CLCKB_MOUSE
ID CLCKB_MOUSE Reviewed; 687 AA.
AC Q9WUB6; A2ADB6; Q8VCF8;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Chloride channel protein ClC-Kb;
DE Short=Chloride channel Kb;
DE AltName: Full=ClC-K2;
GN Name=Clcnkb; Synonyms=Clckb, Clcnk1l;
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] (ISOFORM 1), POSSIBLE FUNCTION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Kidney outer medulla;
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 [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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=FVB/N; TISSUE=Salivary gland;
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).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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: Interacts with BSND. Forms heteromers with BSND in the thick
CC ascending limb of Henle and more distal segments.
CC {ECO:0000269|PubMed:11734858}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11734858};
CC Multi-pass membrane protein {ECO:0000269|PubMed:11734858}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9WUB6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9WUB6-2; Sequence=VSP_011757, VSP_011758;
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 -!- MISCELLANEOUS: [Isoform 2]: Due to intron retention. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the chloride channel (TC 2.A.49) family. CLCNKB
CC subfamily. {ECO:0000305}.
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DR EMBL; AF124847; AAD21082.1; -; mRNA.
DR EMBL; AL670285; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466615; EDL13372.1; -; Genomic_DNA.
DR EMBL; BC019983; AAH19983.1; -; mRNA.
DR CCDS; CCDS18872.1; -. [Q9WUB6-1]
DR RefSeq; NP_062675.2; NM_019701.2. [Q9WUB6-1]
DR RefSeq; XP_011248609.1; XM_011250307.1. [Q9WUB6-1]
DR AlphaFoldDB; Q9WUB6; -.
DR SMR; Q9WUB6; -.
DR STRING; 10090.ENSMUSP00000006378; -.
DR iPTMnet; Q9WUB6; -.
DR PhosphoSitePlus; Q9WUB6; -.
DR PaxDb; Q9WUB6; -.
DR PRIDE; Q9WUB6; -.
DR ProteomicsDB; 283572; -. [Q9WUB6-1]
DR ProteomicsDB; 283573; -. [Q9WUB6-2]
DR DNASU; 56365; -.
DR Ensembl; ENSMUST00000006378; ENSMUSP00000006378; ENSMUSG00000006216. [Q9WUB6-1]
DR Ensembl; ENSMUST00000105788; ENSMUSP00000101414; ENSMUSG00000006216. [Q9WUB6-2]
DR GeneID; 56365; -.
DR KEGG; mmu:56365; -.
DR UCSC; uc008voh.2; mouse. [Q9WUB6-1]
DR UCSC; uc008voi.2; mouse. [Q9WUB6-2]
DR CTD; 1188; -.
DR MGI; MGI:1930643; Clcnkb.
DR VEuPathDB; HostDB:ENSMUSG00000006216; -.
DR eggNOG; KOG0476; Eukaryota.
DR GeneTree; ENSGT00940000158748; -.
DR HOGENOM; CLU_006904_4_0_1; -.
DR InParanoid; Q9WUB6; -.
DR OMA; NYWRAFV; -.
DR OrthoDB; 271925at2759; -.
DR PhylomeDB; Q9WUB6; -.
DR TreeFam; TF300522; -.
DR Reactome; R-MMU-2672351; Stimuli-sensing channels.
DR BioGRID-ORCS; 56365; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Clcnkb; mouse.
DR PRO; PR:Q9WUB6; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9WUB6; protein.
DR Bgee; ENSMUSG00000006216; Expressed in right kidney and 41 other tissues.
DR ExpressionAtlas; Q9WUB6; baseline and differential.
DR Genevisible; Q9WUB6; MM.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005254; F:chloride channel activity; 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:0006821; P:chloride transport; ISO:MGI.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0070294; P:renal sodium ion absorption; ISO: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 SUPFAM; SSF54631; SSF54631; 1.
DR SUPFAM; SSF81340; SSF81340; 1.
DR PROSITE; PS51371; CBS; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; CBS domain; Cell membrane; Chloride;
KW Chloride channel; Ion channel; Ion transport; Membrane; Metal-binding;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport;
KW Voltage-gated channel.
