Protein detail

CLIC5

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

Entry name
CLIC5
UniProt ID
EVMP confidence score
0.88
Supporting publications (n)
24
Transmembrane count
1
Protein classification
Basic Information
Protein Names
Chloride intracellular channel protein 5 (Glutaredoxin-like oxidoreductase CLIC5) (EC 1.8.-.-)
Protein Function (5)
  • 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
Supporting publications (n)
24
EVMP confidence score
0.88
Fluorescence & Localization
CLIC5 fluorescence
Function & Pathway
Relations & Evidence19

Enzyme-Mediated Modification (1)

1 record.

Substrate Gene SymbolEnzyme Gene SymbolEnzyme UniProt IDResidue TypeResidue OffsetModificationDatabaseReferences
CLIC5FYNP06241Y33phosphorylationPhosphoSite_MIMPMIMPProtMapperPhosphoSitePhosphoSite_ProtMapper

Ligand-Receptor Signaling (15)

15 records.

CategoryParentDatabaseTransmitterReceiverSecretedPlasma Membrane (Transmembrane)Plasma Membrane (Peripheral)
intracellularintracellularLOCATE
intracellularintracellularComPPI
intracellularintracellularGO_Intercell
intracellularintracellularUniProt_location
intracellularintracellularOmniPath
ion_channelion_channelDGIdbYes
transportertransporterOmniPathYes
ion_channelion_channelOmniPathYes
transmembranetransmembraneUniProt_location
transmembranetransmembraneUniProt_topology
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Regulatory Interaction Network (1)

1 record.

Source Protein SymbolSource UniProt IDTarget Protein SymbolTarget UniProt IDIs DirectedIs StimulationIs InhibitionDatabaseReferences
FYNP06241CLIC5Q9NZA1YesYesPhosphoSite_MIMPMIMPiPTMnetSIGNORProtMapperPhosphoSitePhosphoSite_ProtMapperPhosphoSite:10930415SIGNOR:10930415

Protein Complex Composition (1)

1 record.

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

Isolation & Detection Technology (1)

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.
Supporting Publications24
PMIDTitleRelated sentences
23585444Identification and characterization of proteins isolated from microvesicles derived from human lung cancer pleural effusions.No related sentences available
25471207Intraluminal proteome and peptidome of human urinary extracellular vesicles.No related sentences available
26538482Insights into immune responses in oral cancer through proteomic analysis of saliva and salivary extracellular vesicles.No related sentences available
30071318Changes in the urinary extracellular vesicle proteome are associated with nephronophthisis-related ciliopathies.No related sentences available
30760538Microvesicle Proteomic Profiling of Uterine Liquid Biopsy for Ovarian Cancer Early Detection.No related sentences available
32795414Extracellular Vesicle and Particle Biomarkers Define Multiple Human Cancers.Among traditional exosome markers, CD9, HSPA8, ALIX, and HSP90AB1 represent pan-EVP markers, while ACTB, MSN, and RAP1B are novel pan-EVP markers.
33709510Unbiased proteomic profiling of host cell extracellular vesicle composition and dynamics upon HIV-1 infection.No related sentences available
34186243A Reductionist Approach Using Primary and Metastatic Cell-Derived Extracellular Vesicles Reveals Hub Proteins Associated with Oral Cancer Prognosis.No related sentences available
36406491Automated Proteomics Sample Preparation of Phosphatidylserine-Positive Extracellular Vesicles from Human Body Fluids.No related sentences available
37686366Identification of a Non-Invasive Urinary Exosomal Biomarker for Diabetic Nephropathy Using Data-Independent Acquisition Proteomics.No related sentences available
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