ID   TRXR1_BOVIN             Reviewed;         499 AA.
AC   O62768;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 3.
DT   16-JUN-2009, entry version 80.
DE   RecName: Full=Thioredoxin reductase 1, cytoplasmic;
DE            Short=TR;
DE            EC=1.8.1.9;
DE   AltName: Full=Thioredoxin reductase TR1;
GN   Name=TXNRD1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Small intestine;
RA   Terashima H.;
RL   Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: Thioredoxin + NADP(+) = thioredoxin disulfide
CC       + NADPH.
CC   -!- COFACTOR: Binds 1 FAD per subunit (By similarity).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC       The selenocysteine residue is also essential for catalytic
CC       activity (By similarity).
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family.
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DR   EMBL; AF053984; AAC13914.1; -; mRNA.
DR   IPI; IPI00685161; -.
DR   RefSeq; NP_777050.1; -.
DR   UniGene; Bt.5534; -.
DR   HSSP; Q94655; 1ONF.
DR   SMR; O62768; 11-493.
DR   Ensembl; ENSBTAG00000013912; Bos taurus.
DR   GeneID; 282388; -.
DR   KEGG; bta:282388; -.
DR   HOVERGEN; O62768; -.
DR   BRENDA; 1.8.1.9; 251.
DR   GO; GO:0050660; F:FAD binding; IEA:InterPro.
DR   GO; GO:0050661; F:NADP or NADPH binding; IEA:InterPro.
DR   GO; GO:0008430; F:selenium binding; IEA:UniProtKB-KW.
DR   GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IEA:EC.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase.
DR   InterPro; IPR000815; Hg_reductase.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR   InterPro; IPR001327; Pyr_OxRdtase_NAD_bd.
DR   InterPro; IPR006338; Reduct_Se.
DR   Gene3D; G3DSA:3.30.390.30; Pyr_redox_dim; 1.
DR   PANTHER; PTHR22912:SF23; Reduct_Se; 1.
DR   Pfam; PF00070; Pyr_redox; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF02852; Pyr_redox_dim; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00945; HGRDTASE.
DR   ProDom; PD000139; FAD_pyr_redox; 1.
DR   TIGRFAMs; TIGR01438; TGR; 1.
DR   PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Disulfide bond; FAD; Flavoprotein; NADP; Oxidoreductase;
KW   Phosphoprotein; Redox-active center; Selenium; Selenocysteine.
FT   CHAIN         1    499       Thioredoxin reductase 1, cytoplasmic.
FT                                /FTId=PRO_0000067981.
FT   NP_BIND      42     59       FAD (By similarity).
FT   ACT_SITE    472    472       Proton acceptor (By similarity).
FT   NON_STD     498    498       Selenocysteine.
FT   MOD_RES      11     11       Phosphotyrosine (By similarity).
FT   MOD_RES      13     13       Phosphotyrosine (By similarity).
FT   MOD_RES     131    131       Phosphotyrosine (By similarity).
FT   MOD_RES     422    422       Phosphotyrosine (By similarity).
FT   DISULFID     59     64       Redox-active (By similarity).
FT   CROSSLNK    497    498       Cysteinyl-selenocysteine (Cys-Sec) (By
FT                                similarity).
SQ   SEQUENCE   499 AA;  54770 MW;  B0F15494D1795AB3 CRC64;
     MNGSKDLPEP YDYDLIIIGG GSGGLAAAKE AAKYDKKVMV LDFVTPTPLG TRWGLGGTCV
     NVGCIPKKLM HQAALLGQAL RDSRNYGWNV EETVKHDWER MTEAVQNHIG SLNWGYRVAL
     REKKVTYENA YGEFVGPHRI KATNNKGKEK IYSAERFLIA TGERPRYLGI PGDKEYCISS
     DDLFSLPYCP GKTLVVGASY VALECAGFLA GIGLDVTVMV RSILLRGFDQ DMANKIGEHM
     QEHGIKFIRQ FVPIKVEQIE AGTPGRLRVI AKSTDSDQTI EGEYNTVLLA IGRDACTRKI
     GLENVGVKIN EKTGKIPVTE EEQTNVPYIY AIGDILEGKL ELTPVAIQAG RLLAQRLYGG
     STVKCDYENV PTTVFTPLEY GSCGLSEEKA VEKFGEENVE VYHSYFWPLE WTIPSRDNNK
     CYAKVVCNIK DNERVVGFHV LGPNAGEVTQ GFAAALKCGL TKDQLDSTIG IHPVCAEVFT
     TLSVTKRSGG NILQTGCUG
//