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CLCN5_MOUSE
ID   CLCN5_MOUSE             Reviewed;         816 AA.
AC   Q9WVD4; B1ATV0; B1AXN0;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   12-AUG-2020, sequence version 2.
DT   03-AUG-2022, entry version 160.
DE   RecName: Full=H(+)/Cl(-) exchange transporter 5;
DE   AltName: Full=Chloride channel protein 5;
DE            Short=ClC-5;
DE   AltName: Full=Chloride transporter ClC-5;
GN   Name=Clcn5; Synonyms=Clc5;
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 [MRNA] (ISOFORM 2).
RC   TISSUE=Kidney;
RX   PubMed=10373326; DOI=10.1006/geno.1999.5839;
RA   Tanaka K., Fisher S.E., Craig I.W.;
RT   "Characterization of novel promoter and enhancer elements of the mouse
RT   homologue of the Dent disease gene, CLCN5, implicated in X-linked
RT   hereditary nephrolithiasis.";
RL   Genomics 58:281-292(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Proton-coupled chloride transporter. Functions as antiport
CC       system and exchanges chloride ions against protons. Important for
CC       normal acidification of the endosome lumen. May play an important role
CC       in renal tubular function (By similarity). The CLC channel family
CC       contains both chloride channels and proton-coupled anion transporters
CC       that exchange chloride or another anion for protons. The absence of
CC       conserved gating glutamate residues is typical for family members that
CC       function as channels (Probable). {ECO:0000250|UniProtKB:P51795,
CC       ECO:0000305}.
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:P51795};
CC   -!- SUBUNIT: Interacts with NEDD4 and NEDD4L.
CC       {ECO:0000250|UniProtKB:P51795}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000250|UniProtKB:P51795}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P51795}. Endosome membrane
CC       {ECO:0000250|UniProtKB:P51795}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P51795}. Cell membrane
CC       {ECO:0000250|UniProtKB:P51795}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P51795}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9WVD4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9WVD4-2; Sequence=VSP_060655;
CC   -!- TISSUE SPECIFICITY: Kidney specific.
CC   -!- PTM: Ubiquitinated by NEDD4L in the presence of albumin; which promotes
CC       endocytosis and proteasomal degradation.
CC       {ECO:0000250|UniProtKB:P51795}.
CC   -!- SIMILARITY: Belongs to the chloride channel (TC 2.A.49) family. ClC-
CC       5/CLCN5 subfamily. {ECO:0000305}.
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DR   EMBL; AF134117; AAD28473.1; -; mRNA.
DR   EMBL; AL663104; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL808124; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL954858; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS29963.1; -. [Q9WVD4-2]
DR   CCDS; CCDS57727.1; -. [Q9WVD4-1]
DR   RefSeq; NP_001230691.1; NM_001243762.1. [Q9WVD4-1]
DR   RefSeq; NP_057900.3; NM_016691.4. [Q9WVD4-2]
DR   AlphaFoldDB; Q9WVD4; -.
DR   SMR; Q9WVD4; -.
DR   BioGRID; 198738; 3.
DR   IntAct; Q9WVD4; 1.
DR   STRING; 10090.ENSMUSP00000004428; -.
DR   iPTMnet; Q9WVD4; -.
DR   PhosphoSitePlus; Q9WVD4; -.
DR   jPOST; Q9WVD4; -.
DR   MaxQB; Q9WVD4; -.
DR   PaxDb; Q9WVD4; -.
DR   PRIDE; Q9WVD4; -.
DR   ProteomicsDB; 285480; -. [Q9WVD4-1]
DR   ProteomicsDB; 351413; -.
DR   ABCD; Q9WVD4; 2 sequenced antibodies.
DR   Antibodypedia; 396; 202 antibodies from 30 providers.
DR   DNASU; 12728; -.
DR   Ensembl; ENSMUST00000004428; ENSMUSP00000004428; ENSMUSG00000004317. [Q9WVD4-2]
DR   Ensembl; ENSMUST00000115746; ENSMUSP00000111412; ENSMUSG00000004317. [Q9WVD4-1]
DR   GeneID; 12728; -.
DR   KEGG; mmu:12728; -.
DR   UCSC; uc009sle.3; mouse. [Q9WVD4-1]
DR   UCSC; uc029xhv.1; mouse.
DR   CTD; 1184; -.
DR   MGI; MGI:99486; Clcn5.
DR   VEuPathDB; HostDB:ENSMUSG00000004317; -.
DR   eggNOG; KOG0475; Eukaryota.
DR   GeneTree; ENSGT00940000153763; -.
DR   HOGENOM; CLU_003181_2_1_1; -.
DR   InParanoid; Q9WVD4; -.
DR   OMA; CLDWTPW; -.
DR   OrthoDB; 271925at2759; -.
DR   PhylomeDB; Q9WVD4; -.
DR   TreeFam; TF313867; -.
DR   Reactome; R-MMU-2672351; Stimuli-sensing channels.
DR   BioGRID-ORCS; 12728; 5 hits in 71 CRISPR screens.
DR   ChiTaRS; Clcn5; mouse.
DR   PRO; PR:Q9WVD4; -.
DR   Proteomes; UP000000589; Chromosome X.
