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CLCN2_MOUSE
ID   CLCN2_MOUSE             Reviewed;         908 AA.
AC   Q9R0A1; Q0VBC2; Q9WUJ9;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   03-AUG-2022, entry version 170.
DE   RecName: Full=Chloride channel protein 2;
DE            Short=ClC-2;
GN   Name=Clcn2; Synonyms=Clc2;
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].
RC   STRAIN=C57BL/6J; TISSUE=Duodenal mucosa;
RX   PubMed=10524221; DOI=10.1016/s0167-4781(99)00110-4;
RA   Joo N.S., Clarke L.L., Han B.H., Forte L.R., Kim H.D.;
RT   "Cloning of ClC-2 chloride channel from murine duodenum and its presence in
RT   CFTR knockout mice.";
RL   Biochim. Biophys. Acta 1446:431-437(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=FVB/N;
RA   Hathaway J.K., Rice W.R., Wert S., Whitsett J.A.;
RT   "CFTR and ClC-2 expression levels in the fetal mouse lung.";
RL   Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-28, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Spleen, and Testis;
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).
RN   [6]
RP   TISSUE SPECIFICITY.
RX   PubMed=29403011; DOI=10.1038/s41588-018-0048-5;
RA   Scholl U.I., Stoelting G., Schewe J., Thiel A., Tan H., Nelson-Williams C.,
RA   Vichot A.A., Jin S.C., Loring E., Untiet V., Yoo T., Choi J., Xu S., Wu A.,
RA   Kirchner M., Mertins P., Rump L.C., Onder A.M., Gamble C., McKenney D.,
RA   Lash R.W., Jones D.P., Chune G., Gagliardi P., Choi M., Gordon R.,
RA   Stowasser M., Fahlke C., Lifton R.P.;
RT   "CLCN2 chloride channel mutations in familial hyperaldosteronism type II.";
RL   Nat. Genet. 50:349-354(2018).
RN   [7]
RP   TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=29403012; DOI=10.1038/s41588-018-0053-8;
RA   Fernandes-Rosa F.L., Daniil G., Orozco I.J., Goeppner C., El Zein R.,
RA   Jain V., Boulkroun S., Jeunemaitre X., Amar L., Lefebvre H.,
RA   Schwarzmayr T., Strom T.M., Jentsch T.J., Zennaro M.C.;
RT   "A gain-of-function mutation in the CLCN2 chloride channel gene causes
RT   primary aldosteronism.";
RL   Nat. Genet. 50:355-361(2018).
CC   -!- FUNCTION: Voltage-gated chloride channel. Chloride channels have
CC       several functions including the regulation of cell volume, membrane
CC       potential stabilization, signal transduction and transepithelial
CC       transport (By similarity). Involved in the regulation of aldosterone
CC       production. The opening of CLCN2 channels at hyperpolarized membrane
CC       potentials in the glomerulosa causes cell membrane depolarization,
CC       activation of voltage-gated Ca2+ channels and increased expression of
CC       aldosterone synthase, the rate-limiting enzyme for aldosterone
CC       biosynthesis (By similarity). {ECO:0000250|UniProtKB:P35525,
CC       ECO:0000250|UniProtKB:P51788}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P35525};
CC       Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Expressed in the adrenal gland and brain.
CC       {ECO:0000269|PubMed:29403011, ECO:0000269|PubMed:29403012}.
CC   -!- PTM: Phosphorylated. Activated by dephosphorylation.
CC       {ECO:0000250|UniProtKB:P35525}.
CC   -!- DISRUPTION PHENOTYPE: Hyperpolarization-activated chloride currents are
CC       absent in glomerulosa cells of knockout mice.
CC       {ECO:0000269|PubMed:29403012}.
CC   -!- MISCELLANEOUS: The CLC channel family contains both chloride channels
CC       and proton-coupled anion transporters that exchange chloride or another
CC       anion for protons. The absence of conserved gating glutamate residues
CC       is typical for family members that function as channels (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the chloride channel (TC 2.A.49) family. ClC-
CC       2/CLCN2 subfamily. {ECO:0000305}.
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DR   EMBL; AF097415; AAD50604.1; -; mRNA.
DR   EMBL; AF139724; AAD26466.1; -; mRNA.
DR   EMBL; AC087898; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CT010490; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC120699; AAI20700.1; -; mRNA.
DR   EMBL; BC137625; AAI37626.1; -; mRNA.
DR   CCDS; CCDS28057.1; -.
DR   RefSeq; NP_034030.2; NM_009900.2.
DR   AlphaFoldDB; Q9R0A1; -.
DR   SMR; Q9R0A1; -.
DR   BioGRID; 198735; 1.
DR   STRING; 10090.ENSMUSP00000007207; -.
DR   GlyConnect; 2209; 1 N-Linked glycan (1 site).
DR   GlyGen; Q9R0A1; 1 site, 1 N-linked glycan (1 site).
DR   iPTMnet; Q9R0A1; -.
DR   PhosphoSitePlus; Q9R0A1; -.
DR   SwissPalm; Q9R0A1; -.
DR   MaxQB; Q9R0A1; -.
DR   PaxDb; Q9R0A1; -.
DR   PRIDE; Q9R0A1; -.
DR   ProteomicsDB; 285479; -.
DR   Antibodypedia; 2994; 311 antibodies from 36 providers.
DR   DNASU; 12724; -.
DR   Ensembl; ENSMUST00000007207; ENSMUSP00000007207; ENSMUSG00000022843.
DR   GeneID; 12724; -.
DR   KEGG; mmu:12724; -.
DR   UCSC; uc012ada.1; mouse.
DR   CTD; 1181; -.
DR   MGI; MGI:105061; Clcn2.
DR   VEuPathDB; HostDB:ENSMUSG00000022843; -.
DR   eggNOG; KOG0476; Eukaryota.
DR   GeneTree; ENSGT00940000155439; -.
DR   HOGENOM; CLU_006904_0_1_1; -.
DR   InParanoid; Q9R0A1; -.
DR   OMA; ACFMFNN; -.
DR   OrthoDB; 1131873at2759; -.
DR   PhylomeDB; Q9R0A1; -.
DR   TreeFam; TF300522; -.
DR   Reactome; R-MMU-2672351; Stimuli-sensing channels.
DR   BioGRID-ORCS; 12724; 0 hits in 74 CRISPR screens.
DR   PRO; PR:Q9R0A1; -.
DR   Proteomes; UP000000589; Chromosome 16.
DR   RNAct; Q9R0A1; protein.
DR   Bgee; ENSMUSG00000022843; Expressed in dorsal pancreas and 209 other tissues.
DR   ExpressionAtlas; Q9R0A1; baseline and differential.
DR   Genevisible; Q9R0A1; MM.
DR   GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR   GO; GO:0030425; C:dendrite; ISO:MGI.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0043204; C:perikaryon; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005247; F:voltage-gated chloride channel activity; IMP:MGI.
DR   GO; GO:0090425; P:acinar cell differentiation; IMP:MGI.
DR   GO; GO:0060689; P:cell differentiation involved in salivary gland development; IMP:MGI.
DR   GO; GO:0006821; P:chloride transport; ISO:MGI.
DR   GO; GO:0030324; P:lung development; ISO:MGI.
DR   GO; GO:0032347; P:regulation of aldosterone biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR   GO; GO:0060041; P:retina development in camera-type eye; IMP:MGI.
DR   Gene3D; 3.10.580.10; -; 2.
DR   InterPro; IPR046342; CBS_dom_sf.
DR   InterPro; IPR002244; Cl-channel-2.
DR   InterPro; IPR014743; Cl-channel_core.
DR   InterPro; IPR001807; Cl-channel_volt-gated.
DR   Pfam; PF00654; Voltage_CLC; 1.
DR   PRINTS; PR00762; CLCHANNEL.
DR   PRINTS; PR01113; CLCHANNEL2.
DR   SUPFAM; SSF54631; SSF54631; 1.
DR   SUPFAM; SSF81340; SSF81340; 1.
