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CLCN2_RAT
ID   CLCN2_RAT               Reviewed;         907 AA.
AC   P35525;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 164.
DE   RecName: Full=Chloride channel protein 2;
DE            Short=ClC-2;
GN   Name=Clcn2;
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], AND FUNCTION.
RC   TISSUE=Brain;
RX   PubMed=1311421; DOI=10.1038/356057a0;
RA   Thiemann A., Gruender S., Pusch M., Jentsch T.J.;
RT   "A chloride channel widely expressed in epithelial and non-epithelial
RT   cells.";
RL   Nature 356:57-60(1992).
RN   [2]
RP   FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AND DEPHOSPHORYLATION.
RX   PubMed=12163466; DOI=10.1083/jcb.200204142;
RA   Rutledge E., Denton J., Strange K.;
RT   "Cell cycle- and swelling-induced activation of a Caenorhabditis elegans
RT   ClC channel is mediated by CeGLC-7alpha/beta phosphatases.";
RL   J. Cell Biol. 158:435-444(2002).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-767, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Voltage-gated chloride channel (PubMed:1311421,
CC       PubMed:12163466). Chloride channels have several functions including
CC       the regulation of cell volume; membrane potential stabilization, signal
CC       transduction and transepithelial transport (PubMed:1311421). Involved
CC       in the regulation of aldosterone production. The opening of CLCN2
CC       channels at hyperpolarized membrane potentials in the glomerulosa
CC       causes cell membrane depolarization, activation of voltage-gated Ca2+
CC       channels and increased expression of aldosterone synthase, the rate-
CC       limiting enzyme for aldosterone biosynthesis (By similarity).
CC       {ECO:0000250|UniProtKB:P51788, ECO:0000269|PubMed:12163466,
CC       ECO:0000269|PubMed:1311421}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255,
CC       ECO:0000269|PubMed:12163466}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC   -!- PTM: Phosphorylated. Activated by dephosphorylation.
CC       {ECO:0000269|PubMed:12163466}.
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; X64139; CAA45500.1; -; mRNA.
DR   PIR; S23399; S23399.
DR   RefSeq; NP_058833.1; NM_017137.1.
DR   RefSeq; XP_006248624.1; XM_006248562.3.
DR   AlphaFoldDB; P35525; -.
DR   SMR; P35525; -.
DR   CORUM; P35525; -.
DR   STRING; 10116.ENSRNOP00000050925; -.
DR   TCDB; 2.A.49.2.6; the chloride carrier/channel (clc) family.
DR   iPTMnet; P35525; -.
DR   PhosphoSitePlus; P35525; -.
DR   PaxDb; P35525; -.
DR   Ensembl; ENSRNOT00000050927; ENSRNOP00000050925; ENSRNOG00000001742.
DR   GeneID; 29232; -.
DR   KEGG; rno:29232; -.
DR   CTD; 1181; -.
DR   RGD; 2361; Clcn2.
DR   eggNOG; KOG0476; Eukaryota.
DR   GeneTree; ENSGT00940000155439; -.
DR   InParanoid; P35525; -.
DR   OMA; ACFMFNN; -.
DR   OrthoDB; 1131873at2759; -.
DR   PhylomeDB; P35525; -.
DR   TreeFam; TF300522; -.
DR   Reactome; R-RNO-2672351; Stimuli-sensing channels.
DR   PRO; PR:P35525; -.
DR   Proteomes; UP000002494; Chromosome 11.
DR   Bgee; ENSRNOG00000001742; Expressed in duodenum and 17 other tissues.
DR   ExpressionAtlas; P35525; baseline.
DR   Genevisible; P35525; RN.
DR   GO; GO:0015629; C:actin cytoskeleton; ISS:UniProtKB.
DR   GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR   GO; GO:0030425; C:dendrite; IDA:RGD.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0043204; C:perikaryon; IDA:RGD.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005247; F:voltage-gated chloride channel activity; IDA:RGD.
DR   GO; GO:0090425; P:acinar cell differentiation; IEA:Ensembl.
DR   GO; GO:0060689; P:cell differentiation involved in salivary gland development; ISO:RGD.
DR   GO; GO:0006821; P:chloride transport; IDA:RGD.
DR   GO; GO:0030324; P:lung development; IMP:RGD.
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; ISO:RGD.
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..907
FT                   /note="Chloride channel protein 2"
FT                   /id="PRO_0000094436"
FT   TOPO_DOM        1..93
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        94..127
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        136..161
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   INTRAMEM        170..177
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        186..204
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        211..229
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   INTRAMEM        245..257
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   INTRAMEM        261..269
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        281..301
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        327..355
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        364..383
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        435..455
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        463..486
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   INTRAMEM        503..517
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   INTRAMEM        518..519
FT                   /note="Note=Loop between two helices"
FT                   /evidence="ECO:0000250"
FT   INTRAMEM        520..531
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   INTRAMEM        532..536
FT                   /note="Note=Loop between two helices"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        537..554
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        555..907
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   DOMAIN          590..648
FT                   /note="CBS 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT   DOMAIN          799..859
FT                   /note="CBS 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT   REGION          650..720
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          865..907
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           167..171
FT                   /note="Selectivity filter part_1"
FT                   /evidence="ECO:0000250"
FT   MOTIF           209..213
FT                   /note="Selectivity filter part_2"
FT                   /evidence="ECO:0000250"
FT   MOTIF           463..467
FT                   /note="Selectivity filter part_3"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        660..691
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        866..880
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         26
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9R0A1"
FT   MOD_RES         767
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
SQ   SEQUENCE   907 AA;  99328 MW;  6192EEB2EE0D6528 CRC64;
     MAAATAAAAT VAGEGMEPRA LQYEQTLMYG RYTQELGAFA KEEAARIRLG GPEPWKGSPS
     ARATPELLEY GQSRCARCRI CSVRCHKFLV SRVGEDWIFL VLLGLLMALV SWAMDYAIAV
     CLQAQQWMSR GLNTNILLQY LAWVTYPVVL ITFSAGFTQI LAPQAVGSGI PEMKTILRGV
     VLKEYLTLKT FVAKVIGLTC ALGSGMPLGK EGPFVHIASM CAALLSKFLS LFGGIYENES
     RNTEMLAAAC AVGVGCCFAA PIGGVLFSIE VTSTFFAVRN YWRGFFAATF SAFIFRVLAV
     WNRDEETITA LFKTRFRLDF PFDLQELPAF AVIGIASGFG GALFVYLNRK IVQVMRKQKT
     INRFLMKKRL LFPALVTLLI STLTFPPGFG QFMAGQLSQK ETLVTLFDNR TWVRQGLVED
     LGAPSTSQAW SPPRANVFLT LVIFILMKFW MSALATTIPV PCGAFMPVFV IGAAFGRLVG
     ESMAAWFPDG IHTDSSTYRI VPGGYAVVGA AALAGAVTHT VSTAVIVFEL TGQIAHILPV
     MIAVILANAV AQSLQPSLYD SIIRIKKLPY LPELGWGRHQ QYRVRVEDIM VRDVPHVALS
     CTFRDLRLAL HRTKGRMLAL VESPESMILL GSIERSQVVA LLGAQLSPAR RRQHMQKLRK
     AQMSPPSDQE SPPSSETSIR FQVNTEDSGF PGAHGQTHKP LKPALKRGPS NATSLQEGTT
     GNMESAGIAL RSLFCGSPPL ESTTSELEKS ESCDKRKLKR VRISLASDSD LEGKMSPEEI
     LEWEEQQLDE PVNFSDCKID PAPFQLVERT SLHKTHTIFS LLGVDHAYVT SIGRLIGIVT
     LKELRKAIEG SVTAQGVKVR PPLASFRDSA TSSSDTETTE VHALWGPRSR HGLPREGTPS
     DSDDKCQ
 
 
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