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0TXND6_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameTXNDC6
DescriptionThioredoxin domain containing protein 6 (thioredoxin-like protein 2) (txl-2).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GON/A
Domain Architecture (Details)
InterPro domains unassigned to SynO:
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
Nucleoside diphosphate kinases () (NDK) are enzymes required for the synthesis of nucleoside triphosphates (NTP) other than ATP. They provide NTPs for nucleic acid synthesis.TP for lipid synthesis.TP for polysaccharide synthesis and GTP for protein elongation.ignal transduction and microtubule polymerization.In eukaryotes.here seems to be a small family of NDK isozymes each of which acts in a different subcellular compartment and/or has a distinct biological function. Eukaryotic NDK isozymes are hexamers of two highly related chains (A and B) . By random association (A6.5B...AB5.6).hese two kinds of chain form isoenzymes differing in their isoelectric point.NDK are proteins of 17 Kd that act via a ping-pong mechanism in which a histidine residue is phosphorylated.y transfer of the terminal phosphate group from ATP. In the presence of magnesium.he phosphoenzyme can transfer its phosphate group to any NDP.o produce an NTP.NDK isozymes have been sequenced from prokaryotic and eukaryotic sources. It has also been shown that the Drosophila awd (abnormal wing discs) protein.s a microtubule-associated NDK. Mammalian NDK is also known as metastasis inhibition factor nm23. The sequence of NDK has been highly conserved through evolution. There is a single histidine residue conserved in all known NDK isozymes.hich is involved in the catalytic mechanism . Our signature pattern contains this residue.
  IPR001564:Nucleoside diphosphate kinase
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-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
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
Dyneins are molecular motors that generate force against microtubules to produce different type of cellular movements. Members of this family have been shown to be outer arm dynein intermediate chains with an unusual domain organisation: they contain thioredoxin and nucleoside-diphosphate kinase (NDK) domains (up to three repeats). Characterised members include IC1 from Anthocidaris crassispina .C3 from Ciona intestinalis. Additionally.uman Sptrx-1 (NM23-H8.perm-specific thioredoxin 2) has been shown to be specifically expressed in sperm cells and its gene maps to a potential locus for flagellar anomalies and male infertility phenotypes ; and human thioredoxin-like protein 2 (Txl-2) has been shown to bind microtubules and is expressed predominantly in the cilia of lung airway epithelium and spermatid manchette and axoneme . Presence of such a dynein intermediate chain (termed TNDK-DIC.or thioredoxin and NDPK-related dynein intermediate chain) in three distantly related species suggests that it was acquired in metazoans during evolution .
  IPR012384:Dynein intermediate chain, thioredoxin and NDK regions
IPR001564:NDK 
Evalue:-59.8538719643218 
Location:158-302IPR013766:Thioredoxin 
Evalue:-3.43179821968079 
Location:11-112IPR000408:RCC1_2 
Evalue:0 
Location:0-0
SequencesProtein: TXND6_HUMAN (330 aa)
mRNA: AF196568
Local Annotation
Synapse Ontology
microtubules of the presynaptic compartment function as the tracks for the intense traffic of organelles from cell body to axon terminals and vice versa. It is generally excluded from the presynaptic vesicle cluster.Microtubules do not directly regulate synapse morphology or function
sdb:0087 microtubules  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 164 residues, 139502745-139503236Exon2: 47 residues, 139505038-139505175Exon3: 53 residues, 139506404-139506559Exon4: 33 residues, 139507535-139507628Exon5: 29 residues, 139507929-139508012Exon6: 27 residues, 139515863-139515939Exon7: 41 residues, 139517058-139517175Exon8: 26 residues, 139519679-139519751Exon9: 36 residues, 139521009-139521113Exon10: 21 residues, 139526404-139526462Exon11: 22 residues, 139530834-139530895Exon12: 2 residues, -Jump to TXND6_HUMAN  
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