MOUSE

Protein

UDP-glucuronosyltransferase 2A1

Gene

Ugt2a1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 86 (01 Oct 2014)
      Sequence version 1 (01 Jun 2003)
      Previous versions | rss
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    Functioni

    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 activityi

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

    GO - Molecular functioni

    1. glucuronosyltransferase activity Source: UniProtKB-EC

    GO - Biological processi

    1. response to stimulus Source: UniProtKB-KW
    2. sensory perception of smell Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Biological processi

    Olfaction, Sensory transduction

    Protein family/group databases

    CAZyiGT1. Glycosyltransferase Family 1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    UDP-glucuronosyltransferase 2A1 (EC:2.4.1.17)
    Short name:
    UDPGT 2A1
    Gene namesi
    Name:Ugt2a1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 5

    Organism-specific databases

    MGIiMGI:2149905. Ugt2a1.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121Sequence AnalysisAdd
    BLAST
    Chaini22 – 528507UDP-glucuronosyltransferase 2A1PRO_0000299143Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi49 – 491N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi314 – 3141N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PaxDbiQ80X89.
    PRIDEiQ80X89.

    PTM databases

    PhosphoSiteiQ80X89.

    Expressioni

    Gene expression databases

    BgeeiQ80X89.
    GenevestigatoriQ80X89.

    Structurei

    3D structure databases

    ProteinModelPortaliQ80X89.
    SMRiQ80X89. Positions 223-446.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini22 – 494473ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini516 – 52813CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei495 – 51521HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the UDP-glycosyltransferase family.Curated

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG1819.
    GeneTreeiENSGT00640000091260.
    HOGENOMiHOG000220831.
    HOVERGENiHBG004033.
    KOiK00699.
    OMAiARRQHAN.
    PhylomeDBiQ80X89.

    Family and domain databases

    InterProiIPR002213. UDP_glucos_trans.
    [Graphical view]
    PANTHERiPTHR11926. PTHR11926. 1 hit.
    PfamiPF00201. UDPGT. 1 hit.
    [Graphical view]
    PROSITEiPS00375. UDPGT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q80X89-1 [UniParc]FASTAAdd to Basket

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    MLKNILLCSL QISLLGMSLG GNVLIWPMEG SHWLNVKIII DELLRKEHNV    50
    TVLVASGALF ITPSSISPSL TFEIYPVPFG KEKIESVIKD FVLTWLENRP 100
    SPSTIWTFYK EMAKVIEEFH LVSRGICDGV LKNEKLMSKL QKEKFEVLLS 150
    DPVFPCGDIV ALKLGIPFIY SLRFSPASTV EKHCGKVPFP PSYVPAILSE 200
    LTDQMSFTDR VRNFISYRMQ DYMFETLWKQ WDSYYTKALG RPTTLCETMG 250
    KAEIWLMRTY WDFEFPRPYL PNFEFVGGLH CKPAKPLPKE MEEFVQTSGE 300
    HGIVVFSLGS MVKNLTDEKA NLIASALAQI PQKVLWRYKG KIPDTLGSNT 350
    RLFDWIPQND LLGHPKTRAF ITHGGTNGIY EAIYHGIPMV GVPMFADQPD 400
    NIAHMKAKGA AVEVNMNTMT SSDLLNALRT VINEPSYKEN AMRLSRIHHD 450
    QPVKPLDRAV FWIEFVMRHK GAKHLRVAAH DLSWFQYHSL DVIGFLLACV 500
    ASAILLVAKC CLFIFQKVGK TGKKKKRD 528
    Length:528
    Mass (Da):59,965
    Last modified:June 1, 2003 - v1
    Checksum:iB53F1CB6680E2F95
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti64 – 641Missing in AAG17003. (PubMed:11376859)Curated
    Sequence conflicti208 – 2081T → A in AAG17003. (PubMed:11376859)Curated
    Sequence conflicti522 – 5221G → R in AAG17003. (PubMed:11376859)Curated
    Sequence conflicti527 – 5271R → S in AAG17003. (PubMed:11376859)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF184901 mRNA. Translation: AAG17003.1.
    AK140757 mRNA. Translation: BAE24468.1.
    BC048926 mRNA. Translation: AAH48926.1.
    CCDSiCCDS39129.1.
    RefSeqiNP_444414.2. NM_053184.2.
    UniGeneiMm.26794.

    Genome annotation databases

    EnsembliENSMUST00000147854; ENSMUSP00000114583; ENSMUSG00000029268.
    GeneIDi94215.
    KEGGimmu:94215.
    UCSCiuc008xyl.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF184901 mRNA. Translation: AAG17003.1 .
    AK140757 mRNA. Translation: BAE24468.1 .
    BC048926 mRNA. Translation: AAH48926.1 .
    CCDSi CCDS39129.1.
    RefSeqi NP_444414.2. NM_053184.2.
    UniGenei Mm.26794.

    3D structure databases

    ProteinModelPortali Q80X89.
    SMRi Q80X89. Positions 223-446.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GT1. Glycosyltransferase Family 1.

    PTM databases

    PhosphoSitei Q80X89.

    Proteomic databases

    PaxDbi Q80X89.
    PRIDEi Q80X89.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000147854 ; ENSMUSP00000114583 ; ENSMUSG00000029268 .
    GeneIDi 94215.
    KEGGi mmu:94215.
    UCSCi uc008xyl.2. mouse.

    Organism-specific databases

    CTDi 10941.
    MGIi MGI:2149905. Ugt2a1.

    Phylogenomic databases

    eggNOGi COG1819.
    GeneTreei ENSGT00640000091260.
    HOGENOMi HOG000220831.
    HOVERGENi HBG004033.
    KOi K00699.
    OMAi ARRQHAN.
    PhylomeDBi Q80X89.

    Miscellaneous databases

    NextBioi 352183.
    PROi Q80X89.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q80X89.
    Genevestigatori Q80X89.

    Family and domain databases

    InterProi IPR002213. UDP_glucos_trans.
    [Graphical view ]
    PANTHERi PTHR11926. PTHR11926. 1 hit.
    Pfami PF00201. UDPGT. 1 hit.
    [Graphical view ]
    PROSITEi PS00375. UDPGT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.

    Entry informationi

    Entry nameiUD2A1_MOUSE
    AccessioniPrimary (citable) accession number: Q80X89
    Secondary accession number(s): Q9ESE4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 21, 2007
    Last sequence update: June 1, 2003
    Last modified: October 1, 2014
    This is version 86 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3