CLCN7_BOVIN
ID CLCN7_BOVIN Reviewed; 809 AA.
AC Q4PKH3;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=H(+)/Cl(-) exchange transporter 7;
DE AltName: Full=Chloride channel 7 alpha subunit;
DE AltName: Full=Chloride channel protein 7;
DE Short=ClC-7;
GN Name=CLCN7;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lens epithelium;
RA Rae J.L.;
RT "Ion channels in ocular epithelia.";
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Slowly voltage-gated channel mediating the exchange of
CC chloride ions against protons (By similarity). Functions as antiporter
CC and contributes to the acidification of the lysosome lumen and may be
CC involved in maintaining lysosomal pH (By similarity). The CLC channel
CC family contains both chloride channels and proton-coupled anion
CC transporters that exchange chloride or another anion for protons (By
CC similarity). The presence of conserved gating glutamate residues is
CC typical for family members that function as antiporters (By
CC similarity). {ECO:0000250|UniProtKB:O70496,
CC ECO:0000250|UniProtKB:P35523}.
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:0000250|UniProtKB:P51798};
CC -!- SUBUNIT: Chloride channel 7 are heteromers of alpha (CLCN7) and beta
CC (OSTM1) subunits. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the chloride channel (TC 2.A.49) family. ClC-
CC 7/CLCN7 subfamily. {ECO:0000305}.
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DR EMBL; DQ073465; AAY82470.1; -; mRNA.
DR RefSeq; NP_001020502.1; NM_001025331.1.
DR AlphaFoldDB; Q4PKH3; -.
DR SMR; Q4PKH3; -.
DR STRING; 9913.ENSBTAP00000021122; -.
DR PaxDb; Q4PKH3; -.
DR Ensembl; ENSBTAT00000021122; ENSBTAP00000021122; ENSBTAG00000015889.
DR GeneID; 513545; -.
DR KEGG; bta:513545; -.
DR CTD; 1186; -.
DR VEuPathDB; HostDB:ENSBTAG00000015889; -.
DR VGNC; VGNC:27401; CLCN7.
DR eggNOG; KOG0474; Eukaryota.
DR GeneTree; ENSGT00940000158458; -.
DR HOGENOM; CLU_003181_4_1_1; -.
DR InParanoid; Q4PKH3; -.
DR OMA; DYDVCEN; -.
DR OrthoDB; 410280at2759; -.
DR TreeFam; TF313867; -.
DR Proteomes; UP000009136; Chromosome 25.
DR Bgee; ENSBTAG00000015889; Expressed in monocyte and 103 other tissues.
DR ExpressionAtlas; Q4PKH3; baseline and differential.
DR GO; GO:0034707; C:chloride channel complex; IEA:Ensembl.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005765; C:lysosomal membrane; IBA:GO_Central.
DR GO; GO:0015297; F:antiporter activity; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0015108; F:chloride transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005247; F:voltage-gated chloride channel activity; IEA:InterPro.
DR GO; GO:0030321; P:transepithelial chloride transport; IEA:Ensembl.
DR Gene3D; 3.10.580.10; -; 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; IPR002249; Cl_channel-7.
DR Pfam; PF00571; CBS; 2.
DR Pfam; PF00654; Voltage_CLC; 1.
DR PRINTS; PR00762; CLCHANNEL.
DR PRINTS; PR01118; CLCHANNEL7.
DR SMART; SM00116; CBS; 2.
DR SUPFAM; SSF54631; SSF54631; 1.
DR SUPFAM; SSF81340; SSF81340; 1.
DR PROSITE; PS51371; CBS; 2.
