CLCN2_CAVPO
ID CLCN2_CAVPO Reviewed; 902 AA.
AC Q9WU45; Q9R247; Q9R248; Q9WU46;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Chloride channel protein 2;
DE Short=ClC-2;
GN Name=CLCN2;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND ALTERNATIVE SPLICING.
RC TISSUE=Small intestine;
RX PubMed=11003600; DOI=10.1152/ajpcell.2000.279.4.c1198;
RA Cid L.P., Niemeyer M.I., Ramirez A., Sepulveda F.V.;
RT "Splice variants of a ClC-2 chloride channel with differing functional
RT characteristics.";
RL Am. J. Physiol. 279:C1198-C1210(2000).
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 {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9WU45-1; Sequence=Displayed;
CC Name=2; Synonyms=Delta77-86;
CC IsoId=Q9WU45-2; Sequence=VSP_001041, VSP_001042;
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; AF113528; AAD37111.1; -; Genomic_DNA.
DR EMBL; AF113528; AAD37112.1; -; Genomic_DNA.
DR EMBL; AF113529; AAD37113.1; -; mRNA.
DR EMBL; AF113530; AAD37114.1; -; mRNA.
DR AlphaFoldDB; Q9WU45; -.
DR SMR; Q9WU45; -.
DR STRING; 10141.ENSCPOP00000008261; -.
DR eggNOG; KOG0476; Eukaryota.
DR InParanoid; Q9WU45; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
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:0032347; P:regulation of aldosterone biosynthetic process; ISS:UniProtKB.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
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 Alternative splicing; CBS domain; Cell membrane; Chloride;
KW Chloride channel; Ion channel; Ion transport; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport;
KW Voltage-gated channel.
FT CHAIN 1..902
FT /note="Chloride channel protein 2"
FT /id="PRO_0000094432"
FT TOPO_DOM 1..89
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 90..123
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 132..157
FT /note="Helical"
FT /evidence="ECO:0000250"
FT INTRAMEM 166..173
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 182..200
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 207..225
FT /note="Helical"
FT /evidence="ECO:0000250"
FT INTRAMEM 241..253
FT /note="Helical"
FT /evidence="ECO:0000250"
FT INTRAMEM 257..265
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 323..351
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 360..379
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 431..451
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 459..482
FT /note="Helical"
FT /evidence="ECO:0000250"
FT INTRAMEM 499..513
FT /note="Helical"
FT /evidence="ECO:0000250"
FT INTRAMEM 514..515
FT /note="Note=Loop between two helices"
FT /evidence="ECO:0000250"
FT INTRAMEM 516..527
FT /note="Helical"
FT /evidence="ECO:0000250"
FT INTRAMEM 528..532
FT /note="Note=Loop between two helices"
FT /evidence="ECO:0000250"
FT TRANSMEM 533..550
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 551..902
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT DOMAIN 586..644
FT /note="CBS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 794..854
FT /note="CBS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT REGION 648..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 860..902
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 163..167
FT /note="Selectivity filter part_1"
FT /evidence="ECO:0000250"
FT MOTIF 205..209
FT /note="Selectivity filter part_2"
FT /evidence="ECO:0000250"
FT MOTIF 459..463
FT /note="Selectivity filter part_3"
FT /evidence="ECO:0000250"
FT COMPBIAS 663..681
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 708..722
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 861..875
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 22
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9R0A1"
FT VAR_SEQ 76
FT /note="I -> M (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_001041"
FT VAR_SEQ 77..86
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_001042"
FT CONFLICT 283
FT /note="S -> A (in Ref. 1; AAD37114)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 902 AA; 98888 MW; F6C57E216B81881D CRC64;
MAASAAAAGE GMEPRALQYE QTLMYGRYTQ ELGAFAKEEA ARIRLGGPEP WKGPPSPRVP
PELLEYGQSR CAPCCICSVR CHKFLVSRVG EDWIFLVLLG LLMALVSWAM DYAIAVCLQA
QQWMSQGLNT NILLQYLAWV TYPVVLITFS AGFTQILAPQ AVGSGIPEMK TILRGVVLKE
YLTLKTFVAK VIGLTCALGS GMPLGKEGPF VHIASMCASL LSKFLSLFGG IYENESRNTE
MLAAACAVGV GCCFAAPIGG VLFSIEVTST FFAVRNYWRG FFSATFSAFI FRVLAVWNRD
EETITALFKT RFRLDFPFDL QELPAFAVIG IASGFGGALF VYLNRKIVQV MRKQKTINRF
LMRKRLLFPA LVTLLISTLT FPPGFGQFMA GQLSQKETLV TLFDNRTWVH QGLVEEQEPP
STSQAWNPPR ANVFLTLVIF ILMKFWMSAL ATTIPVPCGA FMPVFVIGAA FGRLVGESMA
AWFPDGIHTD GSTYRIVPGG YAVVGAAALA GAVTHTVSTA VIVFELTGQI AHILPVMIAV
ILANAVAQSL QPSLYDSIIR IKKLPYLPEL GWGRHQQYRV RVEDIMVRDV PYVALNCTFR
DLRLALHRTK GRMLALVESS ESMILLGSIE RSQVVTLLGA QLSAARRRQH IQERRKAQMS
PPSDQDGLPS PESSVHFQVN TEDSAFIPAR GETHKPLKPA LKRGPSNASK AGETSTGSME
SAGIALRSLF CGSPPPEATS DLEKPESCER RKLKRVRISL ANDADLEGEM SPEEILEWEE
QQLNEPVNFS DCKIDPAPFQ LVERTSLHKT HTIFSLLGVD HAYVTSIGRL IGIVTLKELR
KAIEGSVTAQ GVKVRPPLAS FRDSATSSSD TETTEVHALW GPHSCHGLPR DGSPSDSDDK
CQ
