ID A0A2Y9JJ46_ENHLU Unreviewed; 903 AA.
AC A0A2Y9JJ46;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Chloride channel protein 2 {ECO:0000256|ARBA:ARBA00017377};
GN Name=LOC111148398 {ECO:0000313|RefSeq:XP_022360626.1};
OS Enhydra lutris kenyoni (northern sea otter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Lutrinae; Enhydra.
OX NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022360626.1};
RN [1] {ECO:0000313|RefSeq:XP_022360626.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022360626.1};
RG RefSeq;
RL Submitted (SEP-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_022360626.1; XM_022504918.1.
DR AlphaFoldDB; A0A2Y9JJ46; -.
DR STRING; 391180.A0A2Y9JJ46; -.
DR KEGG; elk:111148398; -.
DR OrthoDB; 1194at2759; -.
DR Proteomes; UP000248482; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005247; F:voltage-gated chloride channel activity; IEA:InterPro.
DR CDD; cd04591; CBS_pair_voltage-gated_CLC_euk_bac; 1.
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:ARBA00023303};
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:UP000248482};
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 94..116
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 137..159
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 211..230
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 242..266
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 324..346
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 367..386
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 434..455
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 462..484
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 532..551
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 649..713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 861..903
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 862..876
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 903 AA; 98870 MW; 20C8DC26C4393ED8 CRC64;
MAAAGAAAAA EGMEPRALQY EQTLMYGRYT QDLGAFAKEE AARIRLGGPE TWRGPPSSRA
PPELLEYGQS RCAQCRICSV RCHKFLVSRV GEDWIFLVLL GLLMALVSWA MDYAIAACLQ
AQQWMSRGLN TSLFLQYLAW VTYPIVLITF SAGFTQILAP QAVGSGIPEM KTILRGVVLK
EYLTLKTFVA KVIGLTCALG SGMPLGKEGP FVHIASMCAA LLSKFLSLFG GIYENESRNT
EMLAAACAVG VGCCFAAPIG GVLFSIEVTS TFFAVRNYWR GFFAATFSAF IFRVLAVWNR
DEETITALFK TRFRLDFPFD LQELPAFAVI GIASGFGGAL FVYLNRKIVQ VMRKQKTINR
FLMKKRLLFP ALVTLLISTL TFPPGFGQFM AGQLSQKETL VTLFDNRTWV RQGLVEDLEP
PGTSQAWSPP RANVFLTLVV FILMKFWMSA LATTIPVPCG AFMPVFVIGA AFGRLVGESM
AAWFPDGIHT DGSTYRIVPG GYAVVGAAAL AGAVTHTVST AVIVFELTGQ IAHILPVMIA
VILANAVAQS LQPSLYDSII RIKKLPYLPE LGWGRHQQYR MRVEDIMVRD VPYVALSCTF
RDLRLALHRT KGRMLALVES PESMILLGSI ERSQVVALLA AQLSPARRRQ YAQERRAAQT
SPPPDQESPP SPEASVRFQV NTEDSGFPAA RGDTHKPLKP ALKRGPSNTM NLGESPTGNM
EQAGIALRSL FCGSPPPEAA SELEKSESGD KRKLKRVRIS LASDSDLEGE MSPEEILEWE
EQKLDEPVNF SDCKIDPAPF QLVERTSLHK THTIFSLLGV DHAYVTSIGR LIGIVTLKEL
RKAIEGSVTA QGVKVRPPLA SFRDSATSSS DTETTEVHAL WGPHSHHGLP REGSPSDSDD
KCQ
//