ID TXD12_RAT Reviewed; 170 AA. AC Q498E0; DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 02-MAY-2006, sequence version 2. DT 16-JUN-2009, entry version 39. DE RecName: Full=Thioredoxin domain-containing protein 12; DE EC=1.8.4.2; DE Flags: Precursor; GN Name=Txndc12; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Placenta; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Possesses significant protein thiol-disulfide oxidase CC activity (By similarity). CC -!- CATALYTIC ACTIVITY: 2 glutathione + protein-disulfide = CC glutathione disulfide + protein-dithiol. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen (By similarity). CC -!- SIMILARITY: Contains 1 thioredoxin domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BC100255; AAI00256.1; ALT_INIT; mRNA. DR IPI; IPI00914741; -. DR RefSeq; NP_001094310.1; -. DR UniGene; Rn.5953; -. DR SMR; Q498E0; 28-161. DR Ensembl; ENSRNOG00000008090; Rattus norvegicus. DR GeneID; 298370; -. DR KEGG; rno:298370; -. DR NMPDR; fig|10116.3.peg.23626; -. DR RGD; 1305960; Txndc12. DR HOVERGEN; Q498E0; -. DR BRENDA; 1.8.4.2; 248. DR ArrayExpress; Q498E0; -. DR GermOnline; ENSRNOG00000008090; Rattus norvegicus. DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW. DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell. DR GO; GO:0019153; F:protein-disulfide reductase (glutathione) a...; IEA:EC. DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR000886; ER_targeting_sequence. DR InterPro; IPR017936; Thioredoxin-like. DR InterPro; IPR017937; Thioredoxin_CS. DR InterPro; IPR012335; Thioredoxin_fold. DR Gene3D; G3DSA:3.40.30.10; Thioredoxin_fold; 1. DR PROSITE; PS00014; ER_TARGET; 1. DR PROSITE; PS00194; THIOREDOXIN_1; 1. DR PROSITE; PS51352; THIOREDOXIN_2; 1. PE 2: Evidence at transcript level; KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; Oxidoreductase; KW Redox-active center; Signal. FT SIGNAL 1 24 By similarity. FT CHAIN 25 170 Thioredoxin domain-containing protein 12. FT /FTId=PRO_0000233975. FT MOTIF 167 170 Prevents secretion from ER (Potential). FT CARBOHYD 128 128 N-linked (GlcNAc...) (Potential). FT DISULFID 64 67 Redox-active (Potential). SQ SEQUENCE 170 AA; 19019 MW; 444B6C9BE12C5E44 CRC64; MSLRFGATCL LSFSFLLLIT SSDGRTGLGK GFGDHIHWRT LEDGKKEAAA SGLPLMVIIH KSWCGACKAL KPKFAESTEI SELSHNFVMV NLEDEEEPRD EDFSPDGGYI PRILFLDPSG KVRPEIINES GNPSYKYFYV SAEQVVQGMK EAQVRLTGDA FREKHFQDEL //