CLCKB_RAT
ID CLCKB_RAT Reviewed; 687 AA.
AC P51802;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Chloride channel protein ClC-Kb;
DE Short=Chloride channel Kb;
DE AltName: Full=ClC-K2;
GN Name=Clcnkb;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
RX PubMed=8041726; DOI=10.1073/pnas.91.15.6943;
RA Kieferle S., Fong P., Bens M., Vandewalle A., Jentsch T.;
RT "Two highly homologous members of the ClC chloride channel family in both
RT rat and human kidney.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:6943-6947(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Kidney;
RX PubMed=8021279; DOI=10.1016/s0021-9258(17)32494-8;
RA Adachi S., Uchida S., Hata M., Hirose M., Marumo F., Sasaki S., Ito H.;
RT "Two isoforms of a chloride channel predominantly expressed in thick
RT ascending limb of Henle's loop and collecting ducts of rat kidney.";
RL J. Biol. Chem. 269:17677-17683(1994).
RN [3]
RP INTERACTION WITH BSND.
RX PubMed=12111250; DOI=10.1007/s00424-002-0819-8;
RA Waldegger S., Jeck N., Barth P., Peters M., Vitzthum H., Wolf K., Kurtz A.,
RA Konrad M., Seyberth H.W.;
RT "Barttin increases surface expression and changes current properties of
RT ClC-K channels.";
RL Pflugers Arch. 444:411-418(2002).
RN [4]
RP SUBUNIT, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=12761627; DOI=10.1007/s00418-003-0535-2;
RA Hayama A., Rai T., Sasaki S., Uchida S.;
RT "Molecular mechanisms of Bartter syndrome caused by mutations in the BSND
RT gene.";
RL Histochem. Cell Biol. 119:485-493(2003).
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.
CC -!- SUBUNIT: Interacts with BSND. {ECO:0000269|PubMed:12111250,
CC ECO:0000269|PubMed:12761627}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12761627};
CC Multi-pass membrane protein {ECO:0000269|PubMed:12761627}. Golgi
CC apparatus membrane {ECO:0000269|PubMed:12761627}; Multi-pass membrane
CC protein {ECO:0000269|PubMed:12761627}. Note=Recruited to the plasma
CC membrane in the presence of BSND protein, whereas remains in the Golgi
CC in its absence.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=ClC-K2L;
CC IsoId=P51802-1; Sequence=Displayed;
CC Name=2; Synonyms=ClC-K2S;
CC IsoId=P51802-2; Sequence=VSP_001049;
CC -!- TISSUE SPECIFICITY: Expressed predominantly in the kidney. Expressed in
CC all segments of the nephron examined, including the S2 segment and the
CC glomerulus.
CC -!- INDUCTION: Expression is consitently weaker in the absence of BSND
CC protein expression than it is in its presence. The half-life with BSND
CC protein is much longer than that without it. Rapidly degraded without
CC BSND protein, exhibiting a very short half-life of less than 1 hour.
CC {ECO:0000269|PubMed:12761627}.
CC -!- SIMILARITY: Belongs to the chloride channel (TC 2.A.49) family. CLCNKB
CC subfamily. {ECO:0000305}.
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DR EMBL; Z30663; CAA83143.1; -; mRNA.
DR EMBL; D26111; BAA05106.1; -; mRNA.
DR EMBL; D26111; BAA05107.1; -; mRNA.
DR PIR; B57713; B57713.
DR RefSeq; NP_775126.1; NM_173103.1. [P51802-1]
DR AlphaFoldDB; P51802; -.
DR SMR; P51802; -.
DR STRING; 10116.ENSRNOP00000013550; -.
DR TCDB; 2.A.49.2.5; the chloride carrier/channel (clc) family.
DR GlyGen; P51802; 1 site.
DR PhosphoSitePlus; P51802; -.
DR jPOST; P51802; -.
DR PaxDb; P51802; -.
DR GeneID; 79430; -.
DR KEGG; rno:79430; -.
DR UCSC; RGD:628639; rat. [P51802-1]
DR CTD; 1188; -.
DR RGD; 628639; Clcnkb.
DR eggNOG; KOG0476; Eukaryota.
DR InParanoid; P51802; -.
DR OrthoDB; 271925at2759; -.
DR PhylomeDB; P51802; -.
DR Reactome; R-RNO-2672351; Stimuli-sensing channels.
DR PRO; PR:P51802; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005254; F:chloride channel activity; IDA:RGD.
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; IDA:RGD.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0070293; P:renal absorption; TAS:UniProtKB.
DR GO; GO:0070294; P:renal sodium ion absorption; ISO:RGD.
DR GO; GO:0030321; P:transepithelial chloride transport; TAS:UniProtKB.
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 Alternative splicing; Calcium; CBS domain; Cell membrane; Chloride;
KW Chloride channel; Glycoprotein; Golgi apparatus; 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-Kb"
FT /id="PRO_0000094462"
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 CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 77..131
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8021279"
FT /id="VSP_001049"
SQ SEQUENCE 687 AA; 75218 MW; 35B0BD7735397880 CRC64;
MEEIVGLREG SPRKPVPLQE LWRPCPRIRR NIQGSLEWLK ERLFRVGEDW YFLVALGVLM
ALISYAMNFA IGRVVRAHKW LYREIGDGHL LRYLSWTVYP VALLSFSSGF SQSITPSSGG
SGIPEVKTIL TGVILEDYLD IKNFGAKVVG LSCTLATGST IFLGKLGPFV HLSVMIAAYL
GRVRTKTVGE PENKTKEMEL LAAGAAVGVA TVFAAPISGV LFSIEVMSSH FSVWDYWRGF
FAATCGAFMF HLLAVFNSEQ ETITSIYKTS FPVDIPFDLP EIFFFVALGA ICGILSCGYN
YCQRTSLFFL KSNGFTSKLL ATSKPLYSAL AAVVLASITY PPGVGRFMAS RLSMSEYLET
LFDNNSWALM TKNSSPPWSA EPDPQNLWLE WCHPQMTVFG TLVFFLVMKF WMLILATTIP
IPAGYFLPIF VYGAAIGRLF GEVLSLAFPE GIVAGGKVSP IMPGAYALAG AAAFSGAVTH
TLSTALLAFE VSGQIVHALP VLMAVLAANA ICQSYQPSFY DGTIIVKKLP YLPWIRGRKI
GSHLVTVGHF MNCTLTTLAK DMPLEEVIKV VISTDVTQYP LVETTESQVL VGIVKRTHLV
QSLHTDSASW APGQQPCLQD ILANGCPTQP VTLQLSTETS LHETHNLFEL LNLQLLFVTS
RGRAVGSVSW VELKKAISTL TNPPAPK
