TCDB is operated by the Saier Lab Bioinformatics Group
« See all members of the family


2.A.49.2.3
The hepatocyte canalicular chloride channel/carrier, CLC-3 or CLCN3 (I- > Br- > Cl-); outward rectifying; inactivated at positive voltages (Shimada et al., 2000). Oxidation induces surface expression of ClC-3 and activation of ClC-3-dependent anion permeability (Kasinathan et al., 2007). It is swell-activated in human neutrophils during a respiratory burst (Ahluwalia, 2008). The ClC-3 Cl-/H+ antiporter becomes uncoupled at low extracellular pH (Matsuda et al., 2010).  It transports superoxide, O2- (Hawkins et al. 2007; Fisher 2009). ClC-3 might be involved in modulating vascular remodeling in hypertension and arteriosclerosis (Guan et al. 2006). ClC-3 upregulation may protect against oxidative stress-induced necrosis (Remillard and Yuan 2005).

Accession Number:P51792
Protein Name:Chloride channel protein 3 aka ClC-3
Length:818
Molecular Weight:90855.00
Species:Rattus norvegicus (Rat) [10116]
Number of TMSs:10
Location1 / Topology2 / Orientation3: Early endosome membrane1 / Multi-pass membrane protein2
Substrate chloride, bromide, iodide, superoxide

Cross database links:

RefSeq: NP_445815.2   
Entrez Gene ID: 84360   
Pfam: PF00571    PF00654   
KEGG: rno:84360   

Gene Ontology

GO:0016324 C:apical plasma membrane
GO:0031901 C:early endosome membrane
GO:0005794 C:Golgi apparatus
GO:0016021 C:integral to membrane
GO:0031902 C:late endosome membrane
GO:0030658 C:transport vesicle membrane
GO:0015297 F:antiporter activity
GO:0005524 F:ATP binding
GO:0030165 F:PDZ domain binding
GO:0005247 F:voltage-gated chloride channel activity
GO:0006821 P:chloride transport
GO:0055085 P:transmembrane transport

References (4)

[1] “Cloning and expression of a protein kinase C-regulated chloride channel abundantly expressed in rat brain neuronal cells.”  Kawasaki M.et.al.   8155321
[2] “Expression and canalicular localization of two isoforms of the ClC-3 chloride channel from rat hepatocytes.”  Shimada K.et.al.   10915634
[3] “Regulation of human CLC-3 channels by multifunctional Ca2+/calmodulin-dependent protein kinase.”  Huang P.et.al.   11274166
[4] “Intracellular localization of ClC chloride channels and their ability to form hetero-oligomers.”  Suzuki T.et.al.   16222710

External Searches:

Analyze:

Predict TMSs (Predict number of transmembrane segments)
Window Size: Angle:  
FASTA formatted sequence
1:	MESEQLFHRG YYRNSYNSIT SASSDEELLD GAGAIMDFQT SEDDNLLDGD TAAGTHYTMT 
61:	NGGSINSSTH LLDLLDEPIP GVGTYDDFHT IDWVREKCKD RERHRRINSK KKESAWEMTK 
121:	SLYDAWSGWL VVTLTGLASG ALAGLIDIAA DWMTDLKEGI CLSALWYNHE QCCWGSNETT 
181:	FEERDKCPQW KTWAELIIGQ AEGPGSYIMN YIMYIFWALS FAFLAVSLVK VFAPYACGSG 
241:	IPEIKTILSG FIIRGYLGKW TLMIKTITLV LAVASGLSLG KEGPLVHVAC CCGNIFSYLF 
301:	PKYSTNEAKK REVLSAASAA GVSVAFGAPI GGVLFSLEEV SYYFPLKTLW RSFFAALVAA 
361:	FVLRSINPFG NSRLVLFYVE YHTPWYLFEL FPFILLGVFG GLWGAFFIRA NIAWCRRRKS 
421:	TKFGKYPVLE VIIVAAITAV IAFPNPYTRL NTSELIKELF TDCGPLESSS LCDYRNDMNA 
481:	SKIVDDIPDR PAGVGVYSAI WQLCLALIFK IIMTVFTFGI KVPSGLFIPS MAIGAIAGRI 
541:	VGIAVEQLAY YHHDWFIFKE WCEVGADCIT PGLYAMVGAA ACLGGVTRMT VSLVVIVFEL 
601:	TGGLEYIVPL MAAVMTSKWV GDAFGREGIY EAHIRLNGYP FLDAKEEFTH TTLAADVMRP 
661:	RRSDPPLAVL TQDNMTVDDI ENMINETSYN GFPVIMSKES QRLVGFALRR DLTIAIESAR 
721:	KKQEGVVGSS RVCFAQHTPS LPAESPRPLK LRSILDMSPF TVTDHTPMEI VVDIFRKLGL 
781:	RQCLVTHNGR LLGIITKKDI LRHMAQTANQ DPASIMFN