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CLCN2_RABIT
ID   CLCN2_RABIT             Reviewed;         898 AA.
AC   P51789;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Chloride channel protein 2;
DE            Short=ClC-2;
DE   AltName: Full=PKA-activated chloride channel;
GN   Name=CLCN2;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=New Zealand white; TISSUE=Gastric mucosa;
RX   PubMed=7840147; DOI=10.1152/ajpcell.1995.268.1.c191;
RA   Malinowska D.H., Kupert E.Y., Bahinski A., Sherry A.M., Cuppoletti J.;
RT   "Cloning, functional expression, and characterization of a PKA-activated
RT   gastric Cl-channel.";
RL   Am. J. Physiol. 268:C191-C200(1995).
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: Ubiquitously expressed.
CC   -!- PTM: Phosphorylated. Activated by dephosphorylation.
CC       {ECO:0000250|UniProtKB:P35525}.
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; U15652; AAB05937.1; -; mRNA.
DR   RefSeq; NP_001076220.1; NM_001082751.1.
DR   AlphaFoldDB; P51789; -.
DR   SMR; P51789; -.
DR   STRING; 9986.ENSOCUP00000006115; -.
DR   PRIDE; P51789; -.
DR   Ensembl; ENSOCUT00000007070; ENSOCUP00000006115; ENSOCUG00000007065.
DR   GeneID; 100009530; -.
DR   KEGG; ocu:100009530; -.
DR   CTD; 1181; -.
DR   eggNOG; KOG0476; Eukaryota.
DR   GeneTree; ENSGT00940000155439; -.
DR   HOGENOM; CLU_006904_0_1_1; -.
DR   InParanoid; P51789; -.
DR   OMA; ACFMFNN; -.
DR   OrthoDB; 1131873at2759; -.
DR   Proteomes; UP000001811; Chromosome 14.
DR   Bgee; ENSOCUG00000007065; Expressed in testis and 18 other tissues.
DR   GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005247; F:voltage-gated chloride channel activity; ISS:UniProtKB.
DR   GO; GO:0090425; P:acinar cell differentiation; IEA:Ensembl.
DR   GO; GO:0060689; P:cell differentiation involved in salivary gland development; IEA:Ensembl.
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; IEA:Ensembl.
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   2: Evidence at transcript 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..898
FT                   /note="Chloride channel protein 2"
FT                   /id="PRO_0000094435"
FT   TOPO_DOM        1..90
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        91..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        133..158
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   INTRAMEM        167..174
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        183..201
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        208..226
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   INTRAMEM        242..254
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   INTRAMEM        258..266
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        278..298
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        324..352
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        361..380
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        432..452
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        460..483
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   INTRAMEM        500..514
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   INTRAMEM        515..516
FT                   /note="Note=Loop between two helices"
FT                   /evidence="ECO:0000250"
FT   INTRAMEM        517..528
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   INTRAMEM        529..533
FT                   /note="Note=Loop between two helices"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        534..551
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        552..898
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   DOMAIN          587..645
FT                   /note="CBS 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT   DOMAIN          790..850
FT                   /note="CBS 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT   REGION          647..675
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          726..766
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          856..898
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           164..168
FT                   /note="Selectivity filter part_1"
FT                   /evidence="ECO:0000250"
FT   MOTIF           206..210
FT                   /note="Selectivity filter part_2"
FT                   /evidence="ECO:0000250"
FT   MOTIF           460..464
FT                   /note="Selectivity filter part_3"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        657..675
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        738..758
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        857..871
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         23
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9R0A1"
FT   MOD_RES         710
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P51788"
FT   MOD_RES         758
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P35525"
SQ   SEQUENCE   898 AA;  98547 MW;  0F84B41123395D33 CRC64;
     MAAPAAAAVE EGMEPRALQY EQTLMYGRYT QDLGAFAKEE AARIRLGGPE PWRSPPSPRT
     PPELLEYGQS RCARCRMCSV RCHKFLVSRV GEDWIFLVLL GLLMALVSWA MDYAIAACLQ
     AQQWMSRGLN TNLLLQYLAW VTYPVVLITF SAGFTQILAP QAVGSGIPEM KTILRGVVLK
     EYLTLKTFVA KVIGLTCALG SGMPLGKEGP FVHIASMCAA LLSKFLSLFG GIYENESRNT
     EMLAAACAVG VGCCFAAPIG GVLFSIEVTS TFFAVRNYWR GFFAATFSAF IFRVLAVWNR
     DEETITALFK TRFRLDFPFD LQELPAFAVI GIASGFGGAL FVYLNRKIVQ VMRKQKTINR
     FLMRKRLLFP ALVTLLISTL TFPPGFGQFM AGQLSQKETL VTLFDNRTWV RQGLVEELEP
     PSTSQAWSPP RANVFLTLVI FILMKFWMSA LATTIPVPCG AFMPVFVIGA AFGRLVGESM
     AAWFPDGIHT DSSTYRIVPG GYAVVGAAAL AGAVTHTVST AVIVFELTGQ IAHILPVMIA
     VILANAVAQS LQPSLYDSII RIKKLPYLPE LGWGRHQQYR VRVEDIMVRD VPHVALSCTF
     RDLRLALHRT KGRTLALVES PESMILLGSI ERTQVVALLA AQLSPARRRQ SKQKRRVAHT
     SPPSCQESPP SPETSVCFQV KAEDAQGEPH KPLKPALKRG CSNSVNLGES PTGHVESAGI
     ALRSLFCGSP PPEAASESEK SESSEKRKSK RVRISLASDS DLEGEMSPEE ILEWEEQQLD
     EPVNFSDCKI DPAPFQLVER TSLHKTHTIF SLLGVDHAYV TSIGRLIGIV TLKELRKAIE
     GSVTAQGVKV RPPLASFRDS ATSSSDTETT EVHALWGPRS RHGLPREGSP SDSDDKCQ
 
 
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