TRXR2_BOVIN
ID TRXR2_BOVIN Reviewed; 511 AA.
AC Q9N2I8;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Thioredoxin reductase 2, mitochondrial {ECO:0000305|PubMed:10447675};
DE Short=mt-TR {ECO:0000303|PubMed:10447675};
DE EC=1.8.1.9 {ECO:0000269|PubMed:10447675};
DE AltName: Full=Thioredoxin reductase TR3;
DE Flags: Precursor;
GN Name=TXNRD2; Synonyms=TRXR2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000312|EMBL:BAA82153.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 22-35; 53-82; 160-181;
RP 208-238; 292-316; 328-340; 420-436; 470-488 AND 499-510, SELENOCYSTEINE AT
RP SEC-510, FUNCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Adrenal cortex;
RX PubMed=10447675; DOI=10.1046/j.1432-1327.1999.00578.x;
RA Watabe S., Makino Y., Ogawa K., Hiroi T., Yamamoto Y., Takahashi S.Y.;
RT "Mitochondrial thioredoxin reductase in bovine adrenal cortex. Its
RT purification, properties, nucleotide/amino acid sequences, and
RT identification of selenocysteine.";
RL Eur. J. Biochem. 264:74-84(1999).
CC -!- FUNCTION: Involved in the control of reactive oxygen species levels and
CC the regulation of mitochondrial redox homeostasis (By similarity).
CC Maintains thioredoxin in a reduced state. May play a role in redox-
CC regulated cell signaling. {ECO:0000250|UniProtKB:Q9NNW7,
CC ECO:0000269|PubMed:10447675}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-dithiol + NADP(+) = [thioredoxin]-disulfide +
CC H(+) + NADPH; Xref=Rhea:RHEA:20345, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC COMP:10700, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.9;
CC Evidence={ECO:0000269|PubMed:10447675};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20346;
CC Evidence={ECO:0000305|PubMed:10447675};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:10447675};
CC -!- ACTIVITY REGULATION: Inhibited by 1-chloro-2,4-dinitrobenzene and by
CC zinc, calcium, magnesium and Fe(2+) ions.
CC {ECO:0000269|PubMed:10447675}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.8 uM for thioredoxin {ECO:0000269|PubMed:10447675};
CC KM=1.4 uM for NADPH {ECO:0000269|PubMed:10447675};
CC Note=kcat is 1200 sec(-1) with thioredoxin as substrate.
CC {ECO:0000269|PubMed:10447675};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:10447675};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10447675}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:10447675}.
CC -!- MISCELLANEOUS: The active site is a redox-active disulfide bond. The
CC selenocysteine residue is also essential for catalytic activity (By
CC similarity). {ECO:0000250|UniProtKB:Q9Z0J5}.
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; AB022283; BAA82153.1; -; mRNA.
DR RefSeq; NP_777051.1; NM_174626.2.
DR STRING; 9913.ENSBTAP00000053158; -.
DR Ensembl; ENSBTAT00000060561; ENSBTAP00000053158; ENSBTAG00000043581.
DR GeneID; 282389; -.
DR KEGG; bta:282389; -.
DR CTD; 10587; -.
DR VEuPathDB; HostDB:ENSBTAG00000043581; -.
DR VGNC; VGNC:36546; TXNRD2.
DR eggNOG; KOG4716; Eukaryota.
DR GeneTree; ENSGT00940000158832; -.
DR InParanoid; Q9N2I8; -.
DR OMA; CFDYVKP; -.
DR OrthoDB; 581771at2759; -.
DR Proteomes; UP000009136; Chromosome 17.
DR Bgee; ENSBTAG00000043581; Expressed in laryngeal cartilage and 103 other tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IDA:UniProtKB.
DR GO; GO:0045454; P:cell redox homeostasis; ISS:UniProtKB.
DR GO; GO:0000305; P:response to oxygen radical; TAS:UniProtKB.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR001100; Pyr_nuc-diS_OxRdtase.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR InterPro; IPR006338; Thioredoxin/glutathione_Rdtase.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR PIRSF; PIRSF000350; Mercury_reductase_MerA; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR SUPFAM; SSF55424; SSF55424; 1.
DR TIGRFAMs; TIGR01438; TGR; 1.
DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; FAD; Flavoprotein;
KW Mitochondrion; NADP; Oxidoreductase; Redox-active center;
KW Reference proteome; Selenocysteine; Transit peptide.
FT TRANSIT 1..21
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:10447675"
FT CHAIN 22..511
FT /note="Thioredoxin reductase 2, mitochondrial"
FT /id="PRO_0000030287"
FT ACT_SITE 484
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 29..58
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT NON_STD 510
FT /note="Selenocysteine"
FT /evidence="ECO:0000269|PubMed:10447675"
FT MOD_RES 316
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9JLT4"
FT DISULFID 74..79
FT /note="Redox-active"
FT /evidence="ECO:0000250"
FT CROSSLNK 509..510
FT /note="Cysteinyl-selenocysteine (Cys-Sec)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 511 AA; 54670 MW; CA74A147B32846ED CRC64;
MAALRGAAAR FRGRAPGGAR GAAGRQCYDL LVIGGGSGGL ACAKEAAQLG KKVAVLDYVE
PSPQGTRWGL GGTCVNVGCI PKKLMHQAAL LGGMIRDAPH YGWGVAQAPH SWATLADAVQ
NHVKSLNWGH RIQLQDRKVK YFNVKASFVD THTVCGVSKG GEETLLSAEH IVIATGGRPR
YPTHIEGALE YGITSDDLFW LKESPGKTLV VGASYVALEC AGLLTGLGLD TTVMIRSVPL
RAFDQQMASL VTEHMAGHGT RILRGCAPEK VEKLPGQQLR VTWVDLTSDR KDAGTFDTVL
WAIGRVPETA SLNLEKAGVH TNPVTGKILV DAQETTSVPH IYAIGDVAEG RPELTPTAIM
AGRLLAQRLS GRTSDLMDYS SVPTTVFTPL EYGCVGLSEE AAVARHGEEH VEVYHAFYKP
LEFTVPQRDA SQCYIKMVCL REPPQLVLGL HFLGPNAGEV IQGFALGIKC GASYQQLMRT
VGIHPTCAEE VAKLRISKRS GLDPTVTGCU G
