CLCKB_XENLA
ID CLCKB_XENLA Reviewed; 689 AA.
AC Q9W701;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Chloride channel protein ClC-Kb {ECO:0000250|UniProtKB:P51801};
DE Short=Chloride channel Kb {ECO:0000250|UniProtKB:P51801};
DE AltName: Full=x6clck;
DE AltName: Full=xCIC-K;
GN Name=clcnkb;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAB51058.1}
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP GLYCOSYLATION.
RC TISSUE=Oocyte {ECO:0000269|PubMed:10359659};
RX PubMed=10359659; DOI=10.1042/bj3400737;
RA Maulet Y., Lambert R.C., Mykita S., Mouton J., Partisani M., Bailly Y.,
RA Bombarde G., Feltz A.;
RT "Expression and targeting to the plasma membrane of xClC-K, a chloride
RT channel specifically expressed in distinct tubule segments of Xenopus
RT laevis kidney.";
RL Biochem. J. 340:737-743(1999).
CC -!- FUNCTION: Voltage-gated chloride channel. Chloride channels have
CC several functions including the regulation of cell volume, the
CC stabilization of membrane potential, signal transduction and
CC transepithelial transport.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10359659};
CC Multi-pass membrane protein {ECO:0000255, ECO:0000269|PubMed:10359659}.
CC -!- TISSUE SPECIFICITY: Expressed in two distinct regions of the kidney;
CC the proximal convoluted tubule and the diluting segment.
CC {ECO:0000269|PubMed:10359659}.
CC -!- PTM: N-glycosylated on a single asparagine, probably Asn-365 or Asn-
CC 375. {ECO:0000269|PubMed:10359659}.
CC -!- SIMILARITY: Belongs to the chloride channel (TC 2.A.49) family.
CC {ECO:0000255}.
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DR EMBL; AJ011385; CAB51058.1; -; mRNA.
DR RefSeq; NP_001079308.1; NM_001085839.1.
DR AlphaFoldDB; Q9W701; -.
DR SMR; Q9W701; -.
DR DNASU; 378616; -.
DR GeneID; 378616; -.
DR KEGG; xla:378616; -.
DR CTD; 378616; -.
DR Xenbase; XB-GENE-6252397; clcnkb.L.
DR OrthoDB; 271925at2759; -.
DR Proteomes; UP000186698; Chromosome 7L.
DR Bgee; 378616; Expressed in kidney and 9 other tissues.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005254; F:chloride channel activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005247; F:voltage-gated chloride channel activity; IEA:InterPro.
DR GO; GO:0006821; P:chloride transport; ISS:UniProtKB.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
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; 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; Cell membrane; Chloride; Chloride channel;
KW Glycoprotein; Ion channel; Ion transport; Membrane; Metal-binding;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport;
KW Voltage-gated channel.
FT CHAIN 1..689
FT /note="Chloride channel protein ClC-Kb"
FT /id="PRO_0000391463"
FT TOPO_DOM 1..51
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P35523"
FT TRANSMEM 52..83
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P35523"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P35523"
FT INTRAMEM 117..128
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P35523"
FT TRANSMEM 142..161
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P35523"
FT TRANSMEM 162..181
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P35523"
FT INTRAMEM 204..225
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P35523"
FT TRANSMEM 237..256
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P35523"
FT TRANSMEM 283..311
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P35523"
FT TRANSMEM 326..343
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P35523"
FT INTRAMEM 350..361
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P35523"
FT TRANSMEM 402..422
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P35523"
FT TRANSMEM 423..442
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P35523"
FT INTRAMEM 466..498
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P35523"
FT TRANSMEM 502..522
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P35523"
FT TOPO_DOM 523..689
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P35523"
FT DOMAIN 553..613
FT /note="CBS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 630..689
FT /note="CBS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT BINDING 122
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250|UniProtKB:P37019"
FT BINDING 260
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 262
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 279
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 282
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 428
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250|UniProtKB:P37019"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 689 AA; 76800 MW; 4C0E95DDF4DC495F CRC64;
MSRVLVIEQR EGEEKTLIQK HIFRPFPNTR RVVIDHLQRL KNFLFRIGDD WYFLFALGVI
MALISFTMDF TVSKMLNAHR WLQQELGGNV LLRYLSWIVY PIALVAFSTG FAQSITPHSG
GSGIPELKTI LSGVILEEYL TIKNFGAKVV GLTCTLSAGS TMFLGKVGPF VHLSSMIAAY
LGRMRTSVAG DYENKSKEHE MLVAAAAVGV STVFGAPISG VLFSVEVMSS HFAIRNYWRG
FFAATCGAFV FRLLAVFNSE QETITAVFKT SFKISFPFDL PEMFFFAILG VVCGLIGCAY
LFCQRWLLGY VRRNSLTSKL LASDKPMYSA LVALLISSIT FPESLGQFLA SRLTMKELLT
SLFDNRTWWI SLSQNSSLDR SPLVDPNNLW LEWANPQFTI FGTLAFFIIM KFWMFILATT
LPMPAGYFMP VFVFGAAIGR LVGETVALLY PEGIAADGIV NPIIPGGYAW QGAPAYSGAV
THSVSTALLA FEATGQIAHI LPVILCVLIA NAFTQKLQPS FYDGTIIVKK LPYLPRIRSR
DIDSYKVNTE EFMNPDIRVL PREAGFEDVL KVITASDDSE YPVVDNTESQ VLVGTVKRPQ
LIHFLETHES HERAGPTEKE NLSEGNLGEA CSIEPVTFQL STWTSLHQAH HLFELLHLQK
AFVTKYGRIV GQVTRKEMKK AIEDLANPK
