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CLH3_CAEEL
ID   CLH3_CAEEL              Reviewed;        1001 AA.
AC   Q9BMK9; Q7KKH7;
DT   24-JUN-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=Chloride channel protein clh-3 {ECO:0000305};
GN   Name=clh-3 {ECO:0000312|WormBase:E04F6.11a};
GN   Synonyms=clc-3 {ECO:0000312|WormBase:E04F6.11a};
GN   ORFNames=E04F6.11 {ECO:0000312|WormBase:E04F6.11a};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN   [1] {ECO:0000312|EMBL:AAF13165.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), FUNCTION, SUBCELLULAR LOCATION, AND
RP   TISSUE SPECIFICITY.
RC   STRAIN=Bristol N2 {ECO:0000312|EMBL:AAF13165.1};
RX   PubMed=10567397; DOI=10.1074/jbc.274.48.34238;
RA   Schriever A.M., Friedrich T., Pusch M., Jentsch T.J.;
RT   "CLC chloride channels in Caenorhabditis elegans.";
RL   J. Biol. Chem. 274:34238-34244(1999).
RN   [2] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, SUBCELLULAR LOCATION, AND
RP   TISSUE SPECIFICITY.
RX   PubMed=11078724; DOI=10.1152/ajpcell.2000.279.6.c2052;
RA   Nehrke K., Begenisich T., Pilato J., Melvin J.E.;
RT   "Into ion channel and transporter function. Caenorhabditis elegans ClC-type
RT   chloride channels: novel variants and functional expression.";
RL   Am. J. Physiol. 279:C2052-2066(2000).
RN   [3] {ECO:0000312|Proteomes:UP000001940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [4] {ECO:0000305}
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=11231150; DOI=10.1016/s0960-9822(01)00051-3;
RA   Rutledge E., Bianchi L., Christensen M., Boehmer C., Morrison R.,
RA   Broslat A., Beld A.M., George A.L., Greenstein D., Strange K.;
RT   "CLH-3, a ClC-2 anion channel ortholog activated during meiotic maturation
RT   in C. elegans oocytes.";
RL   Curr. Biol. 11:161-170(2001).
RN   [5] {ECO:0000305}
RP   FUNCTION, SUBCELLULAR LOCATION, AND DEPHOSPHORYLATION BY GSP-1/2.
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   [6] {ECO:0000305}
RP   FUNCTION, ACTIVATION MECHANISM, AND SUBCELLULAR LOCATION.
RX   PubMed=14565992; DOI=10.1113/jphysiol.2003.053165;
RA   Denton J., Nehrke K., Rutledge E., Morrison R., Strange K.;
RT   "Alternative splicing of N- and C-termini of a C. elegans ClC channel
RT   alters gating and sensitivity to external Cl- and H+.";
RL   J. Physiol. (Lond.) 555:97-114(2004).
RN   [7] {ECO:0000305}
RP   FUNCTION, INTERACTION WITH GCK-3, AND SUBCELLULAR LOCATION.
RX   PubMed=15684092; DOI=10.1085/jgp.200409215;
RA   Denton J., Nehrke K., Yin X., Morrison R., Strange K.;
RT   "GCK-3, a newly identified Ste20 kinase, binds to and regulates the
RT   activity of a cell cycle-dependent ClC anion channel.";
RL   J. Gen. Physiol. 125:113-125(2005).
RN   [8] {ECO:0000305}
RP   FUNCTION, ACTIVATION MECHANISM, SUBCELLULAR LOCATION, DOMAIN, AND
RP   MUTAGENESIS OF GLU-167.
RX   PubMed=16500974; DOI=10.1529/biophysj.105.078295;
RA   He L., Denton J., Nehrke K., Strange K.;
RT   "Carboxy terminus splice variation alters ClC channel gating and
RT   extracellular cysteine reactivity.";
RL   Biophys. J. 90:3570-3581(2006).
RN   [9] {ECO:0000305}
RP   FUNCTION.
