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0TXD13_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameTXNDC13
DescriptionThioredoxin domain containing protein 13 precursor.
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GON/A
Domain Architecture (Details)
InterPro domains unassigned to SynO:
Several biological processes regulate the activity of target proteins through changes in the redox state of thiol groups (S2 to SH2).here a hydrogen donor is linked to an intermediary disulphide protein. Such processes include the ferredoxin/thioredoxin system.he NADP/thioredoxin system.nd the glutathione/glutaredoxin system . Several of these disulphide proteins share a common structure.onsisting of a three-layer alpha/beta/alpha core. Proteins that contain this thioredoxin fold include: 2Fe-2S ferredoxin.hioltransferase.hosducin.lutathione peroxidase-like enzymes.rsenate reductase.isulphide bond isomerase DsbC (C-terminal domain).isulphide bond facilitator DsbA (contains an alpha-helical insertion).lutathione S-transferase (N-terminal domain).ndoplasmic reticulum protein ERP29 (N-terminal domain).pliceosomal protein U5-15Kd.ircadian oscillation regulator KaiB.rotein disulphide isomerase PDI (contains two tandem repeats of this fold).nd calsequestrin (contains three tandem repeats of this fold).This entry differs from the thioredoxin-like fold protein.he classification of this fold in glutathione S-transferase enzymes.here this entry defines two regions containing this fold.nd the thioredoxin-like fold protein defines only the N-terminal as containing this fold.
  IPR012335:Thioredoxin fold
Thioredoxins .re small disulphide-containing redox proteins that have been found in all the kingdoms of living organisms. Thioredoxin serves as a general protein disulphide oxidoreductase. It interacts with a broad range of proteins by a redox mechanism based on reversible oxidation of 2 cysteine thiol groups to a disulphide.ccompanied by the transfer of 2 electrons and 2 protons. The net result is the covalent interconversion of a disulphide and a dithiol. TR-S2 + NADPH + H+ -> TR-(SH)2 + NADP+ (1) trx-S2 + TR-(SH)2 -> trx-(SH)2 + TR-S2 (2) Protein-S2 + trx-(SH)2 -> Protein-(SH)2 + trx-S2 (3) In the NADPH-dependent protein disulphide reduction.hioredoxin reductase (TR) catalyses reduction of oxidised thioredoxin (trx) by NADPH using FAD and its redox-active disulphide (steps 1 and 2). Reduced thioredoxin then directly reduces the disulphide in the substrate protein (step 3) . Protein disulphide isomerase (PDI). resident foldase of the endoplasmic recticulum.s a multi-functional protein that catalyses the formation and isomerisation of disulphide bonds during protein folding . PDI contains 2 redox active domains.ear the N- and C-termini.hat are similar to thioredoxin: both contribute to disulphide isomerase activity.ut are functionally non-equivalent . Interestingly. mutant PDI.ith all 4 of the active cysteines replaced by serine.isplays a low but detectable level of disulphide isomerase activity . Moreover.DI exhibits chaperone-like activity towards proteins that contain no disulphide bonds..e. behaving independently of its disulphide isomerase activity . A number of endoplasmic reticulum proteins that differ from the PDI major isozyme contain 2 (ERp60.Rp5) or 3 (ERp72 ) thioredoxin domains; all of them seem to be PDIs. 3D-structures have been determined for a number of thioredoxins . The molecule has a doubly-wound alternating alpha/beta fold.onsisting of a 5-stranded parallel beta-sheet core.nclosed by 4 alpha-helices. The active site disulphide is located at the N-terminus of helix 2 in a short segment that is separated from the rest of the helix by a kink caused by a conserved proline. The 4-membered disulphide ring is located on the surface of the protein. A flat hydrophobic surface lies adjacent to the disulphide.hich presumably facilitates interaction with other proteins. One invariant feature of all thioredoxins is a cis-proline located in a loop preceding beta-strand 4. This residue is positioned in van der Waals contact with the active site cysteines and is important both for stability and function . Thioredoxin belongs to a structural family that includes glutaredoxin.lutathione peroxidase.acterial protein disulphide isomerase DsbA.nd the N-terminal domain of glutathione transferase . Thioredoxins have a beta-alpha unit preceding the motif common to all these proteins.
