TRXR1_PONAB
ID TRXR1_PONAB Reviewed; 499 AA.
AC Q5NVA2; Q5R5P1;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 3.
DT 03-AUG-2022, entry version 97.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex, and Kidney;
RG The German cDNA consortium;
RL Submitted (DEC-2004) 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; CR860816; CAH92925.2; -; mRNA.
DR EMBL; CR926483; CAI30275.1; -; mRNA.
DR RefSeq; NP_001127133.1; NM_001133661.1.
DR Ensembl; ENSPPYT00000005798; ENSPPYP00000005584; ENSPPYG00000004893.
DR GeneID; 100174180; -.
DR KEGG; pon:100174180; -.
DR CTD; 7296; -.
DR eggNOG; KOG4716; Eukaryota.
DR GeneTree; ENSGT00940000160180; -.
DR InParanoid; Q5NVA2; -.
DR OrthoDB; 581771at2759; -.
DR Proteomes; UP000001595; Chromosome 12.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; 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; IEA:InterPro.
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_0000067984"
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"
FT CONFLICT 56
FT /note="G -> E (in Ref. 1; CAH92925)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="H -> R (in Ref. 1; CAI30275)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="I -> V (in Ref. 1; CAI30275)"
FT /evidence="ECO:0000305"
FT CONFLICT 257
FT /note="E -> G (in Ref. 1; CAH92925)"
FT /evidence="ECO:0000305"
FT CONFLICT 411
FT /note="W -> R (in Ref. 1; CAH92925)"
FT /evidence="ECO:0000305"
FT CONFLICT 485
FT /note="T -> A (in Ref. 1; CAI30275)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 499 AA; 54751 MW; D0535BE1F2405DA7 CRC64;
MNGPEDLPES YDYDLIIIGG GSGGLAAAKE AAQYGKKVMV LDFVTPTPLG TRWGLGGTCV
NVGCIPKKLM HQAALLGQAL QDSRNYGWKV EETVKHDWDR MIEAVQNHIG SLNWGYRVAL
REKKVVYENA YGQFIGPHRI KATNNKGKEK IYSAERFLIA TGERPRYLGI PGDKEYCISS
DDLFSLPYCP GKTLIVGASY VALECAGFLA GIGLDVTVMV RSILLRGFDQ DMANKIGEHM
EEHGIKFIRQ FVPIKVEQIE AGTPGRLRVV AQSTNSEEII EGEYNTVLLA IGRDACTRKI
GLETVGVKIN EKTGKIPVTD EEQTNVPYIY AIGDILEDKV ELTPVAIQAG RLLAQRLYAG
STVKCDYENV PTTVFTPLEY GACGLSEEKA VEKFGEENIE VYHSYFWPLE WTIPSRDNNK
CYAKIICNTK DNERVVGFHV LGPNAGEVTQ GFAAALKCGL TKKQLDSTIG IHPVCAEVFT
TLSVTKRSGA SILQAGCUG