RX   PubMed=18049475; DOI=10.1038/sj.embor.7401128;
RA   Hisamoto N., Moriguchi T., Urushiyama S., Mitani S., Shibuya H.,
RA   Matsumoto K.;
RT   "Caenorhabditis elegans WNK-STE20 pathway regulates tube formation by
RT   modulating ClC channel activity.";
RL   EMBO Rep. 9:70-75(2008).
RN   [10] {ECO:0000305}
RP   SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-742 AND SER-747,
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND MUTAGENESIS OF SER-742; THR-744
RP   AND SER-747.
RX   PubMed=19088383; DOI=10.1085/jgp.200810080;
RA   Falin R.A., Morrison R., Ham A.J., Strange K.;
RT   "Identification of regulatory phosphorylation sites in a cell volume- and
RT   Ste20 kinase-dependent ClC anion channel.";
RL   J. Gen. Physiol. 133:29-42(2009).
RN   [11] {ECO:0000305}
RP   SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF GLU-167; PHE-559; LEU-833;
RP   ALA-836 AND ILE-837.
RX   PubMed=20581474; DOI=10.4161/chan.4.4.12445;
RA   Dave S., Sheehan J.H., Meiler J., Strange K.;
RT   "Unique gating properties of C. elegans ClC anion channel splice variants
RT   are determined by altered CBS domain conformation and the R-helix linker.";
RL   Channels 4:289-301(2010).
RN   [12] {ECO:0000305}
RP   SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF TYR-232; SER-742; SER-747
RP   AND HIS-805.
RX   PubMed=23083714; DOI=10.1016/j.bpj.2012.09.001;
RA   Miyazaki H., Yamada T., Parton A., Morrison R., Kim S., Beth A.H.,
RA   Strange K.;
RT   "CLC anion channel regulatory phosphorylation and conserved signal
RT   transduction domains.";
RL   Biophys. J. 103:1706-1718(2012).
RN   [13] {ECO:0000305}
RP   FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF VAL-495.
RX   PubMed=24431435; DOI=10.1523/jneurosci.3112-13.2014;
RA   Branicky R., Miyazaki H., Strange K., Schafer W.R.;
RT   "The voltage-gated anion channels encoded by clh-3 regulate egg laying in
RT   C. elegans by modulating motor neuron excitability.";
RL   J. Neurosci. 34:764-775(2014).
CC   -!- FUNCTION: [Isoform a]: Voltage-gated chloride channel (PubMed:10567397,
CC       PubMed:11078724, PubMed:11231150, PubMed:12163466, PubMed:15684092).
CC       Insensitive to depolarizing conditioning voltages, requires low
CC       voltages for activation, insensitive to chloride levels and has a mild
CC       sensitivity to low pH. Channel gating properties are conferred by the
CC       cytoplasmic C-terminus (PubMed:14565992, PubMed:16500974). Plays a role
CC       in egg laying by modulating hermaphrodite-specific neurons (HSN)
CC       excitability and the ovulatory contractions of gap-junction-coupled
CC       gonadal sheath cells (PubMed:11231150, PubMed:24431435). When active,
CC       may prevent tubular formation of the excretory canals
CC       (PubMed:18049475). Activated during oocyte meiotic maturation and by
CC       membrane hyperpolarization and cell swelling (PubMed:11231150,
CC       PubMed:14565992). Inhibited by Zn(2+) and to a lesser extent by
CC       Cd(2+)(PubMed:11231150). {ECO:0000269|PubMed:10567397,
CC       ECO:0000269|PubMed:11078724, ECO:0000269|PubMed:11231150,
CC       ECO:0000269|PubMed:12163466, ECO:0000269|PubMed:14565992,
CC       ECO:0000269|PubMed:15684092, ECO:0000269|PubMed:16500974,
CC       ECO:0000269|PubMed:18049475, ECO:0000269|PubMed:24431435}.
CC   -!- FUNCTION: [Isoform b]: Voltage-gated chloride channel (PubMed:10567397,
CC       PubMed:11078724, PubMed:11231150). Sensitive to depolarizing
CC       conditioning voltages, requires stronger voltages for activation and
CC       activation is slower, is inhibited by low concentrations of chloride
CC       and is activated by low pH. Channel gating properties are conferred by
CC       the cytoplasmic C-terminus (PubMed:14565992, PubMed:16500974).