  IPR013766:Thioredoxin domain
Thioredoxins .re small disulphide-containing redox proteins that have been found in all the kingdoms of living organisms. Thioredoxin serves as a general protein disulphide oxidoreductase. It interacts with a broad range of proteins by a redox mechanism based on reversible oxidation of 2 cysteine thiol groups to a disulphide.ccompanied by the transfer of 2 electrons and 2 protons. The net result is the covalent interconversion of a disulphide and a dithiol. TR-S2 + NADPH + H+ -> TR-(SH)2 + NADP+ (1) trx-S2 + TR-(SH)2 -> trx-(SH)2 + TR-S2 (2) Protein-S2 + trx-(SH)2 -> Protein-(SH)2 + trx-S2 (3) In the NADPH-dependent protein disulphide reduction.hioredoxin reductase (TR) catalyses reduction of oxidised thioredoxin (trx) by NADPH using FAD and its redox-active disulphide (steps 1 and 2). Reduced thioredoxin then directly reduces the disulphide in the substrate protein (step 3) . Protein disulphide isomerase (PDI). resident foldase of the endoplasmic recticulum.s a multi-functional protein that catalyses the formation and isomerisation of disulphide bonds during protein folding . PDI contains 2 redox active domains.ear the N- and C-termini.hat are similar to thioredoxin: both contribute to disulphide isomerase activity.ut are functionally non-equivalent . Interestingly. mutant PDI.ith all 4 of the active cysteines replaced by serine.isplays a low but detectable level of disulphide isomerase activity . Moreover.DI exhibits chaperone-like activity towards proteins that contain no disulphide bonds..e. behaving independently of its disulphide isomerase activity . A number of endoplasmic reticulum proteins that differ from the PDI major isozyme contain 2 (ERp60.Rp5) or 3 (ERp72 ) thioredoxin domains; all of them seem to be PDIs. 3D-structures have been determined for a number of thioredoxins . The molecule has a doubly-wound alternating alpha/beta fold.onsisting of a 5-stranded parallel beta-sheet core.nclosed by 4 alpha-helices. The active site disulphide is located at the N-terminus of helix 2 in a short segment that is separated from the rest of the helix by a kink caused by a conserved proline. The 4-membered disulphide ring is located on the surface of the protein. A flat hydrophobic surface lies adjacent to the disulphide.hich presumably facilitates interaction with other proteins. One invariant feature of all thioredoxins is a cis-proline located in a loop preceding beta-strand 4. This residue is positioned in van der Waals contact with the active site cysteines and is important both for stability and function . Thioredoxin belongs to a structural family that includes glutaredoxin.lutathione peroxidase.acterial protein disulphide isomerase DsbA.nd the N-terminal domain of glutathione transferase . Thioredoxins have a beta-alpha unit preceding the motif common to all these proteins.
  IPR006662:Thioredoxin-related
Several biological processes regulate the activity of target proteins through changes in the redox state of thiol groups (S2 to SH2).here a hydrogen donor is linked to an intermediary disulphide protein. Such processes include the ferredoxin/thioredoxin system.he NADP/thioredoxin system.nd the glutathione/glutaredoxin system . Several of these disulphide proteins share a common structure.onsisting of a three-layer alpha/beta/alpha core. Proteins that contain this thioredoxin fold include: 2Fe-2S ferredoxin.hioltransferase.hosducin.lutathione peroxidase-like enzymes.rsenate reductase.isulphide bond isomerase DsbC (C-terminal domain).isulphide bond facilitator DsbA (contains an alpha-helical insertion).lutathione S-transferase (N-terminal domain).ndoplasmic reticulum protein ERP29 (N-terminal domain).pliceosomal protein U5-15Kd.ircadian oscillation regulator KaiB.rotein disulphide isomerase PDI (contains two tandem repeats of this fold).nd calsequestrin (contains three tandem repeats of this fold).This entry differs from the thioredoxin fold protein.he classification of this fold is in the glutathione S-transferase enzymes.here this entry defines two regions containing this fold.nd the thioredoxin fold protein defines only the N-terminal as containing this fold.
  IPR012336:Thioredoxin-like fold
IPR012335:Thioredoxin_fold 
Evalue:-13.7212467193604 
Location:31-137
SequencesProtein: TXD13_HUMAN (349 aa)
mRNA: NM_021156
Local Annotation
Synapse Ontology
Calcium release from RyR (Ryanodine Receptor) in the SR (Sarcoplasmic Reticulum) is activated by the calcium induced-calcium-release
sdb:0325 RyR-CICR  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 518 residues, 7909715-7911268Exon2: 23 residues, 7912440-7912504Exon3: 36 residues, 7915934-7916036Exon4: 17 residues, 7924672-7924718Exon5: 45 residues, 7928378-7928507Exon6: 17 residues, 7930142-7930188Exon7: 40 residues, 7938846-7938962Exon8: 105 residues, 7948084-7948393Exon9: 2 residues, -Jump to TXD13_HUMAN  
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