TRXR1_BOVIN
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 03-AUG-2022, entry version 160.
DE RecName: Full=Thioredoxin reductase 1, cytoplasmic {ECO:0000305};
DE Short=TR;
DE EC=1.8.1.9 {ECO:0000250|UniProtKB:Q16881};
DE AltName: Full=Peroxidase TXNRD1 {ECO:0000250|UniProtKB:Q16881};
DE EC=1.11.1.2 {ECO:0000250|UniProtKB:Q16881};
DE AltName: Full=Thioredoxin reductase TR1;
GN Name=TXNRD1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC 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 -!- FUNCTION: Reduces disulfideprotein thioredoxin (Trx) to its dithiol-
CC containing form. Homodimeric flavoprotein involved in the regulation of
CC cellular redox reactions, growth and differentiation. Contains a
CC selenocysteine residue at the C-terminal active site that is essential
CC for catalysis. Also has reductase activity on hydrogen peroxide (H2O2).
CC {ECO:0000250|UniProtKB:Q16881}.
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:0000250|UniProtKB:Q16881};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:20347;
CC Evidence={ECO:0000250|UniProtKB:Q16881};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + H2O2 + NADPH = 2 H2O + NADP(+); Xref=Rhea:RHEA:15173,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.11.1.2;
CC Evidence={ECO:0000250|UniProtKB:Q16881};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15174;
CC Evidence={ECO:0000250|UniProtKB:Q16881};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q16881};
CC Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:Q16881};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q16881}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q16881}.
CC -!- PTM: ISGylated. {ECO:0000250|UniProtKB:Q16881}.
CC -!- MISCELLANEOUS: The thioredoxin reductase active site is a redox-active
CC disulfide bond. The selenocysteine residue is also essential for
CC catalytic activity. {ECO:0000250|UniProtKB:O89049}.
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; AF053984; AAC13914.1; -; mRNA.
DR RefSeq; NP_777050.1; NM_174625.3.
DR STRING; 9913.ENSBTAP00000053996; -.
DR PaxDb; O62768; -.
DR PeptideAtlas; O62768; -.
DR PRIDE; O62768; -.
DR Ensembl; ENSBTAT00000018473; ENSBTAP00000018473; ENSBTAG00000013912.
DR GeneID; 282388; -.
DR KEGG; bta:282388; -.
DR CTD; 7296; -.
DR VEuPathDB; HostDB:ENSBTAG00000013912; -.
DR VGNC; VGNC:36545; TXNRD1.
DR eggNOG; KOG4716; Eukaryota.
DR GeneTree; ENSGT00940000160180; -.
DR HOGENOM; CLU_016755_2_4_1; -.
DR InParanoid; O62768; -.
DR OMA; SGHAAWH; -.
DR OrthoDB; 581771at2759; -.
DR BRENDA; 1.8.1.9; 908.
DR SABIO-RK; O62768; -.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000013912; Expressed in rumen papilla and 105 other tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0001650; C:fibrillar center; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0071949; F:FAD binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0050137; F:NADPH peroxidase activity; ISS:UniProtKB.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase activity; ISS:UniProtKB.
DR GO; GO:0008283; P:cell population proliferation; IEA:Ensembl.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR GO; GO:0001707; P:mesoderm formation; IEA:Ensembl.
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 2: Evidence at transcript level;
KW Cytoplasm; Disulfide bond; FAD; Flavoprotein; NADP; Oxidoreductase;
KW Phosphoprotein; Redox-active center; Reference proteome; Selenocysteine;
KW Ubl conjugation.
FT CHAIN 1..499
FT /note="Thioredoxin reductase 1, cytoplasmic"
FT /id="PRO_0000067981"
FT ACT_SITE 472
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 22..23
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q16881"
FT BINDING 42..43
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q16881"
FT BINDING 58..59
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q16881"
FT BINDING 63..67
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q16881"
FT BINDING 131..132
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q16881"
FT BINDING 161
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q16881"
FT BINDING 166
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q16881"
FT BINDING 198..204
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q16881"
FT BINDING 200
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q16881"
FT BINDING 221..222
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q16881"
FT BINDING 226..228
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q16881"
FT BINDING 226
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O89049"
FT BINDING 292..293
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q16881"
FT BINDING 315
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q16881"
FT BINDING 334
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q16881"
FT BINDING 341..343
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q16881"
FT BINDING 341
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q16881"
FT BINDING 472
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q16881"
FT NON_STD 498
FT /note="Selenocysteine"
FT MOD_RES 68
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9JMH6"
FT MOD_RES 131
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q16881"
FT DISULFID 59..64
FT /note="Redox-active"
FT /evidence="ECO:0000250"
FT CROSSLNK 497..498
FT /note="Cysteinyl-selenocysteine (Cys-Sec)"
FT /evidence="ECO:0000250"
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