CC       {ECO:0000269|PubMed:10567397, ECO:0000269|PubMed:11078724,
CC       ECO:0000269|PubMed:11231150, ECO:0000269|PubMed:14565992,
CC       ECO:0000269|PubMed:16500974}.
CC   -!- SUBUNIT: Isoform a interacts (via RFLI motif) with gck-3 (via C-
CC       terminus). {ECO:0000269|PubMed:15684092}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10567397,
CC       ECO:0000269|PubMed:11078724, ECO:0000269|PubMed:11231150,
CC       ECO:0000269|PubMed:12163466, ECO:0000269|PubMed:14565992,
CC       ECO:0000269|PubMed:15684092, ECO:0000269|PubMed:16500974,
CC       ECO:0000269|PubMed:19088383, ECO:0000269|PubMed:20581474,
CC       ECO:0000269|PubMed:23083714, ECO:0000269|PubMed:24431435}; Multi-pass
CC       membrane protein {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=a {ECO:0000312|WormBase:E04F6.11a}; Synonyms=clh-3b
CC       {ECO:0000303|PubMed:10567397};
CC         IsoId=Q9BMK9-1; Sequence=Displayed;
CC       Name=b {ECO:0000312|EMBL:AAF13165.1}; Synonyms=clh-3a
CC       {ECO:0000303|PubMed:14565992};
CC         IsoId=Q9BMK9-2; Sequence=VSP_057741, VSP_057742, VSP_057743,
CC                                  VSP_057744;
CC   -!- TISSUE SPECIFICITY: Expressed in excretory cell, 4 anterior epithelial
CC       cells of the intestine, hermaphrodite-specific neurons and enteric
CC       muscles (PubMed:11078724, PubMed:10567397). Expressed also in vulva and
CC       uterus (PubMed:10567397). Isoform a is expressed in oocytes (at protein
CC       level) (PubMed:11231150). {ECO:0000269|PubMed:10567397,
CC       ECO:0000269|PubMed:11078724, ECO:0000269|PubMed:11231150}.
CC   -!- DOMAIN: The CBS domains, the R-helix linker (543-562) and the C-
CC       terminal domain (833-1001) regulate channel sensitivity to voltage, pH
CC       and extracellular chloride concentrations, probably by altering the
CC       outer pore structure (PubMed:16500974, PubMed:20581474). The region
CC       (738-751) between the CBS domains is essential for channel activation
CC       (PubMed:23083714). {ECO:0000269|PubMed:16500974,
CC       ECO:0000269|PubMed:20581474, ECO:0000269|PubMed:23083714}.
CC   -!- PTM: Phosphorylated by gck-3; phosphorylation at both Ser-742 and Ser-
CC       747 is required to inhibit channel activity (PubMed:19088383).
CC       Dephosphorylated by gsp-1/2 during cell swelling and oocyte meiotic
CC       maturation, which results in channel activation (PubMed:12163466).
CC       {ECO:0000269|PubMed:12163466, ECO:0000269|PubMed:19088383}.
CC   -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in oocytes results in
CC       inhibition of hyperpolarization-induced or swelling-induced current and
CC       in premature ovulatory contractions of gonadal sheath cells. Normal
CC       adaptive response to hypotonic swelling. {ECO:0000269|PubMed:11231150}.
CC   -!- SIMILARITY: Belongs to the chloride channel (TC 2.A.49) family.
CC       {ECO:0000305}.
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DR   EMBL; AF173172; AAF13165.1; -; mRNA.
DR   EMBL; AF319614; AAG49524.1; -; mRNA.
DR   EMBL; BX284602; CCD65907.1; -; Genomic_DNA.
DR   RefSeq; NP_001022060.1; NM_001026889.2. [Q9BMK9-1]
DR   AlphaFoldDB; Q9BMK9; -.
DR   SMR; Q9BMK9; -.
DR   STRING; 6239.E04F6.11a; -.
