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0CLIC4_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameCLIC4
DescriptionChloride intracellular channel protein 4 (intracellular chloride ion channel protein p64h1).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005254 chloride channel activity (TAS)
Domain Architecture (Details)
InterPro domains unassigned to SynO:
Chloride (Cl-) channels are known to be present in the plasma andintracellular membranes of many cell types. Whilst the molecular identityof plasma membrane Cl- channels has been known for some time.nly recentlyhave intracellular Cl- channels been characterised. Initially. 64 kDaprotein was purified from solubilised kidney cortical membranes.hich.henreconstituted into phospholipid vesicles.ave rise to chloride channelactivity . An antibody generated against this protein (p64) wassubsequently used to identify and clone it. The predicted amino acidsequence for p64 shows that it contains two.r possibly four.utativetransmembrane (TM) domains and a number of possible phosphorylation sites.Expression studies have revealed that it is targeted to intracellularorganelles.ot the plasma membrane .Subsequently. number of homologous cDNAs have been identified.hich.hen expressed.ive rise to Cl- channels in the membranes of both cellnuclei and endoplasmic reticulum . They do not show significantsequence similarity to the CLC family of plasma membrane voltage-gated Cl-channels.
  IPR002946:Intracellular chloride channel
In eukaryotes.lutathione S-transferases (GSTs) participate in the detoxification of reactive electrophilic compounds by catalysing their conjugation to glutathione. GST is found as a domain in S-crystallins from squid.nd proteins with no known GST activity.uch as eukaryotic elongation factors 1-gamma and the HSP26 family of stress-related proteins.hich include auxin-regulated proteins in plants and stringent starvation proteins in Escherichia coli. The major lens polypeptide of cephalopods is also a GST . Bacterial GSTs of known function often have a specific.rowth-supporting role in biodegradative metabolism: epoxide ring opening and tetrachlorohydroquinone reductive dehalogenation are two examples of the reactions catalysed by these bacterial GSTs. Some regulatory proteins.ike the stringent starvation proteins.lso belong to the GST family . GST seems to be absent from Archaea in which gamma-glutamylcysteine substitute to glutathione as major thiol.Glutathione S-transferases form homodimers.ut in eukaryotes can also form heterodimers of the A1 and A2 or YC1 and YC2 subunits. The homodimeric enzymes display a conserved structural fold. Each monomer is composed of a distinct N-terminal sub-domain.hich adopts the thioredoxin fold.nd a C-terminal all-helical sub-domain.hich adopts a 4-helical bundle fold. This entry is the C-terminal domain.Glutaredoxin 2 (Grx2).lutathione-dependent disulphide oxidoreductases.s structurally similar to GSTs.ven though they lack any sequence similarity. Grx2 is also composed of N and C terminal subdomains. It is thought that the primary function of Grx2 is to catalyse reversible glutathionylation of proteins with glutathione in cellular redox regulation including the response to oxidative stress. Grx2 is dissimilar to other glutaredoxins apart from containing the conserved active site residues .The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR010987:Glutathione S-transferase, C-terminal-like
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
IPR010987:GST_C_like 
Evalue:0 
Location:101-250IPR012336:IPR012336 
Evalue:0 
Location:16-100
SequencesProtein: CLIC4_HUMAN (253 aa)
mRNA: NM_013943
Local Annotation
Synapse Ontology
Large dense core vesicle are not selectively concentrated in proximity to the presynaptic plasma membrane and indeed are often excluded from the synaptic vesicle cluster. it is in a very low number.
sdb:0084 large dense core vesicle  (Evidence:keywords)
KO assignmentK05024
  Level 3 annotation:
    chloride intracellular channel 4
  Level 2 annotation:
    Ion channels
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 90 residues, 24944434-24944703Exon2: 38 residues, 24996819-24996929Exon3: 44 residues, 25013171-25013297Exon4: 37 residues, 25026087-25026194Exon5: 62 residues, 25038937-25039119Exon6: 1167 residues, 25039850-25043345Exon7: 2 residues, -Jump to CLIC4_HUMAN  
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