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Protein

Thioredoxin reductase 2, mitochondrial

Gene

Txnrd2

Organism
Mus musculus (Mouse)
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.

Catalytic activityi

Thioredoxin + NADP+ = thioredoxin disulfide + NADPH.

Cofactori

FADUniRule annotationCurated

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei497Proton acceptorBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi41 – 70FADBy similarityAdd BLAST30

GO - Molecular functioni

GO - Biological processi

  • cell redox homeostasis Source: InterPro
  • heart development Source: MGI
  • hemopoiesis Source: MGI
  • response to oxygen radical Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NADP

Enzyme and pathway databases

BRENDAi1.8.1.9. 3474.

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
OrganismiMus musculus (Mouse)Imported
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1347023. Txnrd2.

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 34Mitochondrion1 PublicationAdd BLAST34
ChainiPRO_000003028935 – 524Thioredoxin reductase 2, mitochondrialAdd BLAST490

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei79N6-succinyllysineCombined sources1
Disulfide bondi86 ↔ 91Redox-activeBy similarity
Modified residuei175N6-succinyllysineCombined sources1
Modified residuei329N6-succinyllysineCombined sources1
Cross-linki522 ↔ 523Cysteinyl-selenocysteine (Cys-Sec)By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiQ9JLT4.
PeptideAtlasiQ9JLT4.
PRIDEiQ9JLT4.

PTM databases

iPTMnetiQ9JLT4.
PhosphoSitePlusiQ9JLT4.

Expressioni

Tissue specificityi

Expressed in liver, heart, testis and kidney.3 Publications

Gene expression databases

BgeeiENSMUSG00000075704.
CleanExiMM_TXNRD2.
GenevisibleiQ9JLT4. MM.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

IntActiQ9JLT4. 4 interactors.
MINTiMINT-1862055.
STRINGi10090.ENSMUSP00000111269.

Structurei

Secondary structure

1524
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi39 – 45Combined sources7
Helixi49 – 60Combined sources12
Beta strandi65 – 68Combined sources4
Helixi85 – 89Combined sources5
Helixi91 – 112Combined sources22
Helixi125 – 149Combined sources25
Beta strandi153 – 155Combined sources3
Beta strandi158 – 170Combined sources13
Beta strandi176 – 186Combined sources11
Beta strandi190 – 192Combined sources3
Helixi201 – 204Combined sources4
Helixi208 – 211Combined sources4
Beta strandi220 – 224Combined sources5
Helixi228 – 239Combined sources12
Beta strandi244 – 250Combined sources7
Turni252 – 255Combined sources4
Helixi258 – 270Combined sources13
Beta strandi274 – 277Combined sources4
Beta strandi279 – 286Combined sources8
Beta strandi292 – 298Combined sources7
Turni299 – 301Combined sources3
Beta strandi304 – 314Combined sources11
Beta strandi318 – 321Combined sources4
Helixi323 – 325Combined sources3
Helixi327 – 330Combined sources4
Beta strandi336 – 338Combined sources3
Beta strandi345 – 348Combined sources4
Beta strandi354 – 356Combined sources3
Helixi358 – 360Combined sources3
Beta strandi361 – 364Combined sources4
Helixi368 – 383Combined sources16
Beta strandi397 – 399Combined sources3
Beta strandi401 – 409Combined sources9
Helixi412 – 419Combined sources8
Helixi421 – 423Combined sources3
Beta strandi424 – 430Combined sources7
Helixi434 – 438Combined sources5
Beta strandi447 – 455Combined sources9
Beta strandi459 – 467Combined sources9
Helixi470 – 482Combined sources13
Helixi487 – 491Combined sources5
Helixi502 – 505Combined sources4
Turni511 – 514Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ZDLX-ray3.00A31-522[»]
1ZKQX-ray2.60A31-522[»]
3DGZX-ray2.25A34-521[»]
ProteinModelPortaliQ9JLT4.
SMRiQ9JLT4.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9JLT4.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center, Transit peptide

Phylogenomic databases

eggNOGiKOG0405. Eukaryota.
COG1249. LUCA.
HOGENOMiHOG000276712.
HOVERGENiHBG004959.
InParanoidiQ9JLT4.
KOiK00384.
OrthoDBiEOG091G03IU.
TreeFamiTF314782.

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. 3 hits.
SSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR01438. TGR. 1 hit.
PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9JLT4-1) [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
MVAAMVAALR GPSRRFRPRT RALTRGTRGA ASAAGGQQSF DLLVIGGGSG
60 70 80 90 100
GLACAKEAAQ LGKKVAVADY VEPSPRGTKW GLGGTCVNVG CIPKKLMHQA
110 120 130 140 150
ALLGGMIRDA HHYGWEVAQP VQHNWKTMAE AVQNHVKSLN WGHRVQLQDR
160 170 180 190 200
KVKYFNIKAS FVDEHTVRGV DKGGKATLLS AEHIVIATGG RPRYPTQVKG
210 220 230 240 250
ALEYGITSDD IFWLKESPGK TLVVGASYVA LECAGFLTGI GLDTTVMMRS
260 270 280 290 300
IPLRGFDQQM SSLVTEHMES HGTQFLKGCV PSHIKKLPTN QLQVTWEDHA
310 320 330 340 350
SGKEDTGTFD TVLWAIGRVP ETRTLNLEKA GISTNPKNQK IIVDAQEATS
360 370 380 390 400
VPHIYAIGDV AEGRPELTPT AIKAGKLLAQ RLFGKSSTLM DYSNVPTTVF
410 420 430 440 450
TPLEYGCVGL SEEEAVALHG QEHVEVYHAY YKPLEFTVAD RDASQCYIKM
460 470 480 490 500
VCMREPPQLV LGLHFLGPNA GEVTQGFALG IKCGASYAQV MQTVGIHPTC
510 520
SEEVVKLHIS KRSGLEPTVT GCUG
Length:524
Mass (Da):56,603
Last modified:February 26, 2008 - v4
Checksum:i74D4713DC8EF6A80
GO
Isoform 2 (identifier: Q9JLT4-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-36: MVAAMVAALRGPSRRFRPRTRALTRGTRGAASAAGG → MEG

Show »
Length:491
Mass (Da):53,240
Checksum:i7CADE2DB621459E5
GO
Isoform 3 (identifier: Q9JLT4-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     318-356: RVPETRTLNL...EATSVPHIYA → KDAASHTDTV...TSWILHSAGS
     357-524: Missing.

