ID   THIOM_BOVIN             Reviewed;         166 AA.
AC   Q95108; Q2KHU7;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 2.
DT   03-AUG-2022, entry version 141.
DE   RecName: Full=Thioredoxin, mitochondrial;
DE            Short=MTRX;
DE            Short=Mt-Trx;
DE   AltName: Full=Thioredoxin-2;
DE   Flags: Precursor;
GN   Name=TXN2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 60-106 AND 111-166.
RC   TISSUE=Adrenal cortex;
RX   PubMed=9363753; DOI=10.1111/j.1432-1033.1997.t01-1-00052.x;
RA   Watabe S., Hiroi T., Yamamoto Y., Fujioka Y., Hasegawa H., Yago N.,
RA   Takahashi S.Y.;
RT   "SP-22 is a thioredoxin-dependent peroxide reductase in mitochondria.";
RL   Eur. J. Biochem. 249:52-60(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Heart ventricle;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Important for the control of mitochondrial reactive oxygen
CC       species homeostasis, apoptosis regulation and cell viability. Possesses
CC       a dithiol-reducing activity. {ECO:0000250|UniProtKB:Q99757}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
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DR   EMBL; D87741; BAA13447.1; -; mRNA.
DR   EMBL; BC112876; AAI12877.1; -; mRNA.
DR   RefSeq; NP_776633.1; NM_174208.2.
DR   AlphaFoldDB; Q95108; -.
DR   SMR; Q95108; -.
DR   IntAct; Q95108; 2.
DR   STRING; 9913.ENSBTAP00000000014; -.
DR   PaxDb; Q95108; -.
DR   PRIDE; Q95108; -.
DR   Ensembl; ENSBTAT00000000014; ENSBTAP00000000014; ENSBTAG00000000014.
DR   GeneID; 281557; -.
DR   KEGG; bta:281557; -.
DR   CTD; 25828; -.
DR   VEuPathDB; HostDB:ENSBTAG00000000014; -.
DR   VGNC; VGNC:36533; TXN2.
DR   eggNOG; KOG0910; Eukaryota.
DR   GeneTree; ENSGT00530000064086; -.
DR   HOGENOM; CLU_090389_11_1_1; -.
DR   InParanoid; Q95108; -.
DR   OMA; CTPCKAL; -.
DR   OrthoDB; 1482186at2759; -.
DR   TreeFam; TF314517; -.
DR   Reactome; R-BTA-1614558; Degradation of cysteine and homocysteine.
DR   Reactome; R-BTA-3299685; Detoxification of Reactive Oxygen Species.
DR   Proteomes; UP000009136; Chromosome 5.
DR   Bgee; ENSBTAG00000000014; Expressed in digestive system secreted substance and 104 other tissues.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR   GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
DR   GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
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   SUPFAM; SSF52833; SSF52833; 1.
DR   TIGRFAMs; TIGR01068; thioredoxin; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Disulfide bond; Electron transport;
KW   Mitochondrion; Redox-active center; Reference proteome; Transit peptide;
KW   Transport.
FT   TRANSIT         1..59
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000269|PubMed:9363753"
FT   CHAIN           60..166
FT                   /note="Thioredoxin, mitochondrial"
FT                   /id="PRO_0000034149"
FT   DOMAIN          61..166
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   ACT_SITE        90
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        93
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   SITE            84
FT                   /note="Deprotonates C-terminal active site Cys"
FT                   /evidence="ECO:0000250"
FT   SITE            91
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            92
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         152
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q99757"
FT   MOD_RES         152
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P97493"
FT   DISULFID        90..93
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   CONFLICT        33
FT                   /note="Q -> K (in Ref. 1; BAA13447)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   166 AA;  18416 MW;  D796F7C155EA5F4A CRC64;
     MAQRLLLRRF LTSIISGKPS QSRWAPVASR ALQTPQYSPG YLTVTPSQAR SIYTTRVCST
     TFNIQDGPDF QDRVVNSETP VVVDFHAQWC GPCKILGPRL EKVVAKQHGK VVMAKVDIDD
     HTDLALEYEV SAVPTVLAMK NGDVVDKFVG IKDEDQLEAF LKKLIG