ID   THIO_CANLF              Reviewed;          21 AA.
AC   P99505;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 2.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Thioredoxin;
DE            Short=Trx;
DE   Flags: Fragment;
GN   Name=TXN;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   PROTEIN SEQUENCE OF 2-21.
RC   TISSUE=Heart;
RA   Dunn M.J., Wheeler C.H.;
RL   Submitted (AUG-1997) to UniProtKB.
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   -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
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DR   AlphaFoldDB; P99505; -.
DR   Proteomes; UP000002254; 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:0043388; P:positive regulation of DNA binding; ISS:UniProtKB.
DR   GO; GO:0009314; P:response to radiation; ISS:UniProtKB.
PE   1: Evidence at protein level;
KW   Acetylation; Activator; Cytoplasm; Direct protein sequencing;
KW   Electron transport; Nucleus; Redox-active center; Reference proteome;
KW   Secreted; Transcription; Transcription regulation; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|Ref.1"
FT   CHAIN           2..>21
FT                   /note="Thioredoxin"
FT                   /id="PRO_0000120002"
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   UNSURE          7
FT   NON_TER         21
SQ   SEQUENCE   21 AA;  2418 MW;  A0699186500086A6 CRC64;
     MVKQIEFKYA FQEALNSAGD K