THIO_ICTPU
ID THIO_ICTPU Reviewed; 107 AA.
AC Q9DGI3;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Thioredoxin;
DE Short=Trx;
GN Name=txn; Synonyms=trx;
OS Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Ictaluridae; Ictalurus.
OX NCBI_TaxID=7998;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11207242; DOI=10.4049/jimmunol.166.5.2937;
RA Khayat M., Stuge T.B., Wilson M., Bengten E., Miller N.W., Clem L.W.;
RT "Thioredoxin acts as a B cell growth factor in channel catfish.";
RL J. Immunol. 166:2937-2943(2001).
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-75 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; AF293651; AAG00612.1; -; mRNA.
DR RefSeq; NP_001187021.1; NM_001200092.1.
DR AlphaFoldDB; Q9DGI3; -.
DR SMR; Q9DGI3; -.
DR STRING; 7998.ENSIPUP00000010620; -.
DR GeneID; 100304506; -.
DR KEGG; ipu:100304506; -.
DR CTD; 7295; -.
DR OrthoDB; 1482186at2759; -.
DR Proteomes; UP000221080; Chromosome 7.
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:0042100; P:B cell proliferation; IDA:AgBase.
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; S-nitrosylation; Secreted; Transcription;
KW Transcription regulation; Transport.
FT CHAIN 1..107
FT /note="Thioredoxin"
FT /id="PRO_0000120015"
FT DOMAIN 2..107
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 71
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250"
FT MOD_RES 75
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 107 AA; 11953 MW; 01DD342F138CF75F CRC64;
MVVHIENLNA FSAALKNAGD KLVVVDFTAT WCGPCQKIGP IFETLSKSED YQNVVFLKVD
VDDAADVSSH CDIKCMPTFH FYKNGQKIDE FSGANEQTLK QKINDHK