ID THI2_MOUSE STANDARD; PRT; 166 AA. AC P97493; DT 15-DEC-1998 (Rel. 37, Created) DT 15-DEC-1998 (Rel. 37, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Thioredoxin, mitochondrial precursor (Mt-TRX) (Thioredoxin 2). GN TXN2. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RA Miranda-Vizuete A., Gustafsson J.-A., Spyrou G.; RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Possess a dithiol-reducing activity. CC -!- SUBCELLULAR LOCATION: Mitochondrial. CC -!- SIMILARITY: Belongs to the thioredoxin family. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U85089; AAB41900.1; -. DR HSSP; P10599; 1TRV. DR MGD; MGI:1929468; Txn2. DR InterPro; IPR006662; Thiored. DR InterPro; IPR006663; Thioredox_dom2. DR InterPro; IPR005746; Thioredoxin. DR Pfam; PF00085; thiored; 1. DR PRINTS; PR00421; THIOREDOXIN. DR TIGRFAMs; TIGR01068; thioredoxin; 1. DR PROSITE; PS00194; THIOREDOXIN; 1. KW Redox-active center; Electron transport; Mitochondrion; KW Transit peptide. FT TRANSIT 1 59 Mitochondrion (By similarity). FT CHAIN 60 166 THIOREDOXIN. FT DISULFID 90 93 Redox-active (By similarity). SQ SEQUENCE 166 AA; 18255 MW; C9A803DF571F3A7D CRC64; MAQRLLLGRF LTSVISRKPP QGVWASLTSK TLQTPQYNAG GLTVMPSPAR TVHTTRVCLT TFNVQDGPDF QDRVVNSETP VVVDFHAQWC GPCKILGPRL EKMVAKQHGK VVMAKVDIDD HTDLAIEYEV SAVPTVLAIK NGDVVDKFVG IKDEDQLEAF LKKLIG //