ID   TXD12_EPICO             Reviewed;         173 AA.
AC   H9D1R1;
DT   18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2012, sequence version 1.
DT   25-MAY-2022, entry version 33.
DE   RecName: Full=Thioredoxin domain-containing protein 12 {ECO:0000303|PubMed:22789714, ECO:0000312|EMBL:AFD54638.1};
DE            EC=1.8.4.2 {ECO:0000269|PubMed:22789714};
DE   Flags: Precursor;
GN   Name=Txndc12 {ECO:0000303|PubMed:22789714};
OS   Epinephelus coioides (Orange-spotted grouper) (Epinephelus nebulosus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Serranoidei; Serranidae; Epinephelinae;
OC   Epinephelini; Epinephelus.
OX   NCBI_TaxID=94232 {ECO:0000312|EMBL:AFD54638.1};
RN   [1] {ECO:0000312|EMBL:AFD54638.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP   SPECIFICITY, INDUCTION, AND PHYLOGENETIC ANALYSIS.
RC   TISSUE=Liver {ECO:0000303|PubMed:22789714};
RX   PubMed=22789714; DOI=10.1016/j.fsi.2012.06.030;
RA   Wei J., Ji H., Guo M., Qin Q.;
RT   "Isolation and characterization of a thioredoxin domain-containing protein
RT   12 from orange-spotted grouper, Epinephelus coioides.";
RL   Fish Shellfish Immunol. 33:667-673(2012).
CC   -!- FUNCTION: Protein-disulfide reductase of the endoplasmic reticulum that
CC       promotes disulfide bond formation in client proteins through its thiol-
CC       disulfide oxidase activity. May function as an important antioxidant,
CC       and may be involved in the responses to viral infection.
CC       {ECO:0000269|PubMed:22789714}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-disulfide + 2 glutathione = [protein]-dithiol +
CC         glutathione disulfide; Xref=Rhea:RHEA:21064, Rhea:RHEA-COMP:10593,
CC         Rhea:RHEA-COMP:10594, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC         ChEBI:CHEBI:57925, ChEBI:CHEBI:58297; EC=1.8.4.2;
CC         Evidence={ECO:0000269|PubMed:22789714};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21066;
CC         Evidence={ECO:0000305|PubMed:22789714};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC       {ECO:0000250|UniProtKB:O95881, ECO:0000255|PROSITE-ProRule:PRU10138}.
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed. Expressed in stomach,
CC       spleen, intestine, gill, heart, head kidney and skin, with the highest
CC       levels in liver, brain, muscle and kidney.
CC       {ECO:0000269|PubMed:22789714}.
CC   -!- INDUCTION: (Microbial infection) Up-regulated to the highest level in
CC       liver 24 hours post Singapore grouper iridovirus (SGIV) infection. 8.2-
CC       fold induction after 4 hours of SGIV injection and the expression
CC       increases up to 42.3-fold at 24 hours post-injection, decreasing to
CC       11.1-fold at 48 hours post-injection. {ECO:0000269|PubMed:22789714}.
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DR   EMBL; JQ514561; AFD54638.1; -; mRNA.
DR   AlphaFoldDB; H9D1R1; -.
DR   SMR; H9D1R1; -.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; ISS:UniProtKB.
DR   GO; GO:0009055; F:electron transfer activity; IDA:UniProtKB.
DR   GO; GO:0019153; F:protein-disulfide reductase (glutathione) activity; IDA:UniProtKB.
DR   GO; GO:0051607; P:defense response to virus; IEP:UniProtKB.
DR   CDD; cd02959; ERp19; 1.
DR   InterPro; IPR037462; ERp19.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; Endoplasmic reticulum; Host-virus interaction;
KW   Oxidoreductase; Redox-active center; Signal.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..173
FT                   /note="Thioredoxin domain-containing protein 12"
FT                   /id="PRO_5003618491"
FT   MOTIF           170..173
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT   DISULFID        67..70
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   173 AA;  19222 MW;  B94D44680EA31713 CRC64;
     MQTSLANIVL FSSLQVLLSL TCFQEVVEAA SGKGFGDNIH WRTLDDGKKE AEASGLPIML
     IIHKSWCGAC KALKPKFAES KEISELAHNF VMINLEDEEE PKDDAFSPDG GYIPRILFLD
     PSGKVHPEIT NKNGNPNYKY FYSNAEQVIS GMKEAQEKLT GDAFKQRHTG DEL