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1.A.12.1.6
Chloride intracellular channel protein 4, CLIC4.  Regulates the histamine H3 receptor (Maeda et al., 2008)) Discriminates poorly between anions and cations (Singh and Ashley, 2007). 76% identical to CLIC5.  May play a role in cancer (Peretti et al. 2014).

Accession Number:Q9Y696
Protein Name:CLIC4
Length:253
Molecular Weight:28772.00
Species:Homo sapiens (Human) [9606]
Number of TMSs:1
Location1 / Topology2 / Orientation3: Cytoplasm1 / Single-pass membrane protein2
Substrate Cl-

Cross database links:

Genevestigator: Q9Y696
HEGENOM: HBG444630
RefSeq: NP_039234.1   
Entrez Gene ID: 25932   
OMIM: 606536  gene
KEGG: hsa:25932   

Gene Ontology

GO:0015629 C:actin cytoskeleton
GO:0034707 C:chloride channel complex
GO:0030659 C:cytoplasmic vesicle membrane
GO:0005902 C:microvillus
GO:0005634 C:nucleus
GO:0005886 C:plasma membrane
GO:0005625 C:soluble fraction
GO:0005247 F:voltage-gated chloride channel activity
GO:0030154 P:cell differentiation
GO:0006821 P:chloride transport
GO:0030336 P:negative regulation of cell migration

References (11)

[1] “A novel p64-related Cl- channel: subcellular distribution and nephron segment-specific expression.”  Edwards J.C.et.al.   10070163
[2] “A 29 kDa intracellular chloride channel p64H1 is associated with large dense-core vesicles in rat hippocampal neurons.”  Chuang J.Z.et.al.   10191309
[3] “Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs.”  Wiemann S.et.al.   11230166
[4] “The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).”  The MGC Project Teamet.al.   15489334
[5] “Reciprocal modifications of CLIC4 in tumor epithelium and stroma mark malignant progression of multiple human cancers.”  Suh K.S.et.al.   17200346
[6] “CLIC4 mediates and is required for Ca2+-induced keratinocyte differentiation.”  Suh K.S.et.al.   17636002
[7] “CLIC4 interacts with histamine H3 receptor and enhances the receptor cell surface expression.”  Maeda K.et.al.   18302930
[8] “Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.”  Gauci S.et.al.   19413330
[9] “Lysine acetylation targets protein complexes and co-regulates major cellular functions.”  Choudhary C.et.al.   19608861
[10] “Crystal structure of the soluble form of the redox-regulated chloride ion channel protein CLIC4.”  Littler D.R.et.al.   16176272
[11] “Trimeric structure of the wild soluble chloride intracellular ion channel CLIC4 observed in crystals.”  Li Y.et.al.   16581025
Structure:
2AHE   2D2Z   3OQS     

External Searches:

  • Search: DB with
  • BLAST ExPASy (Swiss Institute of Bioinformatics (SIB) BLAST)
  • CDD Search (Conserved Domain Database)
  • Search COGs (Clusters of Orthologous Groups of proteins)
  • 2° Structure (Network Protein Sequence Analysis)

Analyze:

Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MALSMPLNGL KEEDKEPLIE LFVKAGSDGE SIGNCPFSQR LFMILWLKGV VFSVTTVDLK 
61:	RKPADLQNLA PGTHPPFITF NSEVKTDVNK IEEFLEEVLC PPKYLKLSPK HPESNTAGMD 
121:	IFAKFSAYIK NSRPEANEAL ERGLLKTLQK LDEYLNSPLP DEIDENSMED IKFSTRKFLD 
181:	GNEMTLADCN LLPKLHIVKV VAKKYRNFDI PKEMTGIWRY LTNAYSRDEF TNTCPSDKEV 
241:	EIAYSDVAKR LTK