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Protein

Thioredoxin reductase 3

Gene

TXNRD3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Displays thioredoxin reductase, glutaredoxin and glutathione reductase activities. Catalyzes disulfide bond isomerization. Promotes disulfide bond formation between GPX4 and various sperm proteins and may play a role in sperm maturation by promoting formation of sperm structural components (By similarity).By similarity

Miscellaneous

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

Catalytic activityi

Thioredoxin + NADP+ = thioredoxin disulfide + NADPH.By similarity

Cofactori

FADBy similarityNote: Binds 1 FAD per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei616Proton acceptorBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi158 – 187FADBy similarityAdd BLAST30

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionDevelopmental protein, Oxidoreductase
Biological processDifferentiation, Electron transport, Spermatogenesis, Transport
LigandFAD, Flavoprotein, NADP

Enzyme and pathway databases

BRENDAi1.8.1.9. 2681.

Names & Taxonomyi

Protein namesi
Recommended name:
Thioredoxin reductase 3 (EC:1.8.1.9)
Alternative name(s):
Thioredoxin and glutathione reductase
Thioredoxin reductase TR2
Gene namesi
Name:TXNRD3Imported
Synonyms:TGRBy similarity, TRXR3Imported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:20667. TXNRD3.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Microsome, Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi114112.
OpenTargetsiENSG00000197763.
PharmGKBiPA134920642.

Chemistry databases

ChEMBLiCHEMBL2096978.

Polymorphism and mutation databases

DMDMi510120859.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003206951 – 643Thioredoxin reductase 3Add BLAST643

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei26Asymmetric dimethylarginine; alternateBy similarity1
Modified residuei26Omega-N-methylarginine; alternateBy similarity1
Modified residuei41PhosphoserineCombined sources1
Modified residuei42PhosphoserineCombined sources1
Disulfide bondi203 ↔ 208Redox-activeBy similarity
Modified residuei379N6-succinyllysineBy similarity1
Cross-linki641 ↔ 642Cysteinyl-selenocysteine (Cys-Sec)By similarity

Keywords - PTMi

Disulfide bond, Methylation, Phosphoprotein

Proteomic databases

EPDiQ86VQ6.
MaxQBiQ86VQ6.
PaxDbiQ86VQ6.
PeptideAtlasiQ86VQ6.
PRIDEiQ86VQ6.

PTM databases

iPTMnetiQ86VQ6.
PhosphoSitePlusiQ86VQ6.

Expressioni

Gene expression databases

CleanExiHS_TXNRD3.

Organism-specific databases

HPAiHPA036109.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi9606.ENSP00000430031.

Chemistry databases

BindingDBiQ86VQ6.

Structurei

Secondary structure

1643
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi53 – 65Combined sources13
Beta strandi67 – 72Combined sources6
Helixi77 – 88Combined sources12
Beta strandi94 – 97Combined sources4
Turni98 – 100Combined sources3
Helixi104 – 115Combined sources12
Beta strandi122 – 125Combined sources4
Beta strandi128 – 132Combined sources5
Helixi133 – 142Combined sources10
Helixi144 – 150Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3H8QX-ray2.21A/B51-156[»]
ProteinModelPortaliQ86VQ6.
SMRiQ86VQ6.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ86VQ6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini56 – 156GlutaredoxinPROSITE-ProRule annotationAdd BLAST101

Domaini

The N-terminal glutaredoxin domain does not contain the C-X-X-C redox-active motif normally found in glutaredoxins but activity may be mediated through a single cysteine. The C-terminal Cys-Sec motif of one subunit of the homodimer may transfer electrons from the thiol-disulfide center to the glutaredoxin domain of the other subunit (By similarity).By similarity

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiKOG1752. Eukaryota.
KOG4716. Eukaryota.
COG1249. LUCA.
GeneTreeiENSGT00390000007578.
HOGENOMiHOG000276712.
HOVERGENiHBG004959.
InParanoidiQ86VQ6.
KOiK00384.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.50.50.60. 2 hits.
InterProiView protein in InterPro
IPR023753. FAD/NAD-binding_dom.
IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR002109. Glutaredoxin.
IPR011899. Glutaredoxin_euk/vir.
IPR001100. Pyr_nuc-diS_OxRdtase.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
IPR012336. Thioredoxin-like_fold.
IPR006338. Thioredoxin/glutathione_Rdtase.
PfamiView protein in Pfam
PF00462. Glutaredoxin. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
PIRSFiPIRSF000350. Mercury_reductase_MerA. 1 hit.
SUPFAMiSSF51905. SSF51905. 3 hits.
SSF52833. SSF52833. 1 hit.
SSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR02180. GRX_euk. 1 hit.
TIGR01438. TGR. 1 hit.
PROSITEiView protein in PROSITE
PS51354. GLUTAREDOXIN_2. 1 hit.
PS00076. PYRIDINE_REDOX_1. 1 hit.

