Thioredoxin reductase 2, mitochondrial

NameThioredoxin reductase 2, mitochondrial
Synonyms
  • 1.8.1.9
  • KIAA1652
  • Selenoprotein Z
  • SelZ
  • Thioredoxin reductase TR3
  • TR-beta
  • TRXR2
Gene NameTXNRD2
OrganismHuman
Amino acid sequence
>lcl|BSEQ0037230|Thioredoxin reductase 2, mitochondrial
MAAMAVALRGLGGRFRWRTQAVAGGVRGAARGAAAGQRDYDLLVVGGGSGGLACAKEAAQ
LGRKVAVVDYVEPSPQGTRWGLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVAQP
VPHDWRKMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVCGVAKGGKEILLS
ADHIIIATGGRPRYPTHIEGALEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGI
GLDTTIMMRSIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDGQLQVTWEDST
TGKEDTGTFDTVLWAIGRVPDTRSLNLEKAGVDTSPDTQKILVDSREATSVPHIYAIGDV
VEGRPELTPIAIMAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAVARHG
QEHVEVYHAHYKPLEFTVAGRDASQCYVKMVCLREPPQLVLGLHFLGPNAGEVTQGFALG
IKCGASYAQVMRTVGIHPTCSEEVVKLRISKRSGLDPTVTGCUG
Number of residues524
Molecular Weight56506.275
Theoretical pI7.53
GO Classification
Functions
  • thioredoxin-disulfide reductase activity
  • flavin adenine dinucleotide binding
Processes
  • cell redox homeostasis
  • heart development
  • response to reactive oxygen species
  • hemopoiesis
  • response to oxygen radical
Components
  • mitochondrion
  • mitochondrial matrix
General FunctionThioredoxin-disulfide reductase activity
Specific FunctionMaintains thioredoxin in a reduced state. Implicated in the defenses against oxidative stress. May play a role in redox-regulated cell signaling.
Pfam Domain Function
Transmembrane RegionsNot Available
GenBank Protein IDNot Available
UniProtKB IDQ9NNW7
UniProtKB Entry NameTRXR2_HUMAN
Cellular LocationMitochondrion
Gene sequence
>lcl|BSEQ0012370|Thioredoxin reductase 2, mitochondrial (TXNRD2)
ATGGCGGCAATGGCGGTGGCGCTGCGGGGATTAGGAGGGCGCTTCCGGTGGCGGACGCAG
GCCGTGGCGGGCGGGGTGCGGGGCGCGGCGCGGGGCGCAGCAGCAGGTCAGCGGGACTAT
GATCTCCTGGTGGTCGGCGGGGGATCTGGTGGCCTGGCTTGTGCCAAGGAGGCCGCCCAG
CTGGGAAGGAAGGTGGCCGTGGTGGACTACGTGGAACCTTCTCCCCAAGGCACCCGGTGG
GGCCTCGGCGGCACCTGCGTCAACGTGGGCTGCATCCCCAAGAAGCTGATGCACCAGGCG
GCACTGCTGGGAGGCCTGATCCAAGATGCCCCCAACTATGGCTGGGAGGTGGCCCAGCCC
GTGCCGCATGACTGGAGGAAGATGGCAGAAGCTGTTCAAAATCACGTGAAATCCTTGAAC
TGGGGCCACCGTGTCCAGCTTCAGGACAGAAAAGTCAAGTACTTTAACATCAAAGCCAGC
TTTGTTGACGAGCACACGGTTTGCGGCGTTGCCAAAGGTGGGAAAGAGATTCTGCTGTCA
GCCGATCACATCATCATTGCTACTGGAGGGCGGCCGAGATACCCCACGCACATCGAAGGT
GCCTTGGAATATGGAATCACAAGTGATGACATCTTCTGGCTGAAGGAATCCCCTGGAAAA
ACGTTGGTGGTCGGGGCCAGCTATGTGGCCCTGGAGTGTGCTGGCTTCCTCACCGGGATT
GGGCTGGACACCACCATCATGATGCGCAGCATCCCCCTCCGCGGCTTCGACCAGCAAATG
TCCTCCATGGTCATAGAGCACATGGCATCTCATGGCACCCGGTTCCTGAGGGGCTGTGCC
CCCTCGCGGGTCAGGAGGCTCCCTGATGGCCAGCTGCAGGTCACCTGGGAGGACAGCACC
ACCGGCAAGGAGGACACGGGCACCTTTGACACCGTCCTGTGGGCCATAGCACCTTGCATC
TCTGCGTGTCTCCCCACCACCGTGGGACATGCTGGAAAAAACCAGAGAAGAGACTGA
GenBank Gene IDAF171054
GeneCard IDNot Available
GenAtlas IDTXNRD2
HGNC IDHGNC:18155
Chromosome Location22
Locus22q11.21
References
  1. 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. 10455115
  2. Gasdaska PY, Berggren MM, Berry MJ, Powis G: Cloning, sequencing and functional expression of a novel human thioredoxin reductase. FEBS Lett. 1999 Jan 8;442(1):105-11. 9923614
  3. Miranda-Vizuete A, Damdimopoulos AE, Pedrajas JR, Gustafsson JA, Spyrou G: Human mitochondrial thioredoxin reductase cDNA cloning, expression and genomic organization. Eur J Biochem. 1999 Apr;261(2):405-12. 10215850
  4. Lescure A, Gautheret D, Carbon P, Krol A: Novel selenoproteins identified in silico and in vivo by using a conserved RNA structural motif. J Biol Chem. 1999 Dec 31;274(53):38147-54. 10608886
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  7. Sun QA, Zappacosta F, Factor VM, Wirth PJ, Hatfield DL, Gladyshev VN: Heterogeneity within animal thioredoxin reductases. Evidence for alternative first exon splicing. J Biol Chem. 2001 Feb 2;276(5):3106-14. Epub 2000 Nov 1. 11060283
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