DR   ChEMBL; CHEMBL2268011; -.
DR   TCDB; 2.A.49.2.13; the chloride carrier/channel (clc) family.
DR   iPTMnet; Q9BMK9; -.
DR   PaxDb; Q9BMK9; -.
DR   PRIDE; Q9BMK9; -.
DR   EnsemblMetazoa; E04F6.11a.1; E04F6.11a.1; WBGene00000530. [Q9BMK9-1]
DR   EnsemblMetazoa; E04F6.11a.2; E04F6.11a.2; WBGene00000530. [Q9BMK9-1]
DR   EnsemblMetazoa; E04F6.11a.3; E04F6.11a.3; WBGene00000530. [Q9BMK9-1]
DR   EnsemblMetazoa; E04F6.11a.4; E04F6.11a.4; WBGene00000530. [Q9BMK9-1]
DR   GeneID; 174187; -.
DR   UCSC; E04F6.11a; c. elegans. [Q9BMK9-1]
DR   CTD; 174187; -.
DR   WormBase; E04F6.11a; CE27906; WBGene00000530; clh-3. [Q9BMK9-1]
DR   eggNOG; KOG0476; Eukaryota.
DR   GeneTree; ENSGT00940000168847; -.
DR   HOGENOM; CLU_006904_1_1_1; -.
DR   InParanoid; Q9BMK9; -.
DR   PhylomeDB; Q9BMK9; -.
DR   Reactome; R-CEL-2672351; Stimuli-sensing channels.
DR   PRO; PR:Q9BMK9; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00000530; Expressed in adult organism and 3 other tissues.
DR   ExpressionAtlas; Q9BMK9; baseline and differential.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IDA:WormBase.
DR   GO; GO:0005247; F:voltage-gated chloride channel activity; IDA:WormBase.
DR   GO; GO:1902476; P:chloride transmembrane transport; IDA:WormBase.
DR   GO; GO:0006821; P:chloride transport; IBA:GO_Central.
DR   Gene3D; 3.10.580.10; -; 2.
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   Pfam; PF00571; CBS; 1.
DR   Pfam; PF00654; Voltage_CLC; 1.
DR   PRINTS; PR00762; CLCHANNEL.
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; Cell membrane; Chloride; Coiled coil; Ion transport;
KW   Membrane; Phosphoprotein; Reference proteome; Repeat; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..1001
FT                   /note="Chloride channel protein clh-3"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000433362"
FT   TOPO_DOM        1..48
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        49..85
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        91..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   INTRAMEM        126..133
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        142..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        167..185
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   INTRAMEM        202..214
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   INTRAMEM        218..226
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        238..258
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        285..313
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        322..341
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        405..425
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        433..456
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   INTRAMEM        473..487
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   INTRAMEM        488..489
FT                   /note="Note=Loop between two helices"
FT                   /evidence="ECO:0000305"
FT   INTRAMEM        490..501
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   INTRAMEM        502..506
FT                   /note="Note=Loop between two helices"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        507..524
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        525..1001
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          560..619
FT                   /note="CBS 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT   DOMAIN          788..845
FT                   /note="CBS 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT   REGION          634..662
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          625..657
FT                   /evidence="ECO:0000255"
FT   MOTIF           123..127
FT                   /note="Selectivity filter part_1"
FT                   /evidence="ECO:0000250|UniProtKB:P37019"
FT   MOTIF           165..169
FT                   /note="Selectivity filter part_2"
FT                   /evidence="ECO:0000250|UniProtKB:P37019"
FT   MOTIF           433..437
FT                   /note="Selectivity filter part_3"
FT                   /evidence="ECO:0000250|UniProtKB:P37019"
FT   COMPBIAS        634..661
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         124
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /evidence="ECO:0000250|UniProtKB:P37019"
FT   BINDING         434
