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Protein

Thioredoxin reductase 2, mitochondrial

Gene

Txnrd2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

FAD1 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. mercury (II) reductase activity Source: InterPro
  3. mercury ion binding Source: InterPro
  4. NADP binding Source: InterPro
  5. protein dimerization activity Source: RGD
  6. protein homodimerization activity Source: UniProtKB
  7. thioredoxin-disulfide reductase activity Source: UniProtKB

GO - Biological processi

  1. cell redox homeostasis Source: InterPro
  2. detoxification of mercury ion Source: InterPro
  3. response to drug Source: RGD
  4. response to hydrogen peroxide Source: RGD
  5. response to hyperoxia Source: RGD
  6. response to oxygen radical Source: UniProtKB
  7. response to selenium ion Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NADP

Enzyme and pathway databases

BRENDAi1.8.1.9. 5301.

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 Componenti: Unplaced

Organism-specific databases

RGDi61960. Txnrd2.

Subcellular locationi

  1. 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
Complete GO annotation...

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.
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]
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. AlignAdd to basket

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

        10         20         30         40         50
MAAIVAALRG SSGRFRPQTR VLTRGTRGAA GAASAAGGQQ NFDLLVIGGG
60 70 80 90 100
SGGLACAKEA AQLGRKVAVA DYVEPSPRGT KWGLGGTCVN VGCIPKKLMH
110 120 130 140 150
QAALLGGMIR DAQHYGWEVA QPVQHNWKAM AEAVQNHVKS LNWGHRVQLQ
160 170 180 190 200
DRKVKYFNIK ASFVNEHTVH GVDKAGKVTQ LSAKHIVIAT GGRPKYPTQV
210 220 230 240 250
KGALEHGITS DDIFWLKESP GKTLVVGASY VALECAGFLT GIGLDTTVMM
260 270 280 290 300
RSVPLRGFDQ QMASLVTEHM ESHGTRFLKG CVPSLIRKLP TNQLQVTWED
310 320 330 340 350
LASGKEDVGT FDTVLWAIGR VPETRNLNLE KAGVNTNPKN QKIIVDAQEA
360 370 380 390 400
TSVPHIYAIG DVAEGRPELT PTAIKAGKLL AQRLFGKSST LMNYSNVPTT
410 420 430 440 450
VFTPLEYGCV GLSEEEAVAL HGQEHIEVYH AYYKPLEFTV ADRDASQCYI
460 470 480 490 500
KMVCMREPPQ LVLGLHFLGP NAGEVTQGFA LGIQCGASYA QVMQTVGIHP
510 520
TCSEEVVKLH ISKRSGLDPT VTGCUG
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
AF072865 mRNA. Translation: AAD13801.1.
BC085734 mRNA. Translation: AAH85734.1.
RefSeqiNP_072106.1. NM_022584.2. [Q9Z0J5-1]
UniGeneiRn.6300.

3D structure databases

ProteinModelPortaliQ9Z0J5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000002593.

Chemistry

BindingDBiQ9Z0J5.
ChEMBLiCHEMBL5086.

Proteomic databases

PaxDbiQ9Z0J5.
PRIDEiQ9Z0J5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi50551.
KEGGirno:50551.

Organism-specific databases

CTDi10587.
RGDi61960. Txnrd2.

Phylogenomic databases

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

Enzyme and pathway databases

BRENDAi1.8.1.9. 5301.

Miscellaneous databases

NextBioi610344.
PROiQ9Z0J5.

Gene expression databases

GenevestigatoriQ9Z0J5.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
InterProiIPR016156. FAD/NAD-linked_Rdtase_dimer.
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]
SUPFAMiSSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR01438. TGR. 1 hit.
PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: April 29, 2015
This is version 126 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.