Thioredoxin reductase 3

Details

Name
Thioredoxin reductase 3
Synonyms
  • 1.8.1.9
  • Tgr
  • Thioredoxin and glutathione reductase
  • Thioredoxin reductase TR2
  • Trxr3
Gene Name
Txnrd3
Organism
Mouse
Amino acid sequence
>lcl|BSEQ0052692|Thioredoxin reductase 3
MEKPPSPPPPPRAQTSPGLGKVGVLPNRRLGAVRGGLMSSPPGRRARLASPGTSRPSSEA
REELRRRLRDLIEGNRVMIFSKSYCPHSTRVKELFSSLGVVYNILELDQVDDGASVQEVL
TEISNQKTVPNIFVNKVHVGGCDRTFQAHQNGLLQKLLQDDSAHDYDLIIIGGGSGGLSC
AKEAANLGKKVMVLDFVVPSPQGTTWGLGGTCVNVGCIPKKLMHQAALLGHALQDAKKYG
WEYNQQVKHNWEAMTEAIQSHIGSLNWGYRVTLREKGVTYVNSFGEFVDLHKIKATNKKG
QETFYTASKFVIATGERPRYLGIQGDKEYCITSDDLFSLPYCPGCTLVVGASYVGLECAG
FLAGLGLDVTVMVRSVLLRGFDQEMAEKVGSYLEQQGVKFQRKFTPILVQQLEKGLPGKL
KVVAKSTEGPETVEGIYNTVLLAIGRDSCTRKIGLEKIGVKINEKNGKIPVNDVEQTNVP
HVYAIGDILDGKPELTPVAIQAGKLLARRLFGVSLEKCDYINIPTTVFTPLEYGCCGLSE
EKAIEMYKKENLEVYHTLFWPLEWTVAGRDNNTCYAKIICNKFDNERVVGFHLLGPNAGE
ITQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTLEITKSSGLDITQKGCUG
Number of residues
652
Molecular Weight
71318.475
Theoretical pI
Not Available
GO Classification
Functions
flavin adenine dinucleotide binding / glutathione oxidoreductase activity / thioredoxin-disulfide reductase activity
Processes
blastocyst formation / cell differentiation / cell redox homeostasis / glutathione metabolic process / spermatogenesis
Components
cytoplasm / cytosol / endoplasmic reticulum / mitochondrion / nucleoplasm
General Function
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.
Specific Function
Flavin adenine dinucleotide binding
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0052693|Thioredoxin reductase 3 (Txnrd3)
CTGGAGAAGCCACCGTCCCCGCCGCCGCCTCCTCGGGCGCAGACCTCGCCCGGGCTGGGG
AAGGTTGGAGTCCTCCCCAACCGCCGCCTGGGTGCTGTCCGTGGCGGCCTCATGTCGTCG
CCACCCGGCCGCCGCGCCCGCCTGGCCTCCCCTGGGACCAGCCGCCCGTCTTCTGAGGCC
CGCGAGGAGCTGCGGCGCCGCCTGCGGGACCTCATCGAGGGCAACAGGGTGATGATCTTC
AGCAAGAGTTACTGTCCACACAGCACGCGGGTTAAGGAACTCTTTTCGTCCTTGGGAGTG
GTCTATAACATCCTGGAACTTGATCAAGTTGATGACGGGGCCAGTGTTCAGGAAGTGCTG
ACAGAAATCAGTAACCAGAAAACGGTGCCCAATATTTTTGTGAATAAAGTGCACGTGGGT
GGATGTGACCGAACTTTCCAGGCACATCAGAATGGTTTACTGCAGAAGCTCCTCCAAGAT
GACTCGGCTCATGATTACGACCTCATCATCATCGGCGGGGGTTCTGGCGGCCTCTCTTGT
GCCAAGGAAGCTGCCAACTTGGGAAAGAAGGTCATGGTGCTAGACTTTGTGGTCCCATCG
CCTCAGGGCACGACCTGGGGCCTTGGCGGCACCTGTGTGAACGTAGGCTGTATTCCAAAG
AAGCTGATGCATCAGGCAGCCCTCCTGGGGCATGCTTTGCAAGATGCCAAGAAATATGGC
TGGGAGTATAACCAGCAGGTGAAGCACAACTGGGAGGCCATGACAGAAGCTATCCAGAGC
CACATTGGCTCCTTGAACTGGGGCTACAGGGTAACCCTTCGGGAGAAAGGCGTGACCTAT
GTCAACTCCTTCGGGGAGTTTGTGGACCTGCATAAAATAAAGGCAACCAATAAGAAAGGG
CAGGAAACGTTTTACACGGCTTCGAAGTTTGTCATAGCAACAGGTGAAAGGCCTCGGTAC
TTGGGAATCCAGGGAGATAAAGAGTACTGTATTACGAGTGACGACCTGTTCTCTCTGCCA
TACTGCCCGGGATGTACATTAGTCGTAGGCGCTTCTTATGTTGGTCTGGAGTGTGCGGGC
