Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Thioredoxin reductase 2, mitochondrial

Gene

TXNRD2

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Maintains 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.

Cofactori

FAD1 Publication

Enzyme regulationi

Inhibited by 1-chloro-2,4-dinitrobenzene and by zinc, calcium, magnesium and Fe2+ ions.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei484 – 4841Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi29 – 5830FADBy similarityAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • cell redox homeostasis Source: InterPro
  • cellular oxidant detoxification Source: GOC
  • response to oxygen radical Source: UniProtKB
Complete GO annotation...

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
OrganismiBos taurus (Bovine)Imported
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2121Mitochondrion1 PublicationAdd
BLAST
Chaini22 – 511490Thioredoxin reductase 2, mitochondrialPRO_0000030287Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi74 ↔ 79Redox-activeBy similarity
Modified residuei316 – 3161N6-succinyllysineBy similarity
Cross-linki509 ↔ 510Cysteinyl-selenocysteine (Cys-Sec)By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiQ9N2I8.

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ9N2I8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center, Transit peptide

Phylogenomic databases

HOVERGENiHBG004959.
InParanoidiQ9N2I8.
KOiK00384.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
IPR006338. Thioredoxin/glutathione_Rdtase.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.
SSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR01438. TGR. 1 hit.
PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9N2I8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAALRGAAAR FRGRAPGGAR GAAGRQCYDL LVIGGGSGGL ACAKEAAQLG
60 70 80 90 100
KKVAVLDYVE PSPQGTRWGL GGTCVNVGCI PKKLMHQAAL LGGMIRDAPH
110 120 130 140 150
YGWGVAQAPH SWATLADAVQ NHVKSLNWGH RIQLQDRKVK YFNVKASFVD
160 170 180 190 200
THTVCGVSKG GEETLLSAEH IVIATGGRPR YPTHIEGALE YGITSDDLFW
210 220 230 240 250
LKESPGKTLV VGASYVALEC AGLLTGLGLD TTVMIRSVPL RAFDQQMASL
260 270 280 290 300
VTEHMAGHGT RILRGCAPEK VEKLPGQQLR VTWVDLTSDR KDAGTFDTVL
310 320 330 340 350
WAIGRVPETA SLNLEKAGVH TNPVTGKILV DAQETTSVPH IYAIGDVAEG
360 370 380 390 400
RPELTPTAIM AGRLLAQRLS GRTSDLMDYS SVPTTVFTPL EYGCVGLSEE
410 420 430 440 450
AAVARHGEEH VEVYHAFYKP LEFTVPQRDA SQCYIKMVCL REPPQLVLGL
460 470 480 490 500
HFLGPNAGEV IQGFALGIKC GASYQQLMRT VGIHPTCAEE VAKLRISKRS
510
GLDPTVTGCU G
Length:511
Mass (Da):54,670
Last modified:February 26, 2008 - v2
Checksum:iCA74A147B32846ED
GO

Non-standard residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-standard residuei510 – 5101Selenocysteine1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB022283 mRNA. Translation: BAA82153.1.
RefSeqiNP_777051.1. NM_174626.2.
UniGeneiBt.4008.

Genome annotation databases

GeneIDi282389.
KEGGibta:282389.

Keywords - Coding sequence diversityi

Selenocysteine

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB022283 mRNA. Translation: BAA82153.1.
RefSeqiNP_777051.1. NM_174626.2.
UniGeneiBt.4008.

3D structure databases

ProteinModelPortaliQ9N2I8.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ9N2I8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi282389.
KEGGibta:282389.

Organism-specific databases

CTDi10587.

Phylogenomic databases

HOVERGENiHBG004959.
InParanoidiQ9N2I8.
KOiK00384.

Miscellaneous databases

NextBioi20806177.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.50.50.60. 2 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
IPR006338. Thioredoxin/glutathione_Rdtase.
[Graphical view]
PfamiPF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.
SSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR01438. TGR. 1 hit.
PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Mitochondrial thioredoxin reductase in bovine adrenal cortex. Its purification, properties, nucleotide/amino acid sequences, and identification of selenocysteine."
    Watabe S., Makino Y., Ogawa K., Hiroi T., Yamamoto Y., Takahashi S.Y.
    Eur. J. Biochem. 264:74-84(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 22-35; 53-82; 160-181; 208-238; 292-316; 328-340; 420-436; 470-488 AND 499-510, SELENOCYSTEINE AT SEC-510, FUNCTION, SUBCELLULAR LOCATION, ENZYME REGULATION.
    Tissue: Adrenal cortex.

Entry informationi

Entry nameiTRXR2_BOVIN
AccessioniPrimary (citable) accession number: Q9N2I8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2003
Last sequence update: February 26, 2008
Last modified: February 17, 2016
This is version 108 of the entry and version 2 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

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 one 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.