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Search results 301 to 309 out of 309 for Clic5

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0.016s

Type

Details

Score

Protein Domain

IPR030264 | CLIC-5

Type:

Family

Description:

CLIC5 belongs to a family of six vertebrate chloride intracellular channel (CLIC) proteins, all sharing a conserved C-terminal CLIC module []. CLIC5 associates with the cortical actin cytoskeleton [, ]. It is strongly and reversibly inhibited by cytosolic F-actin []. The isoform CLIC5A is required for the development and/or maintenance of the proper glomerular endothelial cell and podocyte architecture [].

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Publication

15184393 | -

First Author:	Berryman M
Year:	2004
Journal:	J Biol Chem
Title:	CLIC-5A functions as a chloride channel in vitro and associates with the cortical actin cytoskeleton in vitro and in vivo.
Volume:	279
Issue:	33
Pages:	34794-801

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Publication

20948539 | -

First Author:	Edwards JC
Year:	2010
Journal:	Kidney Int
Title:	What's a CLIC doing in the podocyte?
Volume:	78
Issue:	9
Pages:	831-3

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Protein Domain

IPR042069 | CLIC5_C_GST

Type:

Domain

Description:

This entry represents the C-terminal glutathione S-transferase (GST) domain found in chloride intracellular channel 5 (CLIC5) protein. CLIC5 exists in two alternatively-spliced isoforms, CLIC5A or CLIC5B (also called p64) []. It is expressed at high levels in hair cell stereocilia and is associated with the actin cytoskeleton and ezrin []. A recessive mutation in the CLIC5 gene in mice led to the lack of coordination and deafness, due to a defect in the basal region of the hair bundle causing stereocilia to degrade. CLIC5 is therefore essential for normal inner ear function []. CLIC5 is also highly expressed in podocytes where it is colocalized with the ezrin/radixin/moesin (ERM) complex. It is essential for foot process integrity, and for podocyte morphology and function [, ].CLICs are auto-inserting, self-assembling intracellular anion channels involved in a wide variety of functions including regulated secretion, cell division, and apoptosis. They can exist in both water-soluble and membrane-bound states and are found in various vesicles and membranes, and they may play roles in the maintenance of these intracellular membranes. The membrane localization domain is present in the N-terminal part of the protein. Structures of soluble CLICs reveal that they adopt a fold similar to GSTs, containing an N-terminal domain with a thioredoxin fold and a C-terminal alpha helical domain [, , ].

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Publication

20085760 | -

First Author:	Littler DR
Year:	2010
Journal:	FEBS Lett
Title:	The enigma of the CLIC proteins: Ion channels, redox proteins, enzymes, scaffolding proteins?
Volume:	584
Issue:	10
Pages:	2093-101

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Publication

12202911 | -

First Author:	Cromer BA
Year:	2002
Journal:	Eur Biophys J
Title:	From glutathione transferase to pore in a CLIC.
Volume:	31
Issue:	5
Pages:	356-64

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Protein

Q9CYD1

Organism:	Mus musculus/domesticus
Length:	243
Fragment?:	false

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Protein

Q8BXK9

Organism:	Mus musculus/domesticus
Length:	251
Fragment?:	false

•

Protein

A0A668KLB7

Organism:	Mus musculus/domesticus
Length:	485
Fragment?:	false

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