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Q86VQ6

- TRXR3_HUMAN

UniProt

Q86VQ6 - TRXR3_HUMAN

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Protein

Thioredoxin reductase 3

Gene

TXNRD3

Organism
Homo sapiens (Human)
Status
Reviewed - 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

Catalytic activityi

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

Cofactori

Binds 1 FAD per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei616 – 6161Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi158 – 18730FADBy similarityAdd
BLAST

GO - Molecular functioni

  1. electron carrier activity Source: InterPro
  2. flavin adenine dinucleotide binding Source: InterPro
  3. NADP binding Source: InterPro
  4. protein disulfide oxidoreductase activity Source: InterPro
  5. thioredoxin-disulfide reductase activity Source: UniProtKB

GO - Biological processi

  1. cell differentiation Source: UniProtKB-KW
  2. cell redox homeostasis Source: UniProtKB
  3. multicellular organismal development Source: UniProtKB-KW
  4. spermatogenesis Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Oxidoreductase

Keywords - Biological processi

Differentiation, Electron transport, Spermatogenesis, Transport

Keywords - Ligandi

FAD, Flavoprotein, NADP

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
ProteomesiUP000005640: Unplaced

Organism-specific databases

HGNCiHGNC:20667. TXNRD3.

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity. Microsome By similarity. Endoplasmic reticulum By similarity
Note: Detected in cytoplasm and nucleus in late spermatids.By similarity

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB-KW
  2. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Microsome, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134920642.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 643643Thioredoxin reductase 3PRO_0000320695Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei41 – 411Phosphoserine1 Publication
Modified residuei42 – 421Phosphoserine1 Publication
Disulfide bondi203 ↔ 208Redox-activeBy similarity
Modified residuei379 – 3791N6-succinyllysineBy similarity
Cross-linki641 ↔ 642Cysteinyl-selenocysteine (Cys-Sec)By similarity

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

MaxQBiQ86VQ6.
PaxDbiQ86VQ6.
PRIDEiQ86VQ6.

PTM databases

PhosphoSiteiQ86VQ6.

Expressioni

Gene expression databases

CleanExiHS_TXNRD3.
GenevestigatoriQ86VQ6.

Organism-specific databases

HPAiCAB020802.
HPA036109.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi125281. 1 interaction.

Structurei

Secondary structure

1
643
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi53 – 6513
Beta strandi67 – 726
Helixi77 – 8812
Beta strandi94 – 974
Turni98 – 1003
Helixi104 – 11512
Beta strandi122 – 1254
Beta strandi128 – 1325
Helixi133 – 14210
Helixi144 – 1507

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3H8QX-ray2.21A/B51-156[»]
ProteinModelPortaliQ86VQ6.
SMRiQ86VQ6. Positions 51-638.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ86VQ6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini56 – 156101GlutaredoxinPROSITE-ProRule annotationAdd
BLAST

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

Contains 1 glutaredoxin domain.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiCOG1249.
HOGENOMiHOG000276712.
HOVERGENiHBG004959.
InParanoidiQ86VQ6.
KOiK00384.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR002109. Glutaredoxin.
IPR011899. Glutaredoxin_euk/vir.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR012999. Pyr_OxRdtase_I_AS.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
IPR012336. Thioredoxin-like_fold.
IPR006338. Thioredoxin/glutathione_Rdtase.
[Graphical view]
PfamiPF00462. Glutaredoxin. 1 hit.
PF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
PRINTSiPR00368. FADPNR.
SUPFAMiSSF52833. SSF52833. 1 hit.
SSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR02180. GRX_euk. 1 hit.
TIGR01438. TGR. 1 hit.
PROSITEiPS51354. GLUTAREDOXIN_2. 1 hit.
PS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]

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 AAH30028.1 differs from that shown. Reason: Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.
The sequence AAH50032.1 differs from that shown. Reason: Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.
The sequence AAH30028.1 differs from that shown. Reason: Erroneous termination at position 642. Translated as Sec.
The sequence AAH50032.1 differs from that shown. Reason: Erroneous termination at position 642. Translated as Sec.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti65 – 662RS → AE in AAD51325. (PubMed:10455115)Curated
Sequence conflicti246 – 2461T → I in AAH30028. (PubMed:15489334)Curated
Sequence conflicti337 – 3371T → P in AAD39929. 1 PublicationCurated

Non-standard residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-standard residuei642 – 6421Selenocysteine

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
RefSeqiNP_001166984.1. NM_001173513.1.
NP_443115.1. NM_052883.1.
UniGeneiHs.477475.