PE 2: Evidence at transcript level;
KW Antiport; ATP-binding; CBS domain; Chloride; Ion transport; Lysosome;
KW Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..809
FT /note="H(+)/Cl(-) exchange transporter 7"
FT /id="PRO_0000244028"
FT TOPO_DOM 1..130
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 131..163
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 178..201
FT /note="Helical"
FT /evidence="ECO:0000250"
FT INTRAMEM 210..217
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 227..245
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 251..268
FT /note="Helical"
FT /evidence="ECO:0000250"
FT INTRAMEM 292..304
FT /note="Helical"
FT /evidence="ECO:0000250"
FT INTRAMEM 308..316
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 326..345
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 379..409
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 414..436
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 491..511
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 516..539
FT /note="Helical"
FT /evidence="ECO:0000250"
FT INTRAMEM 549..563
FT /note="Helical"
FT /evidence="ECO:0000250"
FT INTRAMEM 564..566
FT /note="Note=Loop between two helices"
FT /evidence="ECO:0000250"
FT INTRAMEM 567..578
FT /note="Helical"
FT /evidence="ECO:0000250"
FT INTRAMEM 579..582
FT /note="Note=Loop between two helices"
FT /evidence="ECO:0000250"
FT TRANSMEM 583..601
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 602..809
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT DOMAIN 635..699
FT /note="CBS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 745..803
FT /note="CBS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT MOTIF 207..211
FT /note="Selectivity filter part_1"
FT /evidence="ECO:0000250"
FT MOTIF 249..253
FT /note="Selectivity filter part_2"
FT /evidence="ECO:0000250"
FT MOTIF 516..520
FT /note="Selectivity filter part_3"
FT /evidence="ECO:0000250"
FT BINDING 208
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250"
FT BINDING 518
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250"
FT BINDING 606
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250"
FT BINDING 662..664
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 787..790
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT SITE 251
FT /note="Mediates proton transfer from the outer aqueous
FT phase to the interior of the protein; involved in linking
FT H(+) and Cl(-) transport"
FT /evidence="ECO:0000250"
FT SITE 318
FT /note="Mediates proton transfer from the protein to the
FT inner aqueous phase"
FT /evidence="ECO:0000250"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O70496"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51798"
FT MOD_RES 805
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51798"
SQ SEQUENCE 809 AA; 88831 MW; B8A07A7B840FD7F3 CRC64;
MANVSKKVSW SGRDLDDDEA APLLRRAPRL GVPAGEAAPL LNGAGPAAAR ASPHSAFFRI
GQLSSVELDD ELLDPDMDPP HPFPREIPHN EKLLSLKYES LDYDNSENQL FLEEERRINH
TAFRTVEIKR WVICAMVGIL TGLVACFIDI VVEKLAGLKY RLVKDNIDRF TEHGGLSFSL
LLWAALNAAF VLLGSTIVAF IEPVAAGSGI PQIKCFLNGV KIPHVVRLKT LVIKVSGVIL
SVVGGLAVGK EGPMIHSGSV IAAGISQGRS TSLKRDFKIF EYFRRDTEKR DFVSAGAAAG
VSAAFGAPVG GVLFSLEEGA SFWNQFLTWR IFFASMISTF TLNFVLSIYH GNAWDLSSPG
LINFGRFDTE TMVYVIHEIP IFIAMGVVGG ILGAVFNALN YWLTMFRIRY VHRPCLQVVE
ATLVAAVTAT AAFVLIYSSR DCQPLRGSSV SYPLQLFCAD GEYNSMAVAF FNTPEKSVVS
LFHDPPGSYN PMTLGLFTLV YFFLACWTYG LTVSAGVFIP SLLIGAAWGR LFGISLSYIT
GAAVWADPGK YALMGAAAQL GGIVRMTLSL TVIMMEATSS VTYGFPIMLV LMTAKIVGDV
FIEGLYDMHI QLQSVPFLHW EAPVTSHSLT AREVMSTPVT CLRRREKVGV IVDVLSSTAS
NHNGFPVVED ADGTQPARLQ GLILRSQLIV LLKHKVFVER SSMGLLRRRL RLKDFRDAYP
RFPPIQSIHV SQDERECTMD LSEFMNPSPY TVPQEASLPR VFKLFRALGL RHLVVVDNCN
QVVGLVTRKD LARYRLGKGG LEELSLAQT