DR   RNAct; Q9WVD4; protein.
DR   Bgee; ENSMUSG00000004317; Expressed in internal carotid artery and 229 other tissues.
DR   ExpressionAtlas; Q9WVD4; baseline and differential.
DR   Genevisible; Q9WVD4; MM.
DR   GO; GO:0045177; C:apical part of cell; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005769; C:early endosome; IBA:GO_Central.
DR   GO; GO:0005768; C:endosome; IDA:MGI.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0008021; C:synaptic vesicle; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005254; F:chloride channel activity; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0015299; F:solute:proton antiporter activity; IBA:GO_Central.
DR   GO; GO:0005247; F:voltage-gated chloride channel activity; ISO:MGI.
DR   GO; GO:0006821; P:chloride transport; ISO:MGI.
DR   GO; GO:0006897; P:endocytosis; IMP:MGI.
DR   GO; GO:0003014; P:renal system process; ISO:MGI.
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   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; SSF54631; 1.
DR   SUPFAM; SSF81340; SSF81340; 1.
DR   PROSITE; PS51371; CBS; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; Antiport; ATP-binding; CBS domain; Cell membrane;
KW   Chloride; Endosome; Golgi apparatus; Ion transport; Membrane;
KW   Nucleotide-binding; Reference proteome; Repeat; Transmembrane;
KW   Transmembrane helix; Transport; Ubl conjugation.
FT   CHAIN           1..816
FT                   /note="H(+)/Cl(-) exchange transporter 5"
FT                   /id="PRO_0000094447"
FT   TOPO_DOM        1..124
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        125..162
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        208..231
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   INTRAMEM        240..247
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        256..275
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        281..300
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   INTRAMEM        312..324
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   INTRAMEM        328..336
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        348..366
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        389..414
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        422..442
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        498..518
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        523..542
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   INTRAMEM        570..584
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   INTRAMEM        585..587
FT                   /note="Note=Loop between two helices"
FT                   /evidence="ECO:0000250"
FT   INTRAMEM        588..599
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   INTRAMEM        600..604
FT                   /note="Note=Loop between two helices"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        605..622
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        623..816
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   DOMAIN          656..720
FT                   /note="CBS 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT   DOMAIN          752..812
FT                   /note="CBS 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT   MOTIF           237..241
FT                   /note="Selectivity filter part_1"
FT                   /evidence="ECO:0000250"
FT   MOTIF           279..283
FT                   /note="Selectivity filter part_2"
FT                   /evidence="ECO:0000250"
FT   MOTIF           523..527
FT                   /note="Selectivity filter part_3"
FT                   /evidence="ECO:0000250"
FT   BINDING         238
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /evidence="ECO:0000250"
FT   BINDING         525
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /evidence="ECO:0000250"
FT   BINDING         628
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /evidence="ECO:0000250"
FT   BINDING         666
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P51795"
FT   BINDING         687..689
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P51795"
FT   BINDING         794..797
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P51795"
FT   SITE            281
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            338
FT                   /note="Mediates proton transfer from the protein to the
FT                   inner aqueous phase"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         1..70
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_060655"
SQ   SEQUENCE   816 AA;  90706 MW;  76912EA72BD0942F CRC64;
     MAMWQGAMDN RGFHQGSFSS FQSSSSDEDL MDIPGTAMDF SMRDDVPPLD REIEGNKSYN
     GGGIGSSNRV MDFLEEPIPG VGTYDDFNTI DWVREKSRDR DRHREITNKS KESTWALIHS
     VSDAFSGWLL MLLIGLLSGS LAGLIDISAH WMTDLKEGIC TGGFWFNHEH CCWNSEHVTF
     EHRDKCPEWN SWAQLIINTD QGAFAYIVNY FMYVLWALLF AFLAVSLVKA FAPYACGSGI
     PEIKTILSGF IIRGYLGKWT LVIKTITLVL AVSSGLSLGK EGPLVHVACC CGNILCHCFN
     KYRKNEAKRR EVLSAAAAAG VSVAFGAPIG GVLFSLEEVS YYFPLKTLWR SFFAALVAAF
     TLRSINPFGN SRLVLFYVEF HTPWHLFELV PFIVLGIFGG LWGALFIRTN IAWCRKRKTT
     QLGKYPVVEV LIVTAITAIL AFPNEYTRMS TSELISELFN DCGLLDSSKL CDYENHFNTS
     KGGELPDRPA GVGIYSAMWQ LALTLILKIV ITIFTFGMKI PSGLFIPSMA VGAIAGRLLG
     VGMEQLAYYH HDWGIFNSWC SQGADCITPG LYAMVGAAAC LGGVTRMTVS LVVIMFELTG
     GLEYIVPLMA AAMTSKWVAD ALGREGIYDA HIRLNGYPFL EAKEEFAHKT LAMDVMKPRR
     NDPLLTVLTQ DSMTVEDVET IISETTYSGF PVVVSRESQR LVGFVLRRDL IISIENARKK
     QDGVVSTSII YFTEHSPPMP PYTPPTLKLR NILDLSPFTV TDLTPMEIVV DIFRKLGLRQ
     CLVTHNGRLL GIITKKDVLK HIAQMANQDP DSILFN
 
 
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