Genome annotation databases

GeneIDi114112.
KEGGihsa:114112.
UCSCiuc003ejd.2. human.

Polymorphism databases

DMDMi510120859.

Keywords - Coding sequence diversityi

Selenocysteine

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
RefSeqi NP_001166984.1. NM_001173513.1.
NP_443115.1. NM_052883.1.
UniGenei Hs.477475.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3H8Q X-ray 2.21 A/B 51-156 [» ]
ProteinModelPortali Q86VQ6.
SMRi Q86VQ6. Positions 51-638.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 125281. 1 interaction.

Chemistry

BindingDBi Q86VQ6.
ChEMBLi CHEMBL2096978.

PTM databases

PhosphoSitei Q86VQ6.

Polymorphism databases

DMDMi 510120859.

Proteomic databases

MaxQBi Q86VQ6.
PaxDbi Q86VQ6.
PRIDEi Q86VQ6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 114112.
KEGGi hsa:114112.
UCSCi uc003ejd.2. human.

Organism-specific databases

CTDi 114112.
GeneCardsi GC03M126292.
HGNCi HGNC:20667. TXNRD3.
HPAi CAB020802.
HPA036109.
MIMi 606235. gene.
neXtProti NX_Q86VQ6.
PharmGKBi PA134920642.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1249.
HOGENOMi HOG000276712.
HOVERGENi HBG004959.
InParanoidi Q86VQ6.
KOi K00384.

Miscellaneous databases

ChiTaRSi TXNRD3. human.
EvolutionaryTracei Q86VQ6.
GenomeRNAii 114112.
NextBioi 78986.
PROi Q86VQ6.
SOURCEi Search...

Gene expression databases

CleanExi HS_TXNRD3.
Genevestigatori Q86VQ6.

Family and domain databases

Gene3Di 3.30.390.30. 1 hit.
3.40.30.10. 1 hit.
InterProi IPR016156. FAD/NAD-linked_Rdtase_dimer.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR002109. Glutaredoxin.
IPR011899. Glutaredoxin_euk/vir.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
IPR012999. Pyr_OxRdtase_I_AS.
IPR001327. Pyr_OxRdtase_NAD-bd_dom.
IPR012336. Thioredoxin-like_fold.
IPR006338. Thioredoxin/glutathione_Rdtase.
[Graphical view ]
Pfami PF00462. Glutaredoxin. 1 hit.
PF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view ]
PRINTSi PR00368. FADPNR.
SUPFAMi SSF52833. SSF52833. 1 hit.
SSF55424. SSF55424. 1 hit.
TIGRFAMsi TIGR02180. GRX_euk. 1 hit.
TIGR01438. TGR. 1 hit.
PROSITEi PS51354. GLUTAREDOXIN_2. 1 hit.
PS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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].
    Tissue: TestisImported.
  3. "Redox regulation of cell signaling by selenocysteine in mammalian thioredoxin reductases."
    Sun Q.-A., Wu Y., Zappacosta F., Jeang K.-T., Lee B.J., Hatfield D.L., Gladyshev V.N.
    J. Biol. Chem. 274:24522-24530(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 65-643, SELENOCYSTEINE AT SEC-642.
  4. "TrxR3, a novel human thioredoxin reductase."
    Miranda-Vizuete A.
    Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 67-643.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41 AND SER-42, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. "CUG start codon generates thioredoxin/glutathione reductase isoforms in mouse testes."
    Gerashchenko M.V., Su D., Gladyshev V.N.
    J. Biol. Chem. 285:4595-4602(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROBABLE NON-AUG INITIATOR START CODON.

Entry informationi

Entry nameiTRXR3_HUMAN
AccessioniPrimary (citable) accession number: Q86VQ6
Secondary accession number(s): Q6PIS8, Q9NNW6, Q9P101
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: May 29, 2013
Last modified: October 29, 2014
This is version 115 of the entry and version 4 of the sequence. [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

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

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

External Data

Dasty 3