TTTTTGGCTGGTTTGGGGTTAGATGTGACAGTCATGGTACGCTCCGTCCTTCTTCGTGGC
TTTGATCAAGAAATGGCAGAGAAAGTGGGATCCTACCTGGAACAACAAGGTGTCAAGTTC
CAAAGGAAATTCACCCCCATTTTGGTTCAACAGTTGGAGAAAGGTTTACCAGGAAAATTG
AAAGTCGTGGCTAAGTCCACCGAAGGACCGGAAACAGTAGAAGGGATATACAACACGGTT
TTGTTAGCAATTGGTCGTGACTCCTGTACAAGGAAAATAGGGCTGGAGAAGATCGGGGTC
AAAATCAATGAGAAGAATGGCAAAATACCAGTAAACGATGTGGAGCAGACCAACGTGCCT
CATGTTTATGCTATTGGGGACATACTGGACGGCAAACCAGAGCTCACCCCCGTTGCCATA
CAGGCAGGCAAGCTGCTAGCTCGAAGACTCTTTGGGGTCTCTTTAGAAAAGTGTGATTAT
ATTAACATCCCAACAACGGTGTTCACACCTCTGGAATATGGCTGTTGTGGACTGTCGGAA
GAGAAAGCCATCGAAATGTATAAAAAAGAGAATCTGGAAGTGTATCACACCTTGTTTTGG
CCTCTCGAGTGGACAGTTGCTGGCAGAGACAACAACACCTGTTATGCAAAGATAATCTGC
AACAAATTCGACAACGAACGTGTGGTGGGATTTCACCTTCTGGGGCCAAATGCTGGTGAA
ATCACGCAGGGATTTGCAGCTGCAATGAAATGTGGGCTCACGAAGCAGCTACTGGATGAT
ACCATTGGAATCCACCCCACCTGTGGTGAGGTATTCACAACATTGGAAATCACAAAGTCC
TCAGGGCTGGACATTACTCAGAAAGGCTGCTGAGGCTAG
Chromosome Location
6
Locus
6 D1
External Identifiers
ResourceLink
UniProtKB IDQ99MD6
UniProtKB Entry NameTRXR3_MOUSE
General References
  1. Sun QA, Kirnarsky L, Sherman S, Gladyshev VN: Selenoprotein oxidoreductase with specificity for thioredoxin and glutathione systems. Proc Natl Acad Sci U S A. 2001 Mar 27;98(7):3673-8. doi: 10.1073/pnas.051454398. Epub 2001 Mar 20. [Article]
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  4. Sun QA, Wu Y, Zappacosta F, Jeang KT, Lee BJ, Hatfield DL, Gladyshev VN: Redox regulation of cell signaling by selenocysteine in mammalian thioredoxin reductases. J Biol Chem. 1999 Aug 27;274(35):24522-30. [Article]
  5. Sun QA, Su D, Novoselov SV, Carlson BA, Hatfield DL, Gladyshev VN: Reaction mechanism and regulation of mammalian thioredoxin/glutathione reductase. Biochemistry. 2005 Nov 8;44(44):14528-37. doi: 10.1021/bi051321w. [Article]
  6. Su D, Novoselov SV, Sun QA, Moustafa ME, Zhou Y, Oko R, Hatfield DL, Gladyshev VN: Mammalian selenoprotein thioredoxin-glutathione reductase. Roles in disulfide bond formation and sperm maturation. J Biol Chem. 2005 Jul 15;280(28):26491-8. doi: 10.1074/jbc.M503638200. Epub 2005 May 18. [Article]
  7. Huttlin EL, Jedrychowski MP, Elias JE, Goswami T, Rad R, Beausoleil SA, Villen J, Haas W, Sowa ME, Gygi SP: A tissue-specific atlas of mouse protein phosphorylation and expression. Cell. 2010 Dec 23;143(7):1174-89. doi: 10.1016/j.cell.2010.12.001. [Article]
  8. Gerashchenko MV, Su D, Gladyshev VN: CUG start codon generates thioredoxin/glutathione reductase isoforms in mouse testes. J Biol Chem. 2010 Feb 12;285(7):4595-602. doi: 10.1074/jbc.M109.070532. Epub 2009 Dec 14. [Article]
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Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails