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Q9Z0J5

- TRXR2_RAT

UniProt

Q9Z0J5 - TRXR2_RAT

Protein

Thioredoxin reductase 2, mitochondrial

Gene

Txnrd2

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 3 (26 Feb 2008)
      Previous versions | rss
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    Functioni

    Maintains mitochondrial thioredoxin in a reduced state. Implicated in the defenses against oxidative stress. May play a role in redox-regulated cell signaling.1 Publication

    Catalytic activityi

    Thioredoxin + NADP+ = thioredoxin disulfide + NADPH.1 Publication

    Cofactori

    FAD.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei499 – 4991Proton acceptorBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi43 – 7230FADBy similarityAdd
    BLAST

    GO - Molecular functioni

    1. flavin adenine dinucleotide binding Source: InterPro
    2. NADP binding Source: InterPro
    3. protein dimerization activity Source: RGD
    4. protein homodimerization activity Source: UniProtKB
    5. thioredoxin-disulfide reductase activity Source: UniProtKB

    GO - Biological processi

    1. cell redox homeostasis Source: InterPro
    2. response to drug Source: RGD
    3. response to hydrogen peroxide Source: RGD
    4. response to hyperoxia Source: RGD
    5. response to oxygen radical Source: UniProtKB
    6. response to selenium ion Source: RGD

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein, NADP

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Thioredoxin reductase 2, mitochondrial (EC:1.8.1.9)
    Alternative name(s):
    Thioredoxin reductase TR3
    Gene namesi
    Name:Txnrd2
    Synonyms:Trxr2
    OrganismiRattus norvegicus (Rat)Imported
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi61960. Txnrd2.

    Subcellular locationi

    Mitochondrion 1 Publication

    GO - Cellular componenti

    1. axon Source: RGD
    2. cytoplasm Source: RGD
    3. dendrite Source: RGD
    4. mitochondrion Source: UniProtKB
    5. neuronal cell body Source: RGD

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3636Mitochondrion1 PublicationAdd
    BLAST
    Chaini37 – 526490Thioredoxin reductase 2, mitochondrialPRO_0000030290Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei81 – 811N6-succinyllysineBy similarity
    Disulfide bondi88 ↔ 93Redox-activeBy similarity
    Modified residuei177 – 1771N6-succinyllysineBy similarity
    Modified residuei331 – 3311N6-succinyllysineBy similarity
    Cross-linki524 ↔ 525Cysteinyl-selenocysteine (Cys-Sec)By similarity

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PaxDbiQ9Z0J5.
    PRIDEiQ9Z0J5.

    Expressioni

    Tissue specificityi

    Expressed in liver, kidney, adrenal gland and heart.1 Publication

    Gene expression databases

    GenevestigatoriQ9Z0J5.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000002593.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Z0J5.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Redox-active center, Transit peptide

    Phylogenomic databases

    eggNOGiCOG1249.
    HOGENOMiHOG000276712.
    HOVERGENiHBG004959.
    InParanoidiQ9Z0J5.
    KOiK00384.
    PhylomeDBiQ9Z0J5.

    Family and domain databases

    Gene3Di3.30.390.30. 1 hit.
    InterProiIPR016156. FAD/NAD-linked_Rdtase_dimer.
    IPR013027. FAD_pyr_nucl-diS_OxRdtase.
    IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
    IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
    IPR012999. Pyr_OxRdtase_I_AS.
    IPR001327. Pyr_OxRdtase_NAD-bd_dom.
    IPR006338. Thioredoxin/glutathione_Rdtase.
    [Graphical view]
    PfamiPF00070. Pyr_redox. 1 hit.
    PF07992. Pyr_redox_2. 1 hit.
    PF02852. Pyr_redox_dim. 1 hit.
    [Graphical view]
    PRINTSiPR00368. FADPNR.
    SUPFAMiSSF55424. SSF55424. 1 hit.
    TIGRFAMsiTIGR01438. TGR. 1 hit.
    PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9Z0J5-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAAIVAALRG SSGRFRPQTR VLTRGTRGAA GAASAAGGQQ NFDLLVIGGG    50
    SGGLACAKEA AQLGRKVAVA DYVEPSPRGT KWGLGGTCVN VGCIPKKLMH 100
    QAALLGGMIR DAQHYGWEVA QPVQHNWKAM AEAVQNHVKS LNWGHRVQLQ 150
    DRKVKYFNIK ASFVNEHTVH GVDKAGKVTQ LSAKHIVIAT GGRPKYPTQV 200
    KGALEHGITS DDIFWLKESP GKTLVVGASY VALECAGFLT GIGLDTTVMM 250
    RSVPLRGFDQ QMASLVTEHM ESHGTRFLKG CVPSLIRKLP TNQLQVTWED 300
    LASGKEDVGT FDTVLWAIGR VPETRNLNLE KAGVNTNPKN QKIIVDAQEA 350
    TSVPHIYAIG DVAEGRPELT PTAIKAGKLL AQRLFGKSST LMNYSNVPTT 400
    VFTPLEYGCV GLSEEEAVAL HGQEHIEVYH AYYKPLEFTV ADRDASQCYI 450
    KMVCMREPPQ LVLGLHFLGP NAGEVTQGFA LGIQCGASYA QVMQTVGIHP 500
    TCSEEVVKLH ISKRSGLDPT VTGCUG 526
    Length:526
    Mass (Da):56,575
    Last modified:February 26, 2008 - v3
    Checksum:iADEEBAD54BE6F241
    GO
    Isoform 2 (identifier: Q9Z0J5-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-38: MAAIVAALRGSSGRFRPQTRVLTRGTRGAAGAASAAGG → MEG

