TRXR2_RAT
ID TRXR2_RAT Reviewed; 526 AA.
AC Q9Z0J5;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 3.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Thioredoxin reductase 2, mitochondrial;
DE EC=1.8.1.9;
DE AltName: Full=Thioredoxin reductase TR3;
DE Flags: Precursor;
GN Name=Txnrd2; Synonyms=Trxr2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116 {ECO:0000312|EMBL:AAD13801.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 37-55; 206-217;
RP 343-362 AND 515-526, SELENOCYSTEINE AT SEC-525, FUNCTION, CATALYTIC
RP ACTIVITY, MASS SPECTROMETRY, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=9988709; DOI=10.1074/jbc.274.8.4722;
RA Lee S.-R., Kim J.-R., Kwon K.-S., Yoon H.W., Levine R.L., Ginsburg A.,
RA Rhee S.G.;
RT "Molecular cloning and characterization of a mitochondrial selenocysteine-
RT containing thioredoxin reductase from rat liver.";
RL J. Biol. Chem. 274:4722-4734(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Heart;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP ALTERNATIVE SPLICING (ISOFORMS 1 AND 2).
RX PubMed=11060283; DOI=10.1074/jbc.m004750200;
RA Sun Q.-A., Zappacosta F., Factor V.M., Wirth P.J., Hatfield D.L.,
RA Gladyshev V.N.;
RT "Heterogeneity within animal thioredoxin reductases: evidence for
RT alternative first exon splicing.";
RL J. Biol. Chem. 276:3106-3114(2001).
CC -!- FUNCTION: Involved in the control of reactive oxygen species levels and
CC the regulation of mitochondrial redox homeostasis (By similarity).
CC Maintains mitochondrial thioredoxin in a reduced state. May play a role
CC in redox-regulated cell signaling. {ECO:0000250|UniProtKB:Q9NNW7,
CC ECO:0000269|PubMed:9988709}.
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:9988709};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:20347;
CC Evidence={ECO:0000305|PubMed:9988709};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:9988709};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:9988709}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:9988709}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Z0J5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Z0J5-2; Sequence=VSP_008307;
CC -!- TISSUE SPECIFICITY: Expressed in liver, kidney, adrenal gland and
CC heart. {ECO:0000269|PubMed:9988709}.
CC -!- MASS SPECTROMETRY: [Isoform 1]: Mass=53037; Mass_error=2;
CC Method=Electrospray; Note=The measured range is 37-526.;
CC Evidence={ECO:0000269|PubMed:9988709};
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}.
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; AF072865; AAD13801.1; -; mRNA.
DR EMBL; BC085734; AAH85734.1; -; mRNA.
DR RefSeq; NP_072106.1; NM_022584.2. [Q9Z0J5-1]
DR STRING; 10116.ENSRNOP00000002593; -.
DR BindingDB; Q9Z0J5; -.
DR ChEMBL; CHEMBL5086; -.
DR iPTMnet; Q9Z0J5; -.
DR PhosphoSitePlus; Q9Z0J5; -.
DR jPOST; Q9Z0J5; -.
DR PaxDb; Q9Z0J5; -.
DR PRIDE; Q9Z0J5; -.
DR Ensembl; ENSRNOT00000002593; ENSRNOP00000002593; ENSRNOG00000001890. [Q9Z0J5-1]
DR GeneID; 50551; -.
DR KEGG; rno:50551; -.
DR CTD; 10587; -.
DR RGD; 61960; Txnrd2.
DR eggNOG; KOG4716; Eukaryota.
DR GeneTree; ENSGT00940000158832; -.
DR InParanoid; Q9Z0J5; -.
DR OrthoDB; 581771at2759; -.
DR PhylomeDB; Q9Z0J5; -.
DR BRENDA; 1.8.1.9; 5301.
DR Reactome; R-RNO-3299685; Detoxification of Reactive Oxygen Species.
DR SABIO-RK; Q9Z0J5; -.
DR PRO; PR:Q9Z0J5; -.
DR Proteomes; UP000002494; Chromosome 11.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IDA:UniProtKB.
DR GO; GO:0045454; P:cell redox homeostasis; ISS:UniProtKB.
DR GO; GO:0007507; P:heart development; ISO:RGD.
DR GO; GO:0030097; P:hemopoiesis; ISO:RGD.
DR GO; GO:0065003; P:protein-containing complex assembly; TAS:RGD.
DR GO; GO:0042542; P:response to hydrogen peroxide; TAS:RGD.
DR GO; GO:0055093; P:response to hyperoxia; IEP:RGD.
DR GO; GO:0000305; P:response to oxygen radical; TAS:UniProtKB.
DR GO; GO:0010269; P:response to selenium ion; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
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 Alternative splicing; Direct protein sequencing; Disulfide bond; FAD;
KW Flavoprotein; Mitochondrion; NADP; Oxidoreductase; Redox-active center;
KW Reference proteome; Selenocysteine; Transit peptide.
FT TRANSIT 1..36
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:9988709"
FT CHAIN 37..526
FT /note="Thioredoxin reductase 2, mitochondrial"
FT /id="PRO_0000030290"
FT ACT_SITE 499
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 43..72
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT NON_STD 525
FT /note="Selenocysteine"
FT /evidence="ECO:0000269|PubMed:9988709"
FT MOD_RES 81
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9JLT4"
FT MOD_RES 177
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9JLT4"
FT MOD_RES 331
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9JLT4"
FT DISULFID 88..93
FT /note="Redox-active"
FT /evidence="ECO:0000250"
FT CROSSLNK 524..525
FT /note="Cysteinyl-selenocysteine (Cys-Sec)"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..38
FT /note="MAAIVAALRGSSGRFRPQTRVLTRGTRGAAGAASAAGG -> MEG (in
FT isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_008307"
SQ SEQUENCE 526 AA; 56575 MW; ADEEBAD54BE6F241 CRC64;
MAAIVAALRG SSGRFRPQTR VLTRGTRGAA GAASAAGGQQ NFDLLVIGGG SGGLACAKEA
AQLGRKVAVA DYVEPSPRGT KWGLGGTCVN VGCIPKKLMH QAALLGGMIR DAQHYGWEVA
QPVQHNWKAM AEAVQNHVKS LNWGHRVQLQ DRKVKYFNIK ASFVNEHTVH GVDKAGKVTQ
LSAKHIVIAT GGRPKYPTQV KGALEHGITS DDIFWLKESP GKTLVVGASY VALECAGFLT
GIGLDTTVMM RSVPLRGFDQ QMASLVTEHM ESHGTRFLKG CVPSLIRKLP TNQLQVTWED
LASGKEDVGT FDTVLWAIGR VPETRNLNLE KAGVNTNPKN QKIIVDAQEA TSVPHIYAIG
DVAEGRPELT PTAIKAGKLL AQRLFGKSST LMNYSNVPTT VFTPLEYGCV GLSEEEAVAL
HGQEHIEVYH AYYKPLEFTV ADRDASQCYI KMVCMREPPQ LVLGLHFLGP NAGEVTQGFA
LGIQCGASYA QVMQTVGIHP TCSEEVVKLH ISKRSGLDPT VTGCUG