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /evidence="ECO:0000250|UniProtKB:P37019"
FT   BINDING         435
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /evidence="ECO:0000250|UniProtKB:P37019"
FT   BINDING         529
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /evidence="ECO:0000250|UniProtKB:P37019"
FT   SITE            232
FT                   /note="Essential for gck-3-mediated inhibition of channel
FT                   activity"
FT                   /evidence="ECO:0000269|PubMed:23083714"
FT   SITE            805
FT                   /note="Essential for gck-3-mediated inhibition of channel
FT                   activity"
FT                   /evidence="ECO:0000269|PubMed:23083714"
FT   MOD_RES         742
FT                   /note="Phosphoserine; by gck-3"
FT                   /evidence="ECO:0000269|PubMed:19088383"
FT   MOD_RES         747
FT                   /note="Phosphoserine; by gck-3"
FT                   /evidence="ECO:0000269|PubMed:19088383"
FT   VAR_SEQ         1
FT                   /note="M -> MPSRTPLSKIEWQSLLPLPPEKSEKDATIENNEELEKIRMPAGKEYD
FT                   LQPGSHLGVYKTVRGLPIDEDSKSM (in isoform b)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_057741"
FT   VAR_SEQ         669..770
FT                   /note="FLIVPVAKNGPQVAKNETLTGLSEENARKILTVEEKQALFDAASLATPKREM
FT                   SGKTINPVHIESHHTIGDIFRSITHLSFGRQNFPKKNNHNEFDLFGEERT -> Y (in
FT                   isoform b)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_057742"
FT   VAR_SEQ         833..841
FT                   /note="LRLAIEYLQ -> VCFLISRKK (in isoform b)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_057743"
FT   VAR_SEQ         842..1001
FT                   /note="Missing (in isoform b)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_057744"
FT   MUTAGEN         167
FT                   /note="E->A: Constitutive activation and loss of pH
FT                   sensitivity; in isoform a."
FT                   /evidence="ECO:0000269|PubMed:16500974"
FT   MUTAGEN         167
FT                   /note="E->A: Constitutive activation, loss of pH
FT                   sensitivity, loss of sensitivity to chloride levels and
FT                   conditioning depolarizing voltages; in isoform b."
FT                   /evidence="ECO:0000269|PubMed:16500974"
FT   MUTAGEN         167
FT                   /note="E->C: Increased sensitivity to MTSET-mediated
FT                   inhibition; in isoform a and isoform b. Inhibition is
FT                   slower; in isoform a. Reduced sensitivity to MTSET-mediated
FT                   inhibition; when associated with D-559; in isoform a."
FT                   /evidence="ECO:0000269|PubMed:16500974,
FT                   ECO:0000269|PubMed:19088383"
FT   MUTAGEN         232
FT                   /note="Y->A: Loss of gck-3-mediated inhibition."
FT                   /evidence="ECO:0000269|PubMed:23083714"
FT   MUTAGEN         495
FT                   /note="V->A: In n995; increase channel activity and
FT                   accumulation of eggs in the uterus resulting from a defect
FT                   in egg-laying. Reduced HSN activity. Reduced sensitivity to
FT                   gck-3-mediated inhibition; in isoform a."
FT                   /evidence="ECO:0000269|PubMed:24431435"
FT   MUTAGEN         559
FT                   /note="F->D: Confers similar gating properties to isoform
FT                   b; in isoform a. Reduced sensitivity to MTSET-mediated
FT                   inhibition; when associated with C-167; in isoform a."
FT                   /evidence="ECO:0000269|PubMed:20581474"
FT   MUTAGEN         742
FT                   /note="S->A: Constitutively active, loss of inhibition by
FT                   gck-3-mediated phosphorylation."
FT                   /evidence="ECO:0000269|PubMed:19088383"
FT   MUTAGEN         742
FT                   /note="S->E: Phosphomimetic mutant whose activity is
FT                   sensitive to gck-3-mediated inhibition and to cell
FT                   swelling-induced activation. Severe reduction in channel
FT                   activity, loss of cell swelling-induced activation; when
FT                   associated with E-747."
FT                   /evidence="ECO:0000269|PubMed:19088383,
FT                   ECO:0000269|PubMed:23083714"
FT   MUTAGEN         744
FT                   /note="T->A: No effect on activity."
FT                   /evidence="ECO:0000269|PubMed:19088383"
FT   MUTAGEN         747
FT                   /note="S->A: Constitutively active, loss of inhibition by
FT                   gck-3-mediated phosphorylation."
FT                   /evidence="ECO:0000269|PubMed:19088383"
FT   MUTAGEN         747
FT                   /note="S->E: Phosphomimetic mutant whose activity is
FT                   sensitive to gck-3-mediated inhibition but insensitive to
FT                   cell swelling-induced activation. Severe reduction in
FT                   channel activity, loss of cell swelling-induced activation;
FT                   when associated with E-742."
FT                   /evidence="ECO:0000269|PubMed:19088383,
FT                   ECO:0000269|PubMed:23083714"
FT   MUTAGEN         805
FT                   /note="H->A: Loss of gck-3-mediated inhibition."
FT                   /evidence="ECO:0000269|PubMed:23083714"
FT   MUTAGEN         833
FT                   /note="L->E: Confers similar gating properties to isoform
FT                   b; in isoform a."
FT                   /evidence="ECO:0000269|PubMed:20581474"
FT   MUTAGEN         836
FT                   /note="A->K: Confers similar gating properties to isoform
FT                   b; in isoform a."
FT                   /evidence="ECO:0000269|PubMed:20581474"
FT   MUTAGEN         837
FT                   /note="I->K: Confers similar gating properties to isoform
FT                   b; in isoform a."
FT                   /evidence="ECO:0000269|PubMed:20581474"
SQ   SEQUENCE   1001 AA;  110787 MW;  8C6F38A1703DE350 CRC64;
     MGIGTKILSK IEKNKTSDGL TIPLTPTTQK QSSSWCSFES IKTFFRTVIR DWIFLALLGF
     IMASLSFGMD YAILNLQNGQ MRLFDLVKEY HFTLAYLVWV GYVVGLILLS AVCAHYIAPQ
     AIGSGIPEMK TILRGVILKE YLSVRTLLSK MIGLTLSLGS GLPMGKEGPF VHVASVVASQ
     LTRLVHGSSG GIFENESRSG EMLAAGCAVG VACTFSAPIG GVLFSIEVTS VYFAVRNYWR
     GFFAATCSAT LFRILRMFSV SAAVTVEAHY QTNFPPQNVF LPQELPIFAL IGLVCGLAGS
     IFVYLHRRTV LFLRRNWLAK MIFQKYWLIY PIFIATFISS LSFPLGLGKF MGGEERFSHT
     MKEFFVDCAW TAPPNDSYAC PMPTSNATSS DSFDIRHWKG DNYDYSPFVT LSSFQVVYFF
     LAILASTLPV PSGIFMPVFV LGAAFGRLVG EGVFSLDPYG HISGDIQFFV RPGVYAVVGA
     AAFCGAVTHT VSVAVIVFEL TGQLCHLLPV MIAVLIANAV ASYLQPSIYD SIIRIKNLPY
     LPDIPHTTSL YHQMLIEQFM ISPLVYIAKD STVGDIKRAL ETKTRIRAFP LVENMESLAL
     VGSVSRSQLQ RYVDSQIGTK ARFAEATRRI KQRLEDEESE RKRREESKSD DTEDSLETTG
     AGERRASRFL IVPVAKNGPQ VAKNETLTGL SEENARKILT VEEKQALFDA ASLATPKREM
     SGKTINPVHI ESHHTIGDIF RSITHLSFGR QNFPKKNNHN EFDLFGEERT EWEDMMLNQK
     LDLSQLDIDS TPFQLSEYTS LFKAHSLFSL LGLNRAYVTK KGQLIGVVAL KELRLAIEYL
     QSGKVPTPGM SIFNEPPTEQ SIYEKSARLE SGRATGDAQN AAFVTDNGED DAQNDYIQPP
     LEVVRRGALT PNRMSELTRL ENVRTTPESP HFEVSSPSTS SSCVSIDFSP LDAANSENGS
     VGGLVLNVPS LPTRARSANE LTRQNTHVQI NLPDDVHDEK F
 
 
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