THIO_CHICK
ID THIO_CHICK Reviewed; 105 AA.
AC P08629;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Thioredoxin;
DE Short=Trx;
GN Name=TXN;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2838473; DOI=10.1016/s0021-9258(19)81559-4;
RA Jones S.W., Luk K.-C.;
RT "Isolation of a chicken thioredoxin cDNA clone. Thioredoxin mRNA is
RT differentially expressed in normal and Rous sarcoma virus-transformed
RT chicken embryo fibroblasts.";
RL J. Biol. Chem. 263:9607-9611(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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P10599}. Cytoplasm
CC {ECO:0000250|UniProtKB:P10599}. Secreted
CC {ECO:0000250|UniProtKB:P10599}. Note=Shuttles between the nucleus and
CC nucleolus. {ECO:0000250|UniProtKB:Q811S9}.
CC -!- PTM: May be nitrosylated on several cysteine residues, depending on the
CC oxidation state. Nitrosylated Cys-73 may serve as donor for
CC nitrosylation of target proteins (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; J03882; AAA49092.1; -; mRNA.
DR PIR; A30006; A30006.
DR RefSeq; NP_990784.1; NM_205453.1.
DR AlphaFoldDB; P08629; -.
DR SMR; P08629; -.
DR BioGRID; 676686; 1.
DR STRING; 9031.ENSGALP00000025280; -.
DR PaxDb; P08629; -.
DR Ensembl; ENSGALT00000025326; ENSGALP00000025280; ENSGALG00000015704.
DR GeneID; 396437; -.
DR KEGG; gga:396437; -.
DR CTD; 7295; -.
DR VEuPathDB; HostDB:geneid_396437; -.
DR eggNOG; KOG0907; Eukaryota.
DR GeneTree; ENSGT00940000154259; -.
DR HOGENOM; CLU_090389_14_6_1; -.
DR InParanoid; P08629; -.
DR OMA; QVGVAPK; -.
DR OrthoDB; 1482186at2759; -.
DR PhylomeDB; P08629; -.
DR TreeFam; TF318932; -.
DR Reactome; R-GGA-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-GGA-3299685; Detoxification of Reactive Oxygen Species.
DR Reactome; R-GGA-499943; Interconversion of nucleotide di- and triphosphates.
DR Reactome; R-GGA-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-GGA-5676934; Protein repair.
DR Reactome; R-GGA-844456; The NLRP3 inflammasome.
DR PRO; PR:P08629; -.
DR Proteomes; UP000000539; Chromosome Z.
DR Bgee; ENSGALG00000015704; Expressed in kidney and 14 other tissues.
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 Activator; Cytoplasm; Disulfide bond; Electron transport; Nucleus;
KW Redox-active center; Reference proteome; S-nitrosylation; Secreted;
KW Transcription; Transcription regulation; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..105
FT /note="Thioredoxin"
FT /id="PRO_0000120013"
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 69
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250"
FT MOD_RES 73
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250"
FT DISULFID 32..35
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ SEQUENCE 105 AA; 11701 MW; 3A2398BAACE32EBB CRC64;
MVKSVGNLAD FEAELKAAGE KLVVVDFSAT WCGPCKMIKP FFHSLCDKFG DVVFIEIDVD
DAQDVATHCD VKCMPTFQFY KNGKKVQEFS GANKEKLEET IKSLV
