CLCKA_RABIT
ID CLCKA_RABIT Reviewed; 687 AA.
AC P51803;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Chloride channel protein ClC-Ka;
DE Short=Chloride channel Ka;
DE AltName: Full=ClC-K1;
GN Name=CLCNKA;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RX PubMed=8587242; DOI=10.1038/ki.1995.481;
RA Zimniak L., Winters C.J., Reeves W.B., Andreoli T.E.;
RT "Cl- channels in basolateral renal medullary vesicles. X. Cloning of a
RT Cl- channel from rabbit outer medulla.";
RL Kidney Int. 48:1828-1836(1995).
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: Homodimer. Interacts with BSND. Forms heteromers with BSND in
CC the thin ascending limb of Henle (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in the kidney.
CC -!- SIMILARITY: Belongs to the chloride channel (TC 2.A.49) family. CLCNKA
CC subfamily. {ECO:0000305}.
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DR EMBL; U36789; AAC48492.1; -; mRNA.
DR RefSeq; NP_001075830.1; NM_001082361.1.
DR AlphaFoldDB; P51803; -.
DR SMR; P51803; -.
DR STRING; 9986.ENSOCUP00000003674; -.
DR PRIDE; P51803; -.
DR GeneID; 100009213; -.
DR KEGG; ocu:100009213; -.
DR CTD; 1187; -.
DR eggNOG; KOG0476; Eukaryota.
DR InParanoid; P51803; -.
DR OrthoDB; 271925at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
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: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 SUPFAM; SSF54631; SSF54631; 1.
DR SUPFAM; SSF81340; SSF81340; 1.
DR PROSITE; PS51371; CBS; 2.
PE 2: Evidence at transcript 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_0000094457"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..222
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 452..472
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..612
FT /note="CBS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 628..686
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"
SQ SEQUENCE 687 AA; 75202 MW; B4BDB7A43078E28E CRC64;
MEELVGLREG SSGNPVALRE LWGPCPRLRR GIRGGLEWLK QKLFRVGEDW YFLMTLGVLM
ALISYAMNFA LGRVVRAHKW LYREIGDSHL LRYLSWTVYP VALVSFSSGF SQSITPFSGG
SGIPELKTIL SGVVLENYLD IKNFGAKVVG LSCTLATGST LFLGKVGPFV HLSVMIAAYL
GRVRTKTIGE AENKSKQNEM LVAGAAVGVA TVFAAPFSGV LFCIEVMSSH FSVWDYWRGF
FAATCGAFMF RLLAVFNSEQ ETITSLYKTS FPVDVPFDLP EIFFFVLLGA ICGVASCAYL
YCQRTFLAFT KTNKLISKLM ATSKPLYAAL AATVLASITY PPGVGRFMAS RLSMREHLDT
LFDNHSWALL TRNSSPPWPA EPDPQHLWWE WYHPRFTIFG TLAFFLVMKF WMLILATTIP
MPAGYFLPIF IIGAAIGRLL GEALSVAFPE GIVAGGVINP IMPGGYALAG AAAFSGAVTH
SISTALLAFE LTGQIVHALP VLMAVLAANA IAQSCQPSFY DGTIMVKKLP YLPWIRGRPI
NSHRVIVEHF MRRAISTLAR DAALEQVVKV LTSTDEAEYP LVESTESQLL VGIVQRAQLV
QALQAEAPAR ASGQQRCLQD ILAGGCPTEP VTLTLSPETS LHQAHNLFEL LNLRSLYVTS
KGRAVGYVSW VELEKAISAL TNPPPAK
