THIOM_RAT
ID THIOM_RAT Reviewed; 166 AA.
AC P97615;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Thioredoxin, mitochondrial;
DE Short=MTRX;
DE Short=Mt-Trx;
DE AltName: Full=Thioredoxin-2;
DE Flags: Precursor;
GN Name=Txn2; Synonyms=Trx2;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Heart;
RX PubMed=9006939; DOI=10.1074/jbc.272.5.2936;
RA Spyrou G., Enmark E., Miranda-Vizuete A., Gustafsson J.-A.;
RT "Cloning and expression of a novel mammalian thioredoxin.";
RL J. Biol. Chem. 272:2936-2941(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
CC -!- FUNCTION: Important for the control of mitochondrial reactive oxygen
CC species homeostasis, apoptosis regulation and cell viability. Possesses
CC a dithiol-reducing activity. {ECO:0000250|UniProtKB:Q99757,
CC ECO:0000269|PubMed:9006939}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:9006939}.
CC -!- TISSUE SPECIFICITY: Expressed in several tissues with the highest
CC expression levels in heart, muscle, kidney and adrenal gland.
CC {ECO:0000269|PubMed:9006939}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
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DR EMBL; U73525; AAC53008.1; -; mRNA.
DR EMBL; BC081760; AAH81760.1; -; mRNA.
DR RefSeq; NP_445783.1; NM_053331.2.
DR AlphaFoldDB; P97615; -.
DR SMR; P97615; -.
DR STRING; 10116.ENSRNOP00000060694; -.
DR iPTMnet; P97615; -.
DR PhosphoSitePlus; P97615; -.
DR jPOST; P97615; -.
DR PaxDb; P97615; -.
DR PRIDE; P97615; -.
DR Ensembl; ENSRNOT00000067483; ENSRNOP00000060694; ENSRNOG00000005614.
DR GeneID; 79462; -.
DR KEGG; rno:79462; -.
DR UCSC; RGD:71040; rat.
DR CTD; 25828; -.
DR RGD; 71040; Txn2.
DR eggNOG; KOG0910; Eukaryota.
DR GeneTree; ENSGT00530000064086; -.
DR InParanoid; P97615; -.
DR OMA; CTPCKAL; -.
DR OrthoDB; 1482186at2759; -.
DR PhylomeDB; P97615; -.
DR TreeFam; TF314517; -.
DR Reactome; R-RNO-1614558; Degradation of cysteine and homocysteine.
DR Reactome; R-RNO-3299685; Detoxification of Reactive Oxygen Species.
DR PRO; PR:P97615; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000005614; Expressed in skeletal muscle tissue and 20 other tissues.
DR Genevisible; P97615; RN.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR GO; GO:0031669; P:cellular response to nutrient levels; IEP:RGD.
DR GO; GO:0048678; P:response to axon injury; IEP:RGD.
DR GO; GO:0009749; P:response to glucose; IEP:RGD.
DR GO; GO:0009725; P:response to hormone; IEP:RGD.
DR GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0006979; P:response to oxidative stress; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR InterPro; IPR005746; Thioredoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00085; Thioredoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR TIGRFAMs; TIGR01068; thioredoxin; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Disulfide bond; Electron transport; Mitochondrion;
KW Redox-active center; Reference proteome; Transit peptide; Transport.
FT TRANSIT 1..59
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 60..166
FT /note="Thioredoxin, mitochondrial"
FT /id="PRO_0000034152"
FT DOMAIN 61..166
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 90
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 93
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT SITE 84
FT /note="Deprotonates C-terminal active site Cys"
FT /evidence="ECO:0000250"
FT SITE 91
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 92
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT MOD_RES 152
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99757"
FT MOD_RES 152
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P97493"
FT DISULFID 90..93
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ SEQUENCE 166 AA; 18232 MW; 27D18DE8B0F8B52B CRC64;
MAQRLLLRRF LTSVISRKPP QGVWASLTST SLQTPPYNAG GLTGTPSPAR TFHTTRVCST
TFNVQDGPDF QDRVVNSETP VVVDFHAQWC GPCKILGPRL EKMVAKQHGK VVMAKVDIDD
HTDLAIEYEV SAVPTVLAIK NGDVVDKFVG IKDEDQLEAF LKKLIG
