TXD17_EPICO
ID TXD17_EPICO Reviewed; 123 AA.
AC T1SH39;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2013, sequence version 1.
DT 25-MAY-2022, entry version 20.
DE RecName: Full=Thioredoxin domain-containing protein 17 {ECO:0000305};
DE AltName: Full=14 kDa thioredoxin-related protein {ECO:0000303|PubMed:23994424};
DE Short=TRP14 {ECO:0000303|PubMed:23994424};
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:AGT42005.1};
RN [1] {ECO:0000312|EMBL:AGT42005.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND
RP PHYLOGENETIC ANALYSIS.
RX PubMed=23994424; DOI=10.1016/j.fsi.2013.08.010;
RA Wei J., Ji H., Guo M., Yan Y., Qin Q.;
RT "Identification and characterization of TRP14, a thioredoxin-related
RT protein of 14 kDa from orange-spotted grouper, Epinephelus coioides.";
RL Fish Shellfish Immunol. 35:1670-1676(2013).
CC -!- FUNCTION: Disulfide reductase. May participate in various redox
CC reactions through the reversible oxidation of its active center dithiol
CC to a disulfide and catalyze dithiol-disulfide exchange reactions
CC (PubMed:23994424). Has peroxidase activity and may contribute to the
CC elimination of cellular hydrogen peroxide (By similarity). May function
CC as an antioxidant involved in response to viral infection
CC (PubMed:23994424). {ECO:0000250|UniProtKB:Q9BRA2,
CC ECO:0000269|PubMed:23994424}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9BRA2}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in liver, brain and muscle.
CC Also expressed in kidney, intestine, skin, stomach, gill and head
CC kidney. {ECO:0000269|PubMed:23994424}.
CC -!- INDUCTION: Up-regulated in liver in response to Singapore grouper
CC iridovirus (SGIV) infection. 2.8-fold induction after 8 h injection of
CC SGIV and the expression increases up to about 70-fold at 72 hours post
CC injection, then decreases to about 26-fold at 120 h.
CC {ECO:0000269|PubMed:23994424}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
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DR EMBL; KC969667; AGT42005.1; -; mRNA.
DR AlphaFoldDB; T1SH39; -.
DR SMR; T1SH39; -.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0004601; F:peroxidase activity; ISS:UniProtKB.
DR GO; GO:0047134; F:protein-disulfide reductase (NAD(P)) activity; IDA:UniProtKB.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR045108; TXNDC17-like.
DR InterPro; IPR010357; TXNDC17_dom.
DR PANTHER; PTHR12452; PTHR12452; 1.
DR Pfam; PF06110; DUF953; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Disulfide bond; Redox-active center.
FT CHAIN 1..123
FT /note="Thioredoxin domain-containing protein 17"
FT /id="PRO_0000437968"
FT DOMAIN 41..123
FT /note="Thioredoxin"
FT /evidence="ECO:0000255"
FT ACT_SITE 43
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9BRA2"
FT ACT_SITE 46
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9BRA2"
FT SITE 44
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250|UniProtKB:Q9BRA2"
FT SITE 45
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250|UniProtKB:Q9BRA2"
FT DISULFID 43..46
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:Q9BRA2"
SQ SEQUENCE 123 AA; 14009 MW; D25279C448CA6B1F CRC64;
MAHYEEVNVR GYDEFCQAVS ERKGKDIFAY FSGDKDASGK SWCPDCVTAE PIVRGQMSHL
PEGSVFIYCQ VGERAYWKDS TNAFKKTLKL SGVPTLLRYG TPQKLVEEEC FKADLVRMMF
TED
