Detail Information for IndEnz0018001609
IED ID IndEnz0018001609
Enzyme Type ID peroxidase001609
Protein Name Thioredoxin domain-containing protein 17
14 kDa thioredoxin-related protein
TRP14
Protein 42-9-9
Thioredoxin-like protein 5
Gene Name TXNDC17 TXNL5
Organism Homo sapiens (Human)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human)
Enzyme Sequence MARYEEVSVSGFEEFHRAVEQHNGKTIFAYFTGSKDAGGKSWCPDCVQAEPVVREGLKHISEGCVFIYCQVGEKPYWKDPNNDFRKNLKVTAVPTLLKYGTPQKLVESECLQANLVEMLFSED
Enzyme Length 123
Uniprot Accession Number Q9BRA2
Absorption
Active Site ACT_SITE 43; /note=Nucleophile; /evidence=ECO:0000269|PubMed:14607844; ACT_SITE 46; /note=Nucleophile; /evidence=ECO:0000269|PubMed:14607844
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: Disulfide reductase. May participate in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyze dithiol-disulfide exchange reactions. Modulates TNF-alpha signaling and NF-kappa-B activation. Has peroxidase activity and may contribute to the elimination of cellular hydrogen peroxide. {ECO:0000269|PubMed:14607843, ECO:0000269|PubMed:14607844}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Beta strand (5); Chain (1); Disulfide bond (1); Domain (1); Helix (7); Initiator methionine (1); Modified residue (1); Mutagenesis (2); Site (2); Turn (1)
Keywords 3D-structure;Acetylation;Cytoplasm;Direct protein sequencing;Disulfide bond;Redox-active center;Reference proteome
Interact With Q96B26; Q0VD86; Q96T51; Q9BSI4
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14607844}.
Modified Residue MOD_RES 2; /note=N-acetylalanine; /evidence=ECO:0007744|PubMed:19413330
Post Translational Modification PTM: The oxidized protein is reduced by TRXR1.
Signal Peptide
Structure 3D X-ray crystallography (1)
Cross Reference PDB 1WOU;
Mapped Pubmed ID 17353931; 18579519; 21044950; 24778250; 25416956; 25607466; 26496610; 33359085;
Motif
Gene Encoded By
Mass 13,941
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda 1.8.1.6;