KCC3_CAEEL
ID KCC3_CAEEL Reviewed; 1070 AA.
AC Q09573;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 31-JAN-2018, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Potassium/chloride cotransporter 3 {ECO:0000303|PubMed:27062922};
GN Name=kcc-3; ORFNames=K02A2.3;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
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 [2]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=27062922; DOI=10.1016/j.cell.2016.03.026;
RA Singhvi A., Liu B., Friedman C.J., Fong J., Lu Y., Huang X.Y., Shaham S.;
RT "A glial K/Cl transporter controls neuronal receptive ending shape by
RT chloride inhibition of an rGC.";
RL Cell 165:936-948(2016).
RN [3]
RP FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF GLY-122; GLY-602 AND
RP GLY-769.
RX PubMed=26463820; DOI=10.1111/gbb.12260;
RA Yoshida A., Nakano S., Suzuki T., Ihara K., Higashiyama T., Mori I.;
RT "A glial K(+) /Cl(-) cotransporter modifies temperature-evoked dynamics in
RT Caenorhabditis elegans sensory neurons.";
RL Genes Brain Behav. 15:429-440(2016).
CC -!- FUNCTION: Probable potassium/chloride cotransporter that functions in
CC the amphid sheath glial cells to regulate thermotaxis behavior
CC (PubMed:26463820, PubMed:27062922). By maintaining chloride
CC homeostasis, negatively regulates guanylate cyclase gcy-8 in the
CC thermosensory AFD neurons and thereby controls the microvilli receptive
CC ending morphology of the AFD neurons and thermotaxis (PubMed:27062922).
CC Modulates the temperature-evoked neuronal activity of the AFD neurons
CC such as calcium responses to temperature gradients (PubMed:26463820).
CC Might also play a role in the chemotaxis behavior mediated by the
CC sensory neurons AWA and AWC (PubMed:26463820).
CC {ECO:0000269|PubMed:26463820, ECO:0000269|PubMed:27062922}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:27062922};
CC Multi-pass membrane protein {ECO:0000305}. Note=Localizes to the amphid
CC sheath glia apical domain in which the AFD microvilli are embedded.
CC {ECO:0000269|PubMed:27062922}.
CC -!- TISSUE SPECIFICITY: Expressed in the amphid sheath glia and the
CC cephalic sheath glia (PubMed:26463820, PubMed:27062922). Also expressed
CC in the inner labial and outer labial sheath and socket glia and as well
CC as phasmid sheath glia (PubMed:26463820). {ECO:0000269|PubMed:26463820,
CC ECO:0000269|PubMed:27062922}.
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DR EMBL; FO080416; CCD63538.2; -; Genomic_DNA.
DR PIR; G88208; G88208.
DR AlphaFoldDB; Q09573; -.
DR SMR; Q09573; -.
DR STRING; 6239.K02A2.3; -.
DR EPD; Q09573; -.
DR PaxDb; Q09573; -.
DR PeptideAtlas; Q09573; -.
DR EnsemblMetazoa; K02A2.3a.1; K02A2.3a.1; WBGene00019289.
DR UCSC; H16O14.1; c. elegans.
DR WormBase; K02A2.3a; CE52024; WBGene00019289; kcc-3.
DR eggNOG; KOG2082; Eukaryota.
DR HOGENOM; CLU_001883_1_1_1; -.
DR InParanoid; Q09573; -.
DR PhylomeDB; Q09573; -.
DR Reactome; R-CEL-426117; Cation-coupled Chloride cotransporters.
DR PRO; PR:Q09573; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00019289; Expressed in embryo and 3 other tissues.
DR ExpressionAtlas; Q09573; baseline and differential.
DR GO; GO:0016324; C:apical plasma membrane; IDA:WormBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0015379; F:potassium:chloride symporter activity; IBA:GO_Central.
DR GO; GO:0006884; P:cell volume homeostasis; IBA:GO_Central.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0055064; P:chloride ion homeostasis; IBA:GO_Central.
DR GO; GO:1902476; P:chloride transmembrane transport; IBA:GO_Central.
DR GO; GO:0032528; P:microvillus organization; IMP:WormBase.
DR GO; GO:0031283; P:negative regulation of guanylate cyclase activity; IGI:WormBase.
DR GO; GO:0055075; P:potassium ion homeostasis; IBA:GO_Central.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; