CLCN2_RABIT
ID CLCN2_RABIT Reviewed; 898 AA.
AC P51789;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Chloride channel protein 2;
DE Short=ClC-2;
DE AltName: Full=PKA-activated chloride channel;
GN Name=CLCN2;
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 STRAIN=New Zealand white; TISSUE=Gastric mucosa;
RX PubMed=7840147; DOI=10.1152/ajpcell.1995.268.1.c191;
RA Malinowska D.H., Kupert E.Y., Bahinski A., Sherry A.M., Cuppoletti J.;
RT "Cloning, functional expression, and characterization of a PKA-activated
RT gastric Cl-channel.";
RL Am. J. Physiol. 268:C191-C200(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 (By similarity). Involved in the regulation of aldosterone
CC production. The opening of CLCN2 channels at hyperpolarized membrane
CC potentials in the glomerulosa causes cell membrane depolarization,
CC activation of voltage-gated Ca2+ channels and increased expression of
CC aldosterone synthase, the rate-limiting enzyme for aldosterone
CC biosynthesis (By similarity). {ECO:0000250|UniProtKB:P35525,
CC ECO:0000250|UniProtKB:P51788}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P35525};
CC Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC -!- PTM: Phosphorylated. Activated by dephosphorylation.
CC {ECO:0000250|UniProtKB:P35525}.
CC -!- MISCELLANEOUS: The CLC channel family contains both chloride channels
CC and proton-coupled anion transporters that exchange chloride or another
CC anion for protons. The absence of conserved gating glutamate residues
CC is typical for family members that function as channels (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the chloride channel (TC 2.A.49) family. ClC-
CC 2/CLCN2 subfamily. {ECO:0000305}.
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DR EMBL; U15652; AAB05937.1; -; mRNA.
DR RefSeq; NP_001076220.1; NM_001082751.1.
DR AlphaFoldDB; P51789; -.
DR SMR; P51789; -.
DR STRING; 9986.ENSOCUP00000006115; -.
DR PRIDE; P51789; -.
DR Ensembl; ENSOCUT00000007070; ENSOCUP00000006115; ENSOCUG00000007065.
DR GeneID; 100009530; -.
DR KEGG; ocu:100009530; -.
DR CTD; 1181; -.
DR eggNOG; KOG0476; Eukaryota.
DR GeneTree; ENSGT00940000155439; -.
DR HOGENOM; CLU_006904_0_1_1; -.
DR InParanoid; P51789; -.
DR OMA; ACFMFNN; -.
DR OrthoDB; 1131873at2759; -.
DR Proteomes; UP000001811; Chromosome 14.
DR Bgee; ENSOCUG00000007065; Expressed in testis and 18 other tissues.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005247; F:voltage-gated chloride channel activity; ISS:UniProtKB.
DR GO; GO:0090425; P:acinar cell differentiation; IEA:Ensembl.
DR GO; GO:0060689; P:cell differentiation involved in salivary gland development; IEA:Ensembl.
DR GO; GO:0032347; P:regulation of aldosterone biosynthetic process; ISS:UniProtKB.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl.
DR Gene3D; 3.10.580.10; -; 2.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR002244; Cl-channel-2.
DR InterPro; IPR014743; Cl-channel_core.
DR InterPro; IPR001807; Cl-channel_volt-gated.
DR Pfam; PF00654; Voltage_CLC; 1.
DR PRINTS; PR00762; CLCHANNEL.
DR PRINTS; PR01113; CLCHANNEL2.
DR SUPFAM; SSF54631; SSF54631; 1.
DR SUPFAM; SSF81340; SSF81340; 1.
DR PROSITE; PS51371; CBS; 2.
PE 2: Evidence at transcript level;
KW CBS domain; Cell membrane; Chloride; Chloride channel; Ion channel;
KW Ion transport; Membrane; Phosphoprotein; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..898
FT /note="Chloride channel protein 2"
FT /id="PRO_0000094435"
FT TOPO_DOM 1..90
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 91..124
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 133..158
FT /note="Helical"
FT /evidence="ECO:0000250"
FT INTRAMEM 167..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..201
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 208..226
FT /note="Helical"
FT /evidence="ECO:0000250"
FT INTRAMEM 242..254
FT /note="Helical"
FT /evidence="ECO:0000250"
FT INTRAMEM 258..266
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 324..352
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 361..380
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 432..452
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 460..483
FT /note="Helical"
FT /evidence="ECO:0000250"
FT INTRAMEM 500..514
FT /note="Helical"
FT /evidence="ECO:0000250"
FT INTRAMEM 515..516
FT /note="Note=Loop between two helices"
FT /evidence="ECO:0000250"
FT INTRAMEM 517..528
FT /note="Helical"
FT /evidence="ECO:0000250"
FT INTRAMEM 529..533
FT /note="Note=Loop between two helices"
FT /evidence="ECO:0000250"
FT TRANSMEM 534..551
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 552..898
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT DOMAIN 587..645
FT /note="CBS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 790..850
FT /note="CBS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT REGION 647..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 726..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 856..898
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 164..168
FT /note="Selectivity filter part_1"
FT /evidence="ECO:0000250"
FT MOTIF 206..210
FT /note="Selectivity filter part_2"
FT /evidence="ECO:0000250"
FT MOTIF 460..464
FT /note="Selectivity filter part_3"
FT /evidence="ECO:0000250"
FT COMPBIAS 657..675
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..758
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 857..871
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 23
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9R0A1"
FT MOD_RES 710
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51788"
FT MOD_RES 758
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35525"
SQ SEQUENCE 898 AA; 98547 MW; 0F84B41123395D33 CRC64;
MAAPAAAAVE EGMEPRALQY EQTLMYGRYT QDLGAFAKEE AARIRLGGPE PWRSPPSPRT
PPELLEYGQS RCARCRMCSV RCHKFLVSRV GEDWIFLVLL GLLMALVSWA MDYAIAACLQ
AQQWMSRGLN TNLLLQYLAW VTYPVVLITF SAGFTQILAP QAVGSGIPEM KTILRGVVLK
EYLTLKTFVA KVIGLTCALG SGMPLGKEGP FVHIASMCAA LLSKFLSLFG GIYENESRNT
EMLAAACAVG VGCCFAAPIG GVLFSIEVTS TFFAVRNYWR GFFAATFSAF IFRVLAVWNR
DEETITALFK TRFRLDFPFD LQELPAFAVI GIASGFGGAL FVYLNRKIVQ VMRKQKTINR
FLMRKRLLFP ALVTLLISTL TFPPGFGQFM AGQLSQKETL VTLFDNRTWV RQGLVEELEP
PSTSQAWSPP RANVFLTLVI FILMKFWMSA LATTIPVPCG AFMPVFVIGA AFGRLVGESM
AAWFPDGIHT DSSTYRIVPG GYAVVGAAAL AGAVTHTVST AVIVFELTGQ IAHILPVMIA
VILANAVAQS LQPSLYDSII RIKKLPYLPE LGWGRHQQYR VRVEDIMVRD VPHVALSCTF
RDLRLALHRT KGRTLALVES PESMILLGSI ERTQVVALLA AQLSPARRRQ SKQKRRVAHT
SPPSCQESPP SPETSVCFQV KAEDAQGEPH KPLKPALKRG CSNSVNLGES PTGHVESAGI
ALRSLFCGSP PPEAASESEK SESSEKRKSK RVRISLASDS DLEGEMSPEE ILEWEEQQLD
EPVNFSDCKI DPAPFQLVER TSLHKTHTIF SLLGVDHAYV TSIGRLIGIV TLKELRKAIE
GSVTAQGVKV RPPLASFRDS ATSSSDTETT EVHALWGPRS RHGLPREGSP SDSDDKCQ