FT CHAIN 1..687
FT /note="Chloride channel protein ClC-Kb"
FT /id="PRO_0000094460"
FT TOPO_DOM 1..50
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P35523"
FT TRANSMEM 51..82
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P35523"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P35523"
FT INTRAMEM 116..127
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P35523"
FT TRANSMEM 141..160
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P35523"
FT TRANSMEM 161..180
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P35523"
FT INTRAMEM 203..224
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P35523"
FT TRANSMEM 236..255
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P35523"
FT TRANSMEM 282..310
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P35523"
FT TRANSMEM 325..342
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P35523"
FT INTRAMEM 349..360
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P35523"
FT TRANSMEM 400..420
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P35523"
FT TRANSMEM 421..440
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P35523"
FT INTRAMEM 464..496
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P35523"
FT TRANSMEM 500..520
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P35523"
FT TOPO_DOM 521..687
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P35523"
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 121
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250|UniProtKB:P37019"
FT BINDING 259
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 261
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 278
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 281
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 426
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250|UniProtKB:P37019"
FT VAR_SEQ 673..676
FT /note="LKKA -> VLGS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011757"
FT VAR_SEQ 677..687
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011758"
FT CONFLICT 92
FT /note="R -> L (in Ref. 1; AAD21082 and 4; AAH19983)"
FT /evidence="ECO:0000305"
FT CONFLICT 431
FT /note="I -> V (in Ref. 1; AAD21082 and 4; AAH19983)"
FT /evidence="ECO:0000305"
FT CONFLICT 554
FT /note="A -> T (in Ref. 1; AAD21082 and 4; AAH19983)"
FT /evidence="ECO:0000305"
FT CONFLICT 571
FT /note="V -> M (in Ref. 1; AAD21082 and 4; AAH19983)"
FT /evidence="ECO:0000305"
FT CONFLICT 617
FT /note="C -> Y (in Ref. 4; AAH19983)"
FT /evidence="ECO:0000305"
FT CONFLICT 637
FT /note="L -> P (in Ref. 1; AAD21082 and 4; AAH19983)"
FT /evidence="ECO:0000305"
FT CONFLICT 667
FT /note="S -> F (in Ref. 1; AAD21082 and 4; AAH19983)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 687 AA; 75009 MW; BEF5A605DB3A3025 CRC64;
MEELVGLREG ASKKPVPLQE LWGPCPRIRR NIQGGLEWLK ERLFRVGEDW YFLVALGVLM
ALISYAMNFT IGRVVRAHKW LYREIGDGHL LRYLSWTVYP VALLSFSSGF SQSITPSSGG
SGIPEVKTIL TGVVLEDYLD IKNFGAKVVG LSCTLATGST IFLGKLGPFV HLSVMIAAYL
GRVRTKTVGE PESKTKEMEL LAAGAAVGVA TVFAAPISGV LFSIEVMSSH FSVWDYWRGF
FAATCGAFMF HLLAVFNNEQ ETITSIYKTS FPVDIPFDLP EIFFFVALGA ICGILSCGYN
YSQRTFLFFL KANGFTSKLL ATSKPLYSAL AAVVLASITY PPGVGHFMAS RLSMSEHLET
LFDNNSWALM TKNSSPPWAA EPDPQKLWLE WCHPQLTVFG TLVFFLVMKF WMLILATTIP
IPAGYFLPIF IYGAVIGRLF GEVLSVAFPE GIVAGGRVNP IMPGAYALAG AAAFSGAVTH
TLSTALLAFE VTGQLVHALP VLMAVLAANA ISQSFQPSFY DGTIIVKKLP YLPWIRGRQI
GSHSVTVGHF MNCALTTLAK DMPLEQVIQV VISTDVTQYP LVETTESQTL VGVVKRTHLV
QALQTEPASW APGQQPCLQD ILANGCPTQP VTLQLSLETS LHETHNLFEL LNLQTLFVTS
RGRAVGSVSW VELKKAISTL TNPPAPK
