CLCKA_MOUSE
ID CLCKA_MOUSE Reviewed; 687 AA.
AC Q9WUB7; A2ADB3; Q6UB69; Q8JZU7;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Chloride channel protein ClC-Ka;
DE Short=Chloride channel Ka;
DE AltName: Full=ClC-K1;
GN Name=Clcnka; Synonyms=Clcnk1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], POSSIBLE FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Kidney cortex;
RX PubMed=11014860; DOI=10.1007/s002320010005;
RA Winters C.J., Zimniak L., Mikhailova M.V., Reeves W.B., Andreoli T.E.;
RT "Cl(-) channels in basolateral TAL membranes XV. Molecular heterogeneity
RT between cortical and medullary channels.";
RL J. Membr. Biol. 177:221-230(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cochlea;
RA Nie L., Vazquez A.E., Feng W., Stice J.P., Yamoah E.N.;
RT "Functional phenotype of inner ear-specific chloride channel ClC-K and its
RT accessory subunit.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP INTERACTION WITH BSND, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11734858; DOI=10.1038/35107099;
RA Estevez R., Boettger T., Stein V., Birkenhaeger R., Otto E.,
RA Hildebrandt F., Jentsch T.J.;
RT "Barttin is a Cl- channel beta-subunit crucial for renal Cl-reabsorption
RT and inner ear K+ secretion.";
RL Nature 414:558-561(2001).
CC -!- FUNCTION: Voltage-gated chloride channel. Chloride channels have
CC several functions including the regulation of cell volume; membrane
CC potential stabilization, signal transduction and transepithelial
CC transport. May be important in urinary concentrating mechanisms. May be
CC the basolateral chloride channel mediating net chloride absorption in
CC CTAL cells.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with BSND. Forms
CC heteromers with BSND in the thin ascending limb of Henle. {ECO:0000250,
CC ECO:0000269|PubMed:11734858}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:11734858}; Multi-
CC pass membrane protein {ECO:0000269|PubMed:11734858}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in the kidney. All nephron
CC segments expressing BSND also express CLCNK proreins.
CC {ECO:0000269|PubMed:11014860, ECO:0000269|PubMed:11734858}.
CC -!- SIMILARITY: Belongs to the chloride channel (TC 2.A.49) family. CLCNKA
CC subfamily. {ECO:0000305}.
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DR EMBL; AF124848; AAD21083.1; -; mRNA.
DR EMBL; AY373832; AAQ81628.1; -; mRNA.
DR EMBL; AL670285; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC037077; AAH37077.1; -; mRNA.
DR CCDS; CCDS18871.1; -.
DR RefSeq; NP_001139779.1; NM_001146307.1.
DR RefSeq; NP_077723.3; NM_024412.3.
DR AlphaFoldDB; Q9WUB7; -.
DR SMR; Q9WUB7; -.
DR STRING; 10090.ENSMUSP00000101416; -.
DR PhosphoSitePlus; Q9WUB7; -.
DR PaxDb; Q9WUB7; -.
DR PRIDE; Q9WUB7; -.
DR ProteomicsDB; 285477; -.
DR DNASU; 12733; -.
DR Ensembl; ENSMUST00000042617; ENSMUSP00000048520; ENSMUSG00000033770.
DR Ensembl; ENSMUST00000105790; ENSMUSP00000101416; ENSMUSG00000033770.
DR GeneID; 12733; -.
DR KEGG; mmu:12733; -.
DR UCSC; uc008voe.2; mouse.
DR CTD; 1187; -.
DR MGI; MGI:1329026; Clcnka.
DR VEuPathDB; HostDB:ENSMUSG00000033770; -.
DR eggNOG; KOG0476; Eukaryota.
DR GeneTree; ENSGT00940000158748; -.
DR HOGENOM; CLU_006904_4_0_1; -.
DR InParanoid; Q9WUB7; -.
DR OMA; YWRAFFS; -.
DR OrthoDB; 271925at2759; -.
DR PhylomeDB; Q9WUB7; -.
DR TreeFam; TF300522; -.
DR Reactome; R-MMU-2672351; Stimuli-sensing channels.
