ID A0A340Y5R3_LIPVE Unreviewed; 885 AA.
AC A0A340Y5R3;
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_007469026.1};
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_007469026.1};
RN [1] {ECO:0000313|RefSeq:XP_007469026.1}
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_007469026.1; XM_007468964.1.
DR AlphaFoldDB; A0A340Y5R3; -.
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 436..469
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 481..509
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 633..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 717..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 843..885
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..666
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 725..739
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 844..858
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 885 AA; 97202 MW; FC854F43EA1BFAFD 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 GAFMPVFVID GIHTDGSTYR
IVPGGYAVVG AAALAGAVTH TVSTAVIVFE LTGQIAHILP VMIAVILANA VAQSLQPSLY
DSIIRIKKLP YLPELGWGRH QQYRVRVEDI MVRDVPHVAL SCTFRDLRLA LHRTKGRVLA
LVESPESMIL LGSIECSQVV ALLGAQLSPA RRRQYMQEHR AARTSSPSDQ ESPPSPETSL
LFQVNTEDSG FPAARGETHK PLKPALKRGP SNTVNLKESP TGNMEQAGIA LRSLFCGSPP
PEPASEKSEK CDKRKPKRVR ISLASDSDLE GEMTPEEILE WEEQQLDEPV NFSDCKIDPA
PFQLVERTSL HKTHTIFSLL GVDHAYVTSI GRLIGIVTLK ELRKAIEGSV TAQGVKVRPP
LASFRDSATS SSDTETTEVH ALWGPRSRHG LPREGSPSDS DDKCQ
//
