ID   THIO_RABIT              Reviewed;         105 AA.
AC   P08628;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 2.
DT   02-SEP-2026, entry version 143.
DE   RecName: Full=Thioredoxin;
DE            Short=Trx;
GN   Name=TXN;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   PROTEIN SEQUENCE OF 2-105, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Bone marrow;
RX   PubMed=3164311; DOI=10.1016/s0021-9258(19)81557-0;
RA   Johnson R.S., Mathews W.R., Biemann K., Hopper S.;
RT   "Amino acid sequence of thioredoxin isolated from rabbit bone marrow
RT   determined by tandem mass spectrometry.";
RL   J. Biol. Chem. 263:9589-9597(1988).
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   PIR; A28086; A28086.
DR   AlphaFoldDB; P08628; -.
DR   SMR; P08628; -.
DR   FunCoup; P08628; 1152.
DR   STRING; 9986.ENSOCUP00000037757; -.
DR   PaxDb; 9986-ENSOCUP00000037757; -.
DR   eggNOG; KOG0907; Eukaryota.
DR   InParanoid; P08628; -.
DR   Proteomes; UP000001811; 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:0019725; P:cellular homeostasis; IEA:UniProtKB-ARBA.
DR   GO; GO:0043388; P:positive regulation of DNA binding; ISS:UniProtKB.
DR   GO; GO:0009314; P:response to radiation; ISS:UniProtKB.
DR   CDD; cd02947; TRX_family; 1.
DR   FunFam; 3.40.30.10:FF:000130; Thioredoxin; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR005746; Thioredoxin.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR46115; THIOREDOXIN-LIKE PROTEIN 1; 1.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   PIRSF; PIRSF000077; Thioredoxin; 1.
DR   PRINTS; PR00421; THIOREDOXIN.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Activator; Cytoplasm; Direct protein sequencing;
KW   Disulfide bond; Electron transport; Nucleus; Redox-active center;
KW   Reference proteome; S-nitrosylation; Secreted; Transcription;
KW   Transcription regulation; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:3164311"
FT   CHAIN           2..105
FT                   /note="Thioredoxin"
FT                   /id="PRO_0000120010"
FT   DOMAIN          2..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;  11761 MW;  9E239D2AD71FB6B6 CRC64;
     MVKQIESKSA FQEVLDSAGD KLVVVDFSAT WCGPCKMIKP FFHALSEKFN NVVFIEVDVD
     DCKDIAAECE VKCMPTFQFF KKGQKVGEFS GANKEKLEAT INELL
//