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Protein

Thioredoxin reductase 3

Gene

TXNRD3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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

Caution

This sequence initiates at a CTG codon.1 Publication

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
MIMi606235 gene
neXtProtiNX_Q86VQ6

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
ProteomicsDBi70059

PTM databases

iPTMnetiQ86VQ6
PhosphoSitePlusiQ86VQ6

Expressioni

Gene expression databases

CleanExiHS_TXNRD3
ExpressionAtlasiQ86VQ6 baseline and differential

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

3D structure databases

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
KOiK22182

Family and domain databases

Gene3Di3.30.390.30, 1 hit
3.50.50.60, 2 hits
InterProiView protein in InterPro
IPR036188 FAD/NAD-bd_sf
IPR023753 FAD/NAD-binding_dom
IPR016156 FAD/NAD-linked_Rdtase_dimer_sf
IPR002109 Glutaredoxin
IPR011899 Glutaredoxin_euk/vir
IPR001100 Pyr_nuc-diS_OxRdtase
IPR004099 Pyr_nucl-diS_OxRdtase_dimer
IPR012999 Pyr_OxRdtase_I_AS
IPR036249 Thioredoxin-like_sf
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, 1 hit
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

Sequence (1+)i

Sequence statusi: Complete.

This entry has 1 described isoform and 3 potential isoforms that are computationally mapped.Show allAlign All

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

Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
H0YBQ0H0YBQ0_HUMAN
Thioredoxin reductase 3
TXNRD3
643Annotation score:
H0YBI6H0YBI6_HUMAN
Thioredoxin reductase 3
TXNRD3
607Annotation score:
A0A1W2PR67A0A1W2PR67_HUMAN
Thioredoxin reductase 3
TXNRD3
607Annotation score:

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

Cross-referencesi

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

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...

Protein-protein interaction databases

STRINGi9606.ENSP00000430031

Chemistry databases

BindingDBiQ86VQ6
ChEMBLiCHEMBL2096978

PTM databases

iPTMnetiQ86VQ6
PhosphoSitePlusiQ86VQ6

Polymorphism and mutation databases

DMDMi510120859

Proteomic databases

EPDiQ86VQ6
MaxQBiQ86VQ6
PaxDbiQ86VQ6
PeptideAtlasiQ86VQ6
PRIDEiQ86VQ6
ProteomicsDBi70059

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000640433; ENSP00000492093; ENSG00000197763
GeneIDi114112
KEGGihsa:114112

Organism-specific databases

CTDi114112
DisGeNETi114112
GeneCardsiTXNRD3
HGNCiHGNC:20667 TXNRD3
HPAiHPA036109
MIMi606235 gene
neXtProtiNX_Q86VQ6
OpenTargetsiENSG00000197763
PharmGKBiPA134920642
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1752 Eukaryota
KOG4716 Eukaryota
COG1249 LUCA
GeneTreeiENSGT00390000007578
HOGENOMiHOG000276712
HOVERGENiHBG004959
InParanoidiQ86VQ6
KOiK22182

Enzyme and pathway databases

BRENDAi1.8.1.9 2681

Miscellaneous databases

ChiTaRSiTXNRD3 human
EvolutionaryTraceiQ86VQ6
GenomeRNAii114112
PROiPR:Q86VQ6
SOURCEiSearch...

Gene expression databases

CleanExiHS_TXNRD3
ExpressionAtlasiQ86VQ6 baseline and differential

Family and domain databases

Gene3Di3.30.390.30, 1 hit
3.50.50.60, 2 hits
InterProiView protein in InterPro
IPR036188 FAD/NAD-bd_sf
IPR023753 FAD/NAD-binding_dom
IPR016156 FAD/NAD-linked_Rdtase_dimer_sf
IPR002109 Glutaredoxin
IPR011899 Glutaredoxin_euk/vir
IPR001100 Pyr_nuc-diS_OxRdtase
IPR004099 Pyr_nucl-diS_OxRdtase_dimer
IPR012999 Pyr_OxRdtase_I_AS
IPR036249 Thioredoxin-like_sf
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, 1 hit
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
ProtoNetiSearch...

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: November 7, 2018
This is version 150 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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