CLCN7_RAT
ID CLCN7_RAT Reviewed; 803 AA.
AC P51799;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 155.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=8543009; DOI=10.1016/0014-5793(95)01298-2;
RA Brandt S., Jentsch T.J.;
RT "ClC-6 and ClC-7 are two novel broadly expressed members of the CLC
RT chloride channel family.";
RL FEBS Lett. 377:15-20(1995).
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=16222710; DOI=10.1002/jcp.20516;
RA Suzuki T., Rai T., Hayama A., Sohara E., Suda S., Itoh T., Sasaki S.,
RA Uchida S.;
RT "Intracellular localization of ClC chloride channels and their ability to
RT form hetero-oligomers.";
RL J. Cell. Physiol. 206:792-798(2006).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18449189; DOI=10.1038/nature06907;
RA Graves A.R., Curran P.K., Smith C.L., Mindell J.A.;
RT "The Cl-/H+ antiporter ClC-7 is the primary chloride permeation pathway in
RT lysosomes.";
RL Nature 453:788-792(2008).
CC -!- FUNCTION: Slowly voltage-gated channel mediating the exchange of
CC chloride ions against protons (PubMed:18449189). Functions as
CC antiporter and contributes to the acidification of the lysosome lumen
CC and may be involved in maintaining lysosomal pH (By similarity). The
CC CLC channel family contains both chloride channels and proton-coupled
CC anion transporters that exchange chloride or another anion for protons
CC (PubMed:18449189). The presence of conserved gating glutamate residues
CC is typical for family members that function as antiporters (By
CC similarity). {ECO:0000250|UniProtKB:O70496,
CC ECO:0000250|UniProtKB:P35523, ECO:0000269|PubMed:18449189}.
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:0000269|PubMed:16222710,
CC ECO:0000269|PubMed:18449189}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16222710, ECO:0000269|PubMed:18449189}.
CC -!- TISSUE SPECIFICITY: Brain, testis, muscle and kidney.
CC -!- SIMILARITY: Belongs to the chloride channel (TC 2.A.49) family. ClC-
CC 7/CLCN7 subfamily. {ECO:0000305}.
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 EMBL; Z67744; CAA91557.1; -; mRNA.
DR PIR; S68426; S68426.
DR RefSeq; NP_113756.1; NM_031568.2.
DR AlphaFoldDB; P51799; -.
DR SMR; P51799; -.
DR IntAct; P51799; 2.
DR MINT; P51799; -.
DR STRING; 10116.ENSRNOP00000023615; -.
DR iPTMnet; P51799; -.
DR PhosphoSitePlus; P51799; -.
DR jPOST; P51799; -.
DR PaxDb; P51799; -.
DR GeneID; 29233; -.
DR KEGG; rno:29233; -.
DR UCSC; RGD:61836; rat.
DR CTD; 1186; -.
DR RGD; 61836; Clcn7.
DR VEuPathDB; HostDB:ENSRNOG00000016976; -.
DR eggNOG; KOG0474; Eukaryota.
DR HOGENOM; CLU_003181_4_1_1; -.
DR InParanoid; P51799; -.
DR OMA; DYDVCEN; -.
DR OrthoDB; 410280at2759; -.
DR PhylomeDB; P51799; -.
DR TreeFam; TF313867; -.
DR Reactome; R-RNO-2672351; Stimuli-sensing channels.
DR PRO; PR:P51799; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000016976; Expressed in frontal cortex and 19 other tissues.
DR Genevisible; P51799; RN.
DR GO; GO:0034707; C:chloride channel complex; ISO:RGD.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:RGD.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005765; C:lysosomal membrane; ISO:RGD.
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:0009268; P:response to pH; IDA:RGD.
DR GO; GO:0030321; P:transepithelial chloride transport; ISO:RGD.
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..803
FT /note="H(+)/Cl(-) exchange transporter 7"
FT /id="PRO_0000094454"
FT TOPO_DOM 1..124
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 125..157
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 172..195
FT /note="Helical"
FT /evidence="ECO:0000250"
FT INTRAMEM 204..211
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 221..239
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 245..262
FT /note="Helical"
FT /evidence="ECO:0000250"
FT INTRAMEM 286..298
FT /note="Helical"
FT /evidence="ECO:0000250"
FT INTRAMEM 302..310
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 320..339
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 373..403
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 408..430
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 485..505
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 510..533
FT /note="Helical"
FT /evidence="ECO:0000250"
FT INTRAMEM 543..557
FT /note="Helical"
FT /evidence="ECO:0000250"
FT INTRAMEM 558..560
FT /note="Note=Loop between two helices"
FT /evidence="ECO:0000250"
FT INTRAMEM 561..572
FT /note="Helical"
FT /evidence="ECO:0000250"
FT INTRAMEM 573..576
FT /note="Note=Loop between two helices"
FT /evidence="ECO:0000250"
FT TRANSMEM 577..595
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 596..803
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT DOMAIN 629..693
FT /note="CBS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 739..797
FT /note="CBS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 201..205
FT /note="Selectivity filter part_1"
FT /evidence="ECO:0000250"
FT MOTIF 243..247
FT /note="Selectivity filter part_2"
FT /evidence="ECO:0000250"
FT MOTIF 510..514
FT /note="Selectivity filter part_3"
FT /evidence="ECO:0000250"
FT COMPBIAS 9..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 202
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250"
FT BINDING 512
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250"
FT BINDING 600
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250"
FT BINDING 656..658
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 781..784
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT SITE 245
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 312
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 799
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51798"
SQ SEQUENCE 803 AA; 88731 MW; A7D6AA3D21DA6FED CRC64;
MANVSKKVSW SGRDRDDEEG APLLRRTGQP DEETPLLNGA GPGARQSHSA LFRIGQMNNV
ELDDELLDPE VDPPHTFPKE IPHNEKLLSL KYESLDYDNS ENQLFLEEER RINHTAFRTV
EIKRWVICAL IGILTGLVAC FIDIVVENLA GLKYRVIKDN IDKFTEKGGL SFSLLLWATL
NSAFVLVGSV IVAFIEPVAA GSGIPQIKCF LNGVKIPHVV RLKTLVIKVS GVILSVVGGL
AVGKEGPMIH SGSVIAAGIS QGRSTSLKRD FKIFEYFRRD TEKRDFVSAG AAAGVSAAFG
APVGGVLFSL EEGASFWNQF LTWRIFFASM ISTFTLNFVL SIYHGNMWDL SSPGLINFGR
FDSEKMAYTI HEIPVFIAMG VVGGILGAVF NALNYWLTMF RIRYIHRPCL QVIEAMLVAA
VTATVAFVLI YSSRDCQPLQ GSSMSYPLQL FCADGEYNSM AAAFFNTPEK SVVSLFHDPP
GSYNPMTLGL FTLVYFFLAC WTYGLTVSAG VFIPSLLIGA AWGRLFGISM SYLTGAAIWA
DPGKYALMGA AAQLGGIVRM TLSLTVIMME ATSNVTYGFP IMLVLMTAKI VGDVFIEGLY
DMHIQLQSVP FLHWEAPVTS HSLTAREVMS TPVTCLRRRE KVGIIVDVLS DTASNHNGFP
VVEDVGDTQP ARLQGLILRS QLIVLLKHKV FVERSNMGLV QRRLRLKDFR DAYPRFPPIQ
SIHVSQDERE CTMDLSEFMN PSPYTVPQEA SLPRVFKLFR ALGLRHLVVV DNHNQVVGLV
TRKDLARYRL GKGGLEELSL AQT