    Show »
    Length:491
    Mass (Da):53,239
    Checksum:i2700A49416B63831
    GO

    Mass spectrometryi

    Isoform 1 : Molecular mass is 53037±2 Da from positions 37 - 526. Determined by ESI. 1 Publication

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 3838MAAIV…SAAGG → MEG in isoform 2. CuratedVSP_008307Add
    BLAST

    Non-standard residue

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-standard residuei525 – 5251Selenocysteine1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF072865 mRNA. Translation: AAD13801.1.
    BC085734 mRNA. Translation: AAH85734.1.
    RefSeqiNP_072106.1. NM_022584.2. [Q9Z0J5-1]
    UniGeneiRn.6300.

    Genome annotation databases

    GeneIDi50551.
    KEGGirno:50551.

    Keywords - Coding sequence diversityi

    Alternative splicing, Selenocysteine

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF072865 mRNA. Translation: AAD13801.1 .
    BC085734 mRNA. Translation: AAH85734.1 .
    RefSeqi NP_072106.1. NM_022584.2. [Q9Z0J5-1 ]
    UniGenei Rn.6300.

    3D structure databases

    ProteinModelPortali Q9Z0J5.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10116.ENSRNOP00000002593.

    Chemistry

    BindingDBi Q9Z0J5.
    ChEMBLi CHEMBL5086.

    Proteomic databases

    PaxDbi Q9Z0J5.
    PRIDEi Q9Z0J5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 50551.
    KEGGi rno:50551.

    Organism-specific databases

    CTDi 10587.
    RGDi 61960. Txnrd2.

    Phylogenomic databases

    eggNOGi COG1249.
    HOGENOMi HOG000276712.
    HOVERGENi HBG004959.
    InParanoidi Q9Z0J5.
    KOi K00384.
    PhylomeDBi Q9Z0J5.

    Miscellaneous databases

    NextBioi 610344.
    PROi Q9Z0J5.

    Gene expression databases

    Genevestigatori Q9Z0J5.

    Family and domain databases

    Gene3Di 3.30.390.30. 1 hit.
    InterProi IPR016156. FAD/NAD-linked_Rdtase_dimer.
    IPR013027. FAD_pyr_nucl-diS_OxRdtase.
    IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
    IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
    IPR012999. Pyr_OxRdtase_I_AS.
    IPR001327. Pyr_OxRdtase_NAD-bd_dom.
    IPR006338. Thioredoxin/glutathione_Rdtase.
    [Graphical view ]
    Pfami PF00070. Pyr_redox. 1 hit.
    PF07992. Pyr_redox_2. 1 hit.
    PF02852. Pyr_redox_dim. 1 hit.
    [Graphical view ]
    PRINTSi PR00368. FADPNR.
    SUPFAMi SSF55424. SSF55424. 1 hit.
    TIGRFAMsi TIGR01438. TGR. 1 hit.
    PROSITEi PS00076. PYRIDINE_REDOX_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and characterization of a mitochondrial selenocysteine-containing thioredoxin reductase from rat liver."
      Lee S.-R., Kim J.-R., Kwon K.-S., Yoon H.W., Levine R.L., Ginsburg A., Rhee S.G.
      J. Biol. Chem. 274:4722-4734(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 37-55; 206-217; 343-362 AND 515-526, SELENOCYSTEINE AT SEC-525, FUNCTION, CATALYTIC ACTIVITY, MASS SPECTROMETRY, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Strain: Sprague-Dawley.
      Tissue: Liver.
    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] (ISOFORM 1).
      Tissue: Heart.
    3. "Heterogeneity within animal thioredoxin reductases: evidence for alternative first exon splicing."
      Sun Q.-A., Zappacosta F., Factor V.M., Wirth P.J., Hatfield D.L., Gladyshev V.N.
      J. Biol. Chem. 276:3106-3114(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING (ISOFORMS 1 AND 2).

    Entry informationi

    Entry nameiTRXR2_RAT
    AccessioniPrimary (citable) accession number: Q9Z0J5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 19, 2003
    Last sequence update: February 26, 2008
    Last modified: October 1, 2014
    This is version 121 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The active site is a redox-active disulfide bond. The selenocysteine residue is also essential for catalytic activity By similarity.By similarity

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3