DR BioGRID-ORCS; 12733; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Clcnka; mouse.
DR PRO; PR:Q9WUB7; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9WUB7; protein.
DR Bgee; ENSMUSG00000033770; Expressed in right kidney and 43 other tissues.
DR ExpressionAtlas; Q9WUB7; baseline and differential.
DR Genevisible; Q9WUB7; MM.
DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
DR GO; GO:0005254; F:chloride channel activity; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005247; F:voltage-gated chloride channel activity; IBA:GO_Central.
DR GO; GO:0005244; F:voltage-gated ion channel activity; ISO:MGI.
DR GO; GO:0006821; P:chloride transport; IBA:GO_Central.
DR GO; GO:0050878; P:regulation of body fluid levels; IMP:MGI.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0072053; P:renal inner medulla development; IMP:MGI.
DR Gene3D; 3.10.580.10; -; 1.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR014743; Cl-channel_core.
DR InterPro; IPR001807; Cl-channel_volt-gated.
DR InterPro; IPR002250; Cl_channel-K.
DR Pfam; PF00571; CBS; 1.
DR Pfam; PF00654; Voltage_CLC; 1.
DR PRINTS; PR00762; CLCHANNEL.
DR PRINTS; PR01119; CLCHANNELKDY.
DR SMART; SM00116; CBS; 1.
DR SUPFAM; SSF54631; SSF54631; 1.
DR SUPFAM; SSF81340; SSF81340; 1.
DR PROSITE; PS51371; CBS; 2.
PE 1: Evidence at protein level;
KW Calcium; CBS domain; Chloride; Chloride channel; Ion channel;
KW Ion transport; Membrane; Metal-binding; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..687
FT /note="Chloride channel protein ClC-Ka"
FT /id="PRO_0000094456"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..224
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 282..302
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 325..345
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 396..416
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 417..437
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 458..478
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 486..506
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 507..687
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 551..609
FT /note="CBS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 626..687
FT /note="CBS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT BINDING 259
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P51800"
FT BINDING 261
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P51800"
FT BINDING 278
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P51800"
FT BINDING 281
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P51800"
FT CONFLICT 372
FT /note="R -> W (in Ref. 4; AAH37077)"
FT /evidence="ECO:0000305"
FT CONFLICT 380
FT /note="S -> A (in Ref. 1; AAD21083 and 4; AAH37077)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 687 AA; 75684 MW; A04ADFFC220224FA CRC64;
MEELVGLREG SSGKPVTLQE LWGPCPRIRR GIRGGLEWLK ERLFRAREDW YFLVALGVLM
ALISYAMNFA IGRVVRAHKW LYREVGDGHL LRYLSWTVYP VALLSFSSGF SQSITPFSGG
SGLPELKTML SGVVLENYLD IKNFGAKVVG LSCTLATGST IFLGKVGPFV HLSVMISAYL
GRVRAKAVGD TESKAKEVEM LSAAAAVGVA TVFAAPFSGV LFSIEVMSSH FSVWNYWRGF
FAATCGAFMF RLLAVFNSEQ ETITSIYKTR FRVDVPFDLP EIFFFVALGF ICGILSCVYL
FCQRNFLRFI KTNRYTSKLL ATSKPSYAAL VALVLASVTY PPGVGRFMAS RLSMAEHLHS
LFDNNSWALM TRNASPPWPS EPDPQNLWFE WYHPRFTIFG TLAFFLIMKF WMLILATTIP
MPAGYFMPIF IIGAAIGRLL GEALSVAFPE GIVAGGEVYP IMPGGYALAG AAAFSGAVTH
TISTALLAFE LTGQIVHALP VLMAVLAANV ISQNLQPSFY DGTIMAKKLP YLPWIRGRQI
GSYPVTVEHF MNSNLTTLAK DMPLEEVVKV VTSTDVSQYP LVETRESQTL VGIVERTHLV
QALQTQPASW APGQERFLQD ILAGGCPTQP VTLQLSPETS LYQAHRLFEL LTLQALFVTS
RGRAVGSVSW VELKKAISTL INPPAPK
