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CLCN7_MOUSE
ID   CLCN7_MOUSE             Reviewed;         803 AA.
AC   O70496;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 177.
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 {ECO:0000312|MGI:MGI:1347048}; Synonyms=Clc7;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=11207362; DOI=10.1016/s0092-8674(01)00206-9;
RA   Kornak U., Kasper D., Boesl M.R., Kaiser E., Schweizer M., Schulz A.,
RA   Friedrich W., Delling G., Jentsch T.J.;
RT   "Loss of the ClC-7 chloride channel leads to osteopetrosis in mice and
RT   man.";
RL   Cell 104:205-215(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   FUNCTION, SUBUNIT, INTERACTION WITH OSTM1, AND SUBCELLULAR LOCATION.
RX   PubMed=16525474; DOI=10.1038/nature04535;
RA   Lange P.F., Wartosch L., Jentsch T.J., Fuhrmann J.C.;
RT   "ClC-7 requires Ostm1 as a beta-subunit to support bone resorption and
RT   lysosomal function.";
RL   Nature 440:220-223(2006).
RN   [4]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=19661288; DOI=10.1096/fj.09-130880;
RA   Wartosch L., Fuhrmann J.C., Schweizer M., Stauber T., Jentsch T.J.;
RT   "Lysosomal degradation of endocytosed proteins depends on the chloride
RT   transport protein ClC-7.";
RL   FASEB J. 23:4056-4068(2009).
RN   [5]
RP   TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF TYR-713.
RX   PubMed=31155284; DOI=10.1016/j.ajhg.2019.04.008;
RG   Undiagnosed Diseases Network;
RA   Nicoli E.R., Weston M.R., Hackbarth M., Becerril A., Larson A., Zein W.M.,
RA   Baker P.R. II, Burke J.D., Dorward H., Davids M., Huang Y., Adams D.R.,
RA   Zerfas P.M., Chen D., Markello T.C., Toro C., Wood T., Elliott G., Vu M.,
RA   Zheng W., Garrett L.J., Tifft C.J., Gahl W.A., Day-Salvatore D.L.,
RA   Mindell J.A., Malicdan M.C.V.;
RT   "Lysosomal Storage and Albinism Due to Effects of a De Novo CLCN7 Variant
RT   on Lysosomal Acidification.";
RL   Am. J. Hum. Genet. 104:1127-1138(2019).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Slowly voltage-gated channel mediating the exchange of
CC       chloride ions against protons (PubMed:16525474, PubMed:19661288).
CC       Functions as antiporter and contributes to the acidification of the
CC       lysosome lumen and may be involved in maintaining lysosomal pH
CC       (PubMed:16525474, PubMed:19661288). The CLC channel family contains
CC       both chloride channels and proton-coupled anion transporters that
CC       exchange chloride or another anion for protons (By similarity). The
CC       presence of conserved gating glutamate residues is typical for family
CC       members that function as antiporters (By similarity).
CC       {ECO:0000250|UniProtKB:P35523, ECO:0000269|PubMed:16525474,
CC       ECO:0000269|PubMed:19661288}.
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:0000269|PubMed:16525474}.
CC   -!- INTERACTION:
CC       O70496; Q8BGT0: Ostm1; NbExp=7; IntAct=EBI-987482, EBI-987431;
CC   -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:16525474,
CC       ECO:0000269|PubMed:31155284}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:16525474}.
CC   -!- TISSUE SPECIFICITY: Liver, spleen, kidneys and brain.
CC       {ECO:0000269|PubMed:31155284}.
CC   -!- DISRUPTION PHENOTYPE: Accumulates undegraded endocyted material in
CC       neurons or renal proximal tubular cells. Almost all ClC-7-deficient
CC       neurons die. {ECO:0000269|PubMed:19661288}.
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; AF063101; AAC18832.1; -; Genomic_DNA.
DR   EMBL; AF063098; AAC18832.1; JOINED; Genomic_DNA.
DR   EMBL; AF063099; AAC18832.1; JOINED; Genomic_DNA.
DR   EMBL; AF063100; AAC18832.1; JOINED; Genomic_DNA.
DR   EMBL; BC050907; AAH50907.1; -; mRNA.
DR   EMBL; BC053049; AAH53049.1; -; mRNA.
DR   EMBL; BC054799; AAH54799.1; -; mRNA.
DR   CCDS; CCDS28509.1; -.
DR   RefSeq; NP_036060.1; NM_011930.4.
DR   AlphaFoldDB; O70496; -.
DR   SMR; O70496; -.
DR   BioGRID; 204933; 2.
DR   IntAct; O70496; 1.
DR   STRING; 10090.ENSMUSP00000035964; -.
DR   iPTMnet; O70496; -.
DR   PhosphoSitePlus; O70496; -.
DR   SwissPalm; O70496; -.
DR   EPD; O70496; -.
DR   jPOST; O70496; -.
DR   PaxDb; O70496; -.
DR   PeptideAtlas; O70496; -.
DR   PRIDE; O70496; -.
DR   ProteomicsDB; 283282; -.
DR   Antibodypedia; 23121; 200 antibodies from 27 providers.
DR   DNASU; 26373; -.
DR   Ensembl; ENSMUST00000040729; ENSMUSP00000035964; ENSMUSG00000036636.
DR   GeneID; 26373; -.
DR   KEGG; mmu:26373; -.
DR   UCSC; uc008azv.1; mouse.
DR   CTD; 1186; -.
DR   MGI; MGI:1347048; Clcn7.
DR   VEuPathDB; HostDB:ENSMUSG00000036636; -.
DR   eggNOG; KOG0474; Eukaryota.
DR   GeneTree; ENSGT00940000158458; -.
DR   HOGENOM; CLU_003181_4_1_1; -.
DR   InParanoid; O70496; -.
DR   OrthoDB; 410280at2759; -.
DR   PhylomeDB; O70496; -.
DR   TreeFam; TF313867; -.
DR   Reactome; R-MMU-2672351; Stimuli-sensing channels.
DR   BioGRID-ORCS; 26373; 2 hits in 73 CRISPR screens.
DR   ChiTaRS; Clcn7; mouse.
DR   PRO; PR:O70496; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   RNAct; O70496; protein.
DR   Bgee; ENSMUSG00000036636; Expressed in superior surface of tongue and 255 other tissues.
DR   ExpressionAtlas; O70496; baseline and differential.
DR   Genevisible; O70496; MM.
DR   GO; GO:0034707; C:chloride channel complex; ISO:MGI.
DR   GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0005765; C:lysosomal membrane; ISO:MGI.
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; ISO:MGI.
DR   GO; GO:0030321; P:transepithelial chloride transport; ISO:MGI.
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   1: Evidence at protein 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_0000094453"
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:0007744|PubMed:19144319"
FT   MOD_RES         799
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P51798"
FT   MUTAGEN         713
FT                   /note="Y->C: Increased cytoplasmic vacuole size. Knockin
FT                   mice develop albinism and lysosomal-storage disease."
FT                   /evidence="ECO:0000269|PubMed:31155284"
SQ   SEQUENCE   803 AA;  88713 MW;  A7D6DA5791DAA48C 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 AWGRLFGISL 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
 
 
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