ID G7Q2R0_MACFA Unreviewed; 816 AA.
AC G7Q2R0;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Chloride channel protein {ECO:0000256|RuleBase:RU361221};
GN Name=CLCN5 {ECO:0000313|Ensembl:ENSMFAP00000017039.2};
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541 {ECO:0000313|Ensembl:ENSMFAP00000017039.2, ECO:0000313|Proteomes:UP000233100};
RN [1] {ECO:0000313|Ensembl:ENSMFAP00000017039.2, ECO:0000313|Proteomes:UP000233100}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSMFAP00000017039.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 chloride(in) + H(+)(out) = 2 chloride(out) + H(+)(in);
CC Xref=Rhea:RHEA:29567, ChEBI:CHEBI:15378, ChEBI:CHEBI:17996;
CC Evidence={ECO:0000256|ARBA:ARBA00029360};
CC -!- SUBUNIT: Interacts with NEDD4 and NEDD4L.
CC {ECO:0000256|ARBA:ARBA00011608}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Endosome
CC membrane {ECO:0000256|ARBA:ARBA00004337}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004337}. Golgi apparatus membrane
CC {ECO:0000256|ARBA:ARBA00004653}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004653}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361221}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU361221}.
CC -!- SIMILARITY: Belongs to the chloride channel (TC 2.A.49) family. ClC-
CC 5/CLCN5 subfamily. {ECO:0000256|ARBA:ARBA00010639}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU361221}.
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DR AlphaFoldDB; G7Q2R0; -.
DR STRING; 9541.ENSMFAP00000017039; -.
DR Ensembl; ENSMFAT00000067578.2; ENSMFAP00000017039.2; ENSMFAG00000031675.2.
DR VEuPathDB; HostDB:ENSMFAG00000031675; -.
DR eggNOG; KOG0475; Eukaryota.
DR GeneTree; ENSGT00940000153763; -.
DR OrthoDB; 150430at2759; -.
DR Proteomes; UP000233100; Chromosome X.
DR Bgee; ENSMFAG00000031675; Expressed in adult mammalian kidney and 13 other cell types or tissues.
DR GO; GO:0045177; C:apical part of cell; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0005247; F:voltage-gated chloride channel activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006897; P:endocytosis; IEA:Ensembl.
DR GO; GO:0003014; P:renal system process; IEA:Ensembl.
DR CDD; cd04591; CBS_pair_voltage-gated_CLC_euk_bac; 1.
DR CDD; cd03684; ClC_3_like; 1.
DR Gene3D; 3.10.580.20; -; 1.
DR Gene3D; 3.90.1280.20; -; 1.
DR Gene3D; 1.10.3080.10; Clc chloride channel; 1.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR014743; Cl-channel_core.
DR InterPro; IPR001807; Cl-channel_volt-gated.
DR InterPro; IPR002247; Cl_channel-5.
DR PANTHER; PTHR45711; CHLORIDE CHANNEL PROTEIN; 1.
DR PANTHER; PTHR45711:SF7; H(+)_CL(-) EXCHANGE TRANSPORTER 5; 1.
DR Pfam; PF00571; CBS; 2.
DR Pfam; PF00654; Voltage_CLC; 1.
DR PRINTS; PR00762; CLCHANNEL.
DR PRINTS; PR01116; CLCHANNEL5.
DR SMART; SM00116; CBS; 2.
DR SUPFAM; SSF54631; CBS-domain pair; 1.
DR SUPFAM; SSF81340; Clc chloride channel; 1.
DR PROSITE; PS51371; CBS; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW CBS domain {ECO:0000256|ARBA:ARBA00023122, ECO:0000256|PROSITE-
KW ProRule:PRU00703};
KW Chloride {ECO:0000256|ARBA:ARBA00023214, ECO:0000256|RuleBase:RU361221};
KW Endosome {ECO:0000256|ARBA:ARBA00022753};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Ion transport {ECO:0000256|RuleBase:RU361221};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361221};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000233100};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU361221};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU361221}; Transport {ECO:0000256|RuleBase:RU361221};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 210..235
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 312..336
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 386..407
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 427..444
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 497..517
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 524..543
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT TRANSMEM 571..596
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361221"
FT DOMAIN 656..720
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 752..812
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 816 AA; 90891 MW; B401B2AD41EEFA11 CRC64;
MAMWQGAMDN RGFQQGSFSS FQNSSSDEDL MDIPTTAMDF SMRDDVPPLD REVGEDKSYN
GGGIGYSNRI MDFLEEPIPG VGTYDDFNTI DWVREKSRDR DRHREITNKS KESTWALIHS
VSDAFSGWLL MLLIGLLSGS LAGLIDISAH WMTDLKEGIC TGGFWFNHEH CCWNSDHVTF
EERDKCPEWN SWSQLIISTD EGAFAYIVNY FMYVLWALLF AFLAVSLVKV FAPYACGSGI
PEIKTILSGF IIRGYLGKWT LVIKTITLVL AVSSGLSLGK EGPLVHVACC CGNILCHCFN
KYRKNEAKRR EVLSAAAAAG VSVAFGAPIG GVLFSLEEVS YYFPLKTLWR SFFAALVAAF
TLRSINPFGN SRLVLFYVEF HTPWHLFELV PFILLGIFGG LWGALFIRTN IAWCRKRKTT
QLGKYPVIEV LVVTAITAIL AFPNEYTRMS TSELISELFN DCGLLDSSKL CDYENRFNTS
KGGELPDRPA GVGVYSAMWQ LALTLILKIV ITIFTFGMKI PSGLFIPSMA VGAIAGRLLG
VGMEQLAYYH QEWTIFNSWC SQGADCITPG LYAMVGAAAC LGGVTRMTVS LVVIMFELTG
GLEYIVPLMA AAMTSKWVAD ALGREGIYDA HIRLNGYPFL EAKEEFAHKT LAMDVMKPRR
NDPLLTVLTQ DSMTVEDVET IISETTYSGF PVVVSRESQR LVGFVLRRDL IISIENARKK
QDGVVSTSII YFTEHSPPLP PYTPPTLKLR NILDLSPFTV TDLTPMEIVV DIFRKLGLRQ
CLVTHNGRLL GIITKKDVLK HIAQMANQDP DSILFN
//
