ID A0A3P8YFL6_ESOLU Unreviewed; 913 AA.
AC A0A3P8YFL6;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, 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|Ensembl:ENSELUP00000015407.1};
OS Esox lucius (Northern pike).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC Esocidae; Esox.
OX NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000015407.1, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000015407.1, ECO:0000313|Proteomes:UP000265140}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25069045;
RA Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT "The genome and linkage map of the northern pike (Esox lucius): conserved
RT synteny revealed between the salmonid sister group and the Neoteleostei.";
RL PLoS ONE 9:e102089-e102089(2014).
RN [2] {ECO:0000313|Ensembl:ENSELUP00000015407.1}
RP IDENTIFICATION.
RG Ensembl;
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_010877684.1; XM_010879382.3.
DR AlphaFoldDB; A0A3P8YFL6; -.
DR STRING; 8010.ENSELUP00000015407; -.
DR Ensembl; ENSELUT00000024463.2; ENSELUP00000015407.1; ENSELUG00000015368.2.
DR GeneID; 105015878; -.
DR KEGG; els:105015878; -.
DR GeneTree; ENSGT00940000155439; -.
DR OrthoDB; 1194at2759; -.
DR Proteomes; UP000265140; LG01.
DR Bgee; ENSELUG00000015368; Expressed in pharyngeal gill and 11 other cell types or tissues.
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; IPR017896; 4Fe4S_Fe-S-bd.
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.
DR PROSITE; PS51379; 4FE4S_FER_2; 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:UP000265140};
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 84..107
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 127..149
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 201..220
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 232..256
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 268..288
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 314..336
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 357..376
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 420..438
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 445..467
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 487..514
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 521..541
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 53..82
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT REGION 867..913
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 870..884
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 885..913
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 913 AA; 101747 MW; F925550FD299C1CF CRC64;
MAADDQRALQ YEQTLMYGRY TQELGVYAKE EAARLREESG RRRSITERSR SLELLEYDKG
RCAKCRICTF RCQKFLISRV GEDWIFLILL GLFMALVSWV MDYAIAICLE AQKWMYGGLE
SNVFLQYLAW VTYPVVLITF SAGFTQILAP QAVGSGIPEM KTILRGVVLK EYLTFKTFVA
KVIGLTCALG SGMPLGKEGP FVHIASLCAA LLSKFMSLFG GIYENESRNI EMLAAACAVG
VGCCFAAPIG GVLFSIEVTS TFFAVRNYWR GFFAATFSAF IFRVLAVWNR DEETITALFK
TRFRLDFPFD LQELPAFAVI GIASGFAGAL FVYLNRLIVQ FIRKQKTINK FLMKKRLLYP
ALVTLLVSTL TFPPGFGQFM AGKLTQKESL VTFFDNQTWT KQGIAKEFDY TDNSQAWKNP
QVNVFVTLVV FIVMKFWMSA LATTIPVPCG AFMPVFVIGA AFGRLVGESM AAWFPDGIHS
DGTIYPIVPG GYAVVGAAAL SGAVTHTVST AVIVFELTGQ ISHILPVMIA VILANAVAQS
LQPSLYDSII RIKKLPYLPE LGWGHHEKYN IRVEDIMIRD VTYITLNCCY RDLHDVLLAG
HHLKTLALLE SSESMILLGS IERAQLQALL SQQLGRPRRL EYLRERAAAE KKRQSVVSHL
SSEDGSTKVN QEVRFQISTE ESTFSPIHTP SLKPLKPALK RPSVVDRPAE IPIPTSPQDH
SGSTLKHLFC ANPETEGLEK NNVHIDIGGT ASSPATPDLR RPPKRVRISV VDDDVEDDMT
IREIAEWEEN QLDEPVNFDN CKIDPAPFQL VERTSLHKTH TIFSLLGLDH AYVTSIGRLI
GVVSLKELRK AIEGSVEVKG VKVRPPLASF RDSGTSSSNS ENEATELHKL WDRHKSMSLP
REHLPSDSDE KSQ
//
