ID A0A340Y9D4_LIPVE Unreviewed; 873 AA.
AC A0A340Y9D4;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Chloride channel protein 2 {ECO:0000256|ARBA:ARBA00017377};
GN Name=CLCN2 {ECO:0000313|RefSeq:XP_007469027.1};
OS Lipotes vexillifer (Yangtze river dolphin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Lipotidae; Lipotes.
OX NCBI_TaxID=118797 {ECO:0000313|Proteomes:UP000265300, ECO:0000313|RefSeq:XP_007469027.1};
RN [1] {ECO:0000313|RefSeq:XP_007469027.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the chloride channel (TC 2.A.49) family. ClC-
CC 2/CLCN2 subfamily. {ECO:0000256|ARBA:ARBA00005423}.
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DR RefSeq; XP_007469027.1; XM_007468965.1.
DR AlphaFoldDB; A0A340Y9D4; -.
DR GeneID; 103087980; -.
DR CTD; 1181; -.
DR OrthoDB; 1194at2759; -.
DR Proteomes; UP000265300; Unplaced.
DR GO; GO:0034702; C:monoatomic ion channel complex; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005247; F:voltage-gated chloride channel activity; IEA:InterPro.
DR CDD; cd03683; ClC_1_like; 1.
DR Gene3D; 3.10.580.10; CBS-domain; 2.
DR Gene3D; 1.10.3080.10; Clc chloride channel; 1.
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 PANTHER; PTHR45720; CHLORIDE CHANNEL PROTEIN 2; 1.
DR PANTHER; PTHR45720:SF6; CHLORIDE CHANNEL PROTEIN 2; 1.
DR Pfam; PF00654; Voltage_CLC; 1.
DR PRINTS; PR00762; CLCHANNEL.
DR PRINTS; PR01113; CLCHANNEL2.
DR SUPFAM; SSF54631; CBS-domain pair; 1.
DR SUPFAM; SSF81340; Clc chloride channel; 1.
PE 3: Inferred from homology;
KW CBS domain {ECO:0000256|ARBA:ARBA00023122};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Ion channel {ECO:0000256|ARBA:ARBA00022882};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000265300};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448};
KW Voltage-gated channel {ECO:0000256|ARBA:ARBA00022882}.
FT TRANSMEM 95..117
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 138..160
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 180..200
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 212..231
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 243..267
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 279..299
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 325..347
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 368..387
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 435..456
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 463..485
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 533..552
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 650..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 734..756
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 827..873
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..683
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 742..756
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 832..846
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 873 AA; 95814 MW; 41BEB104E7E787F4 CRC64;
MAAAAGAAAA EEGMEPRALQ YEQTLMYGRY TQDLGAFAKE EAARIRLGGP EPWRGPPSPR
AAPELLEYGQ SRCTRCRICT VHCHKFLVSR VGEDWIFLVL LGLLMALVSW AMDYAIAACL
QAQQWMSRGL NTNLLLQYLA WVTYPVVLIT FSAGFTQILA PQAVGSGIPE MKTILRGVVL
KEYLTLKTFV AKVIGLTCAL GSGMPLGKEG PFVHIASMCA ALLSKFLSLF GGIYENESRN
TEMLAAACAV GVGCCFAAPI GGVLFSIEVT STFFAVRNYW RGFFAATFSA FIFRVLAVWN
RDEETITALF KTRFRLDFPF DLQELPAFAV IGIASGFGGA LFVYLNRKIV QVMRKQKTIN
RFLMKKRLLF PALVTLLIST LTFPPGFGQF MAGQLSQKET LVTLFDNRTW VRQGLMEELE
PPGTSQAWNP PRANVFLTLV IFILMKFWMS ALATTIPVPC GAFMPVFVIG AAFGRLVGES
MAAWFPDGIH TDGSTYRIVP GGYAVVGAAA LAGAVTHTVS TAVIVFELTG QIAHILPVMI
AVILANAVAQ SLQPSLYDSI IRIKKLPYLP ELGWGRHQQY RVRVEDIMVR DVPHVALSCT
FRDLRLALHR TKGRVLALVE SPESMILLGS IECSQVVALL GAQLSPARRR QYMQEHRAAR
TSSPSDQESP PSPETSLLFQ VNTEDSGFPA ARGETHKPLK PALKRGPSNT VNLKESPTGN
MEQAGIALRS LFCGSPPPEP ASEKSEKCDK RKPKRVRISL ASDSDLEGEM TPEEILEWEE
QQLDEPVNFS DCKIDPAPFQ LVERTSLHKL RKAIEGSVTA QGVKVRPPLA SFRDSATSSS
DTETTEVHAL WGPRSRHGLP REGSPSDSDD KCQ
//
