THIO_MACMU
ID THIO_MACMU Reviewed; 105 AA.
AC P29451;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 138.
DE RecName: Full=Thioredoxin;
DE Short=Trx;
GN Name=TXN;
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1543487; DOI=10.1016/0006-291x(92)91624-y;
RA An G., Wu R.;
RT "Thioredoxin gene expression is transcriptionally up-regulated by retinol
RT in monkey conducting airway epithelial cells.";
RL Biochem. Biophys. Res. Commun. 183:170-175(1992).
CC -!- FUNCTION: Participates in various redox reactions through the
CC reversible oxidation of its active center dithiol to a disulfide and
CC catalyzes dithiol-disulfide exchange reactions (By similarity). Plays a
CC role in the reversible S-nitrosylation of cysteine residues in target
CC proteins, and thereby contributes to the response to intracellular
CC nitric oxide. Nitrosylates the active site Cys of CASP3 in response to
CC nitric oxide (NO), and thereby inhibits caspase-3 activity. Induces the
CC FOS/JUN AP-1 DNA binding activity in ionizing radiation (IR) cells
CC through its oxidation/reduction status and stimulates AP-1
CC transcriptional activity (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Interacts with TXNIP through the
CC redox-active site. Interacts with MAP3K5 and CASP3. Interacts with
CC APEX1; the interaction stimulates the FOS/JUN AP-1 DNA-binding activity
CC in a redox-dependent manner (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P10599}. Cytoplasm
CC {ECO:0000250|UniProtKB:P10599}. Secreted
CC {ECO:0000250|UniProtKB:P10599}. Note=Translocates from the cytoplasm
CC into the nucleus after phorbol 12-myristate 13-acetate induction (PMA).
CC Predominantly in the cytoplasm in non irradiated cells. Radiation
CC induces translocation of TRX from the cytoplasm to the nucleus.
CC Secreted by a leaderless secretory pathway.
CC {ECO:0000250|UniProtKB:P10599}.
CC -!- PTM: In the fully reduced protein, both Cys-69 and Cys-73 are
CC nitrosylated in response to nitric oxide (NO). When two disulfide bonds
CC are present in the protein, only Cys-73 is nitrosylated. Cys-73 can
CC serve as donor for nitrosylation of target proteins (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
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DR EMBL; M84643; AAA36921.1; -; mRNA.
DR PIR; JS0667; JS0667.
DR AlphaFoldDB; P29451; -.
DR SMR; P29451; -.
DR STRING; 9544.ENSMMUP00000013528; -.
DR eggNOG; KOG0907; Eukaryota.
DR InParanoid; P29451; -.
DR Proteomes; UP000006718; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
DR GO; GO:0043388; P:positive regulation of DNA binding; ISS:UniProtKB.
DR GO; GO:0009314; P:response to radiation; ISS:UniProtKB.
DR InterPro; IPR005746; Thioredoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00085; Thioredoxin; 1.
DR PIRSF; PIRSF000077; Thioredoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Acetylation; Activator; Cytoplasm; Disulfide bond; Electron transport;
KW Nucleus; Redox-active center; Reference proteome; S-nitrosylation;
KW Secreted; Transcription; Transcription regulation; Transport.
FT CHAIN 1..105
FT /note="Thioredoxin"
FT /id="PRO_0000120006"
FT DOMAIN 3..105
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 32
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 35
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT SITE 26
FT /note="Deprotonates C-terminal active site Cys"
FT /evidence="ECO:0000250"
FT SITE 33
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 34
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT MOD_RES 3
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P10599"
FT MOD_RES 8
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P10639"
FT MOD_RES 39
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P10599"
FT MOD_RES 62
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:P10599"
FT MOD_RES 69
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:P10599"
FT MOD_RES 73
FT /note="S-nitrosocysteine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10599"
FT MOD_RES 94
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10639"
FT MOD_RES 94
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10639"
FT DISULFID 32..35
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 73
FT /note="Interchain; alternate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 105 AA; 11737 MW; 929126DA137BE542 CRC64;
MVKQIESKAA FQEALDDAGD KLVVVDFSAT WCGPCKMIKP FFHSLSEKYS NVVFLEVDVD
DCQDVASECE VKCMPTFQFF KKGQKVGEFS GANKEKLEAT INELV
