Protein detail

CLIC5

Chloride intracellular channel protein 5 (Glutaredoxin-like oxidoreductase CLIC5) (EC 1.8.-.-)

Protein symbol
CLIC5
UniProt ID
EVMP score
0.75
Frequency
24
Transmembrane count
1
Protein classification
Basic Information
Protein Names
Chloride intracellular channel protein 5 (Glutaredoxin-like oxidoreductase CLIC5) (EC 1.8.-.-)
Protein Function
  • Predicted intracellular proteins
  • Potential drug targets
  • Transporters:Transporter channels and pores
  • Disease related genes
  • Human disease related genes:Nervous system diseases:Ear disease
Transmembrane
193..213; Helical; Note=After insertion into the membrane
Transmembrane Count
1
Entrez Gene Symbol
Frequency
24
EVMP Score
0.75
Fluorescence & Localization
Function & Pathway
Relations & Evidence

Enzyme-Mediated Modification

1 record.

Substrate Gene SymbolEnzyme Gene SymbolEnzyme UniProt IDResidue TypeResidue OffsetModificationDatabaseReferences
CLIC5FYNP06241Y33phosphorylationPhosphoSite_MIMPMIMPProtMapperPhosphoSitePhosphoSite_ProtMapper

Ligand-Receptor Signaling

15 records.

CategoryParentDatabaseTransmitterReceiverSecretedPlasma Membrane (Transmembrane)Plasma Membrane (Peripheral)
intracellularintracellularLOCATENoNoNoNoNo
intracellularintracellularComPPINoNoNoNoNo
intracellularintracellularGO_IntercellNoNoNoNoNo
intracellularintracellularUniProt_locationNoNoNoNoNo
intracellularintracellularOmniPathNoNoNoNoNo
ion_channelion_channelDGIdbNoYesNoNoNo
transportertransporterOmniPathNoYesNoNoNo
ion_channelion_channelOmniPathNoYesNoNoNo
transmembranetransmembraneUniProt_locationNoNoNoNoNo
transmembranetransmembraneUniProt_topologyNoNoNoNoNo
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Regulatory Interaction Network

1 record.

Source Protein SymbolSource UniProt IDTarget Protein SymbolTarget UniProt IDIs DirectedIs StimulationIs InhibitionDatabaseReferences
FYNP06241CLIC5Q9NZA1YesYesNoPhosphoSite_MIMPMIMPiPTMnetSIGNORProtMapperPhosphoSitePhosphoSite_ProtMapperPhosphoSite:10930415SIGNOR:10930415

Protein Complex Composition

1 record.

Component NameComponent Gene SymbolsComponent UniProt IDStoichiometryDatabaseDatabase IDsReferences
CLIC5Q9NZA14PDBPDB:6y2hPDB:8q4jPDB:8q4i

Isolation & Detection Technology

1 record.

EV Isolation MethodDetection MethodNumber of ReferencesReferences
Density Gradient CentrifugationMass spectrometry135495589
Sequence, Structure & Domains

Sequences

Length
410
Mass
46,503
Sequence
MNDEDYSTIYDTIQNERTYEVPDQPEENESPHYDDVHEYLRPENDLYATQLNTHEYDFVSVYTIKGEETSLASVQSEDRGYLLPDEIYSELQEAHPGEPQEDRGISMEGLYSSTQDQQLCAAELQENGSVMKEDLPSPSSFTIQHSKAFSTTKYSCYSDAEGLEEKEGAHMNPEIYLFVKAGIDGESIGNCPFSQRLFMILWLKGVVFNVTTVDLKRKPADLHNLAPGTHPPFLTFNGDVKTDVNKIEEFLEETLTPEKYPKLAAKHRESNTAGIDIFSKFSAYIKNTKQQNNAALERGLTKALKKLDDYLNTPLPEEIDANTCGEDKGSRRKFLDGDELTLADCNLLPKLHVVKIVAKKYRNYDIPAEMTGLWRYLKNAYARDEFTNTCAADSEIELAYADVAKRLSRS
Alternative Products
Event=Alternative splicing; Named isoforms=3; Name=2; Synonyms=CLIC5B; IsoId=Q9NZA1-1; Sequence=Displayed; Name=1; Synonyms=CLIC5A; IsoId=Q9NZA1-2; Sequence=VSP_000869, VSP_000870; Name=3; IsoId=Q9NZA1-3; Sequence=VSP_044889, VSP_044890, VSP_044891
Alternative Sequence
1..159; Missing (in isoform 1); 1..17; MNDEDYSTIYDTIQNER -> MTDSATANGDDRDPEIE (in isoform 3); 18..176; Missing (in isoform 3); 160..180; AEGLEEKEGAHMNPEIYLFVK -> MTDSATANGDDRDPEIELFVK (in isoform 1); 356..410; IVAKKYRNYDIPAEMTGLWRYLKNAYARDEFTNTCAADSEIELAYADVAKRLSRS -> EQVPLKGMI (in isoform 3)

3D Structural Models

Turn
257..259; 272..276; 400..403
Helix
192..204; 244..254; 268..271; 277..286; 290..292; 293..312; 316..319; 342..362; 371..381; 384..387; 393..399
Beta Strand
175..181; 185..188; 209..213; 233..236; 239..241; 337..339
3D Structure
X-ray crystallography (3)

Domain & Motif Annotations

Motif
191..194; G-site
Domain (CC)
The active G-site contains a monothiol Cys-X-X-Ser motif which mediates glutathione-dependent redox catalysis.; DOMAIN: Members of this family may change from a globular, soluble state to a state where the N-terminal domain is inserted into the membrane and functions as a chloride channel. The redox status of the active cysteine in Cys-X-X-Cys/Ser motif likely determines the capacity to adopt a soluble or membrane-inserted state. A conformation change of the N-terminal domain is thought to expose hydrophobic surfaces that trigger membrane insertion (By similarity).
Domain (FT)
260..400; GST C-terminal
Protein Families
Chloride channel CLIC family
Sequence Similarities
Belongs to the chloride channel CLIC family.
Clinical Relevance