DR   PROSITE; PS51371; CBS; 2.
PE   1: Evidence at protein level;
KW   CBS domain; Cell membrane; Chloride; Chloride channel; Ion channel;
KW   Ion transport; Membrane; Phosphoprotein; Reference proteome; Repeat;
KW   Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN           1..908
FT                   /note="Chloride channel protein 2"
FT                   /id="PRO_0000094434"
FT   TOPO_DOM        1..95
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        96..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        138..163
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   INTRAMEM        172..179
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        188..206
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        213..231
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   INTRAMEM        247..259
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   INTRAMEM        263..271
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        283..303
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        329..357
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        366..385
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        437..457
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        465..488
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   INTRAMEM        505..519
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   INTRAMEM        520..521
FT                   /note="Note=Loop between two helices"
FT                   /evidence="ECO:0000250"
FT   INTRAMEM        522..533
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   INTRAMEM        534..538
FT                   /note="Note=Loop between two helices"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        539..556
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        557..908
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   DOMAIN          592..650
FT                   /note="CBS 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT   DOMAIN          800..860
FT                   /note="CBS 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT   REGION          653..722
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          866..908
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           169..173
FT                   /note="Selectivity filter part_1"
FT                   /evidence="ECO:0000250"
FT   MOTIF           211..215
FT                   /note="Selectivity filter part_2"
FT                   /evidence="ECO:0000250"
FT   MOTIF           465..469
FT                   /note="Selectivity filter part_3"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        662..694
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        867..881
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         170
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /evidence="ECO:0000250"
FT   BINDING         467
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /evidence="ECO:0000250"
FT   BINDING         561
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         28
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         768
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P35525"
FT   CONFLICT        667
FT                   /note="P -> S (in Ref. 1; AAD50604)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   908 AA;  99447 MW;  6CF58033B60CA578 CRC64;
     MAAATAAAAA AAAAGEGMEP RALQYEQTLM YGRYTQELGA FAKEEAARIR LGGPEPWKGS
     PSARATPELL EYGQSRCARC RICSVRCHKF LVSRVGEDWI FLVLLGLLMA LVSWAMDYAI
     AVCLQAQQWM SRGLNTNILL QYLAWVTYPV VLITFSAGFT QILAPQAVGS GIPEMKTILR
     GVVLKEYLTL KTFVAKVIGL TCALGSGMPL GKEGPFVHIA SMCAALLSKF LSLFGGIYEH
     ESRNTEMLAA ACAVGVGCCF AAPIGGVLFS IEVTSTFFAV RNYWRGFFAA TFSAFIFRVL
     AVWNRDEETI TALFKTRFRL DFPFDLQELP AFAVIGIASG FGGALFVYLN RKIVQVMRKQ
     KTINRFLMRK RLLFPALVTL LISTLTFPPG FGQFMAGQLS QKETLVTLFD NRTWVRQGLV
     EDLELPSTSQ AWSPPRANVF LTLVIFILMK FWMSALATTI PVPCGAFMPV FVIGAAFGRL
     VGESMAAWFP DGIHTDSSTY RIVPGGYAVV GAAALAGAVT HTVSTAVIVF ELTGQIAHIL
     PVMIAVILAN AVAQSLQPSL YDSIIRIKKL PYLPELGWGR HQQYRVRVED IMVRDVPHVA
     LSCTFRDLRL ALHRTKGRML ALVESPESMI LLGSIERSQV VALLGAQLSP ARRRQHMQKL
     RKAQLSPPSD QESPPSSETS IRFQVNTEDS GFSGAHGQTH KPLKPALKRG PSNSTSLQEG
     TTGNMESAGI ALRSLFCGSP PLEATSELEK SESCDKRKLK RVRISLASDS DPEAEMSPEE
     ILEWEEQQLD EPVNFSDCKI DPAPFQLVER TSLHKTHTIF SLLGVDHAYV TSIGRLIGIV
     TLKELRKAIE GSVTAQGVKV RPPLASFRDS ATSSSDTETT EVHALWGPRS RHGLPREGTP
     SDSDDKCQ
 
 
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