CLCKB_RABIT
ID CLCKB_RABIT Reviewed; 678 AA.
AC P51804;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Chloride channel protein ClC-Kb;
DE Short=Chloride channel Kb;
DE AltName: Full=ClC-K2;
GN Name=CLCNKB;
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 -!- SUBCELLULAR LOCATION: Cell 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. CLCNKB
CC subfamily. {ECO:0000305}.
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DR EMBL; U36790; AAC48493.1; -; mRNA.
DR AlphaFoldDB; P51804; -.
DR SMR; P51804; -.
DR PRIDE; P51804; -.
DR InParanoid; P51804; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; 1.
PE 2: Evidence at transcript 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..678
FT /note="Chloride channel protein ClC-Kb"
FT /id="PRO_0000094461"
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..678
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P35523"
FT DOMAIN 551..612
FT /note="CBS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 620..678
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 364
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 678 AA; 74469 MW; 62816AB2877125F2 CRC64;
MEELVGLREG SSGNPVALRE LWSPCPRLRR 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
KGRAVVYVSW VERQHTGF