Sequencei

Sequence statusi: Complete.

Q86VQ6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MERSPPQSPG PGKAGDAPNR RSGHVRGARV LSPPGRRARL SSPGPSRSSE
60 70 80 90 100
AREELRRHLV GLIERSRVVI FSKSYCPHST RVKELFSSLG VECNVLELDQ
110 120 130 140 150
VDDGARVQEV LSEITNQKTV PNIFVNKVHV GGCDQTFQAY QSGLLQKLLQ
160 170 180 190 200
EDLAYDYDLI IIGGGSGGLS CAKEAAILGK KVMVLDFVVP SPQGTSWGLG
210 220 230 240 250
GTCVNVGCIP KKLMHQAALL GQALCDSRKF GWEYNQQVRH NWETMTKAIQ
260 270 280 290 300
NHISSLNWGY RLSLREKAVA YVNSYGEFVE HHKIKATNKK GQETYYTAAQ
310 320 330 340 350
FVIATGERPR YLGIQGDKEY CITSDDLFSL PYCPGKTLVV GASYVALECA
360 370 380 390 400
GFLAGFGLDV TVMVRSILLR GFDQEMAEKV GSYMEQHGVK FLRKFIPVMV
410 420 430 440 450
QQLEKGSPGK LKVLAKSTEG TETIEGVYNT VLLAIGRDSC TRKIGLEKIG
460 470 480 490 500
VKINEKSGKI PVNDVEQTNV PYVYAVGDIL EDKPELTPVA IQSGKLLAQR
510 520 530 540 550
LFGASLEKCD YINVPTTVFT PLEYGCCGLS EEKAIEVYKK ENLEIYHTLF
560 570 580 590 600
WPLEWTVAGR ENNTCYAKII CNKFDHDRVI GFHILGPNAG EVTQGFAAAM
610 620 630 640
KCGLTKQLLD DTIGIHPTCG EVFTTLEITK SSGLDITQKG CUG
Length:643
Mass (Da):70,683
Last modified:May 29, 2013 - v4
Checksum:i6FB04128943A4017
GO

Sequence cautioni

The sequence AAH30028 differs from that shown. Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.Curated
The sequence AAH30028 differs from that shown. Reason: Erroneous termination at position 642. Translated as Sec.Curated
The sequence AAH50032 differs from that shown. Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.Curated
The sequence AAH50032 differs from that shown. Reason: Erroneous termination at position 642. Translated as Sec.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti65 – 66RS → AE in AAD51325 (PubMed:10455115).Curated2
Sequence conflicti246T → I in AAH30028 (PubMed:15489334).Curated1
Sequence conflicti337T → P in AAD39929 (Ref. 4) Curated1

Non-standard residue

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-standard residuei642Selenocysteine1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC024558 Genomic DNA. No translation available.
BC030028 mRNA. Translation: AAH30028.1. Sequence problems.
BC050032 mRNA. Translation: AAH50032.1. Sequence problems.
AF171055 mRNA. Translation: AAD51325.1.
AF133519 mRNA. Translation: AAD39929.1.
CCDSiCCDS77811.1.
RefSeqiNP_001166984.1. NM_001173513.1.
NP_443115.1. NM_052883.1.
UniGeneiHs.477475.

Genome annotation databases

EnsembliENST00000640433; ENSP00000492093; ENSG00000197763.
GeneIDi114112.
KEGGihsa:114112.

Keywords - Coding sequence diversityi

Selenocysteine

Similar proteinsi

Entry informationi

Entry nameiTRXR3_HUMAN
AccessioniPrimary (citable) accession number: Q86VQ6
Secondary accession number(s): Q6PIS8, Q9NNW6, Q9P101
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: May 29, 2013
Last modified: September 27, 2017
This is version 142 of the entry and version 4 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Caution

This sequence initiates at a CTG codon.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families