Note: No experimental confirmation available.
Show »
Length:356
Mass (Da):38,475
Checksum:iD9DAA8F46B034082
GO
Isoform 4 (identifier: Q9JLT4-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     395-425: Missing.

Show »
Length:493
Mass (Da):53,279
Checksum:i7BFA5DCA255CD55D
GO

Sequence cautioni

The sequence AAF03359 differs from that shown. Reason: Erroneous initiation.Curated
The sequence AAH52157 differs from that shown. Reason: Erroneous initiation.Curated
The sequence AAL90457 differs from that shown. Reason: Erroneous initiation.Curated
The sequence AAQ03230 differs from that shown. Reason: Erroneous initiation.Curated
The sequence BAA86986 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti4 – 6AMV → GRMW in AAF03359 (PubMed:10500251).Curated3

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0082931 – 36MVAAM…SAAGG → MEG in isoform 2. CuratedAdd BLAST36
Alternative sequenceiVSP_008294318 – 356RVPET…PHIYA → KDAASHTDTVSSSRKPYFLG RRVFAFLPITSWILHSAGS in isoform 3. 1 PublicationAdd BLAST39
Alternative sequenceiVSP_008295357 – 524Missing in isoform 3. 1 PublicationAdd BLAST168
Alternative sequenceiVSP_008296395 – 425Missing in isoform 4. 1 PublicationAdd BLAST31

Non-standard residue

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-standard residuei523SelenocysteineBy similarity1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF136399 mRNA. Translation: AAF03359.1. Different initiation.
AF171053 mRNA. Translation: AAD51323.1.
AB027566 mRNA. Translation: BAA86986.2. Different initiation.
AF414359
, AF414356, AF414357, AF414358 Genomic DNA. Translation: AAL90457.1. Different initiation.
AF412308 mRNA. Translation: AAQ03230.1. Different initiation.
BC013688 mRNA. Translation: AAH13688.1.
BC052157 mRNA. Translation: AAH52157.3. Different initiation.
RefSeqiNP_038739.2. NM_013711.3.
UniGeneiMm.390906.

Genome annotation databases

GeneIDi26462.
KEGGimmu:26462.
UCSCiuc007ynx.1. mouse. [Q9JLT4-3]
uc007yny.1. mouse. [Q9JLT4-1]

Keywords - Coding sequence diversityi

Alternative splicing, Selenocysteine

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF136399 mRNA. Translation: AAF03359.1. Different initiation.
AF171053 mRNA. Translation: AAD51323.1.
AB027566 mRNA. Translation: BAA86986.2. Different initiation.
AF414359
, AF414356, AF414357, AF414358 Genomic DNA. Translation: AAL90457.1. Different initiation.
AF412308 mRNA. Translation: AAQ03230.1. Different initiation.
BC013688 mRNA. Translation: AAH13688.1.
BC052157 mRNA. Translation: AAH52157.3. Different initiation.
RefSeqiNP_038739.2. NM_013711.3.
UniGeneiMm.390906.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ZDLX-ray3.00A31-522[»]
1ZKQX-ray2.60A31-522[»]
3DGZX-ray2.25A34-521[»]
ProteinModelPortaliQ9JLT4.
SMRiQ9JLT4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9JLT4. 4 interactors.
MINTiMINT-1862055.
STRINGi10090.ENSMUSP00000111269.

PTM databases

iPTMnetiQ9JLT4.
PhosphoSitePlusiQ9JLT4.

Proteomic databases

PaxDbiQ9JLT4.
PeptideAtlasiQ9JLT4.
PRIDEiQ9JLT4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi26462.
KEGGimmu:26462.
UCSCiuc007ynx.1. mouse. [Q9JLT4-3]
uc007yny.1. mouse. [Q9JLT4-1]

Organism-specific databases

CTDi10587.
MGIiMGI:1347023. Txnrd2.

Phylogenomic databases

eggNOGiKOG0405. Eukaryota.
COG1249. LUCA.
HOGENOMiHOG000276712.
HOVERGENiHBG004959.
InParanoidiQ9JLT4.
KOiK00384.
OrthoDBiEOG091G03IU.
TreeFamiTF314782.

Enzyme and pathway databases

BRENDAi1.8.1.9. 3474.

Miscellaneous databases

EvolutionaryTraceiQ9JLT4.
PROiQ9JLT4.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000075704.
CleanExiMM_TXNRD2.
GenevisibleiQ9JLT4. MM.

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. 3 hits.
SSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR01438. TGR. 1 hit.
PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTRXR2_MOUSE
AccessioniPrimary (citable) accession number: Q9JLT4
Secondary accession number(s): Q6KG49
, Q80VZ4, Q91YX4, Q9JHA7, Q9JMH5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2003
Last sequence update: February 26, 2008
Last modified: November 2, 2016
This is version 144 of the entry and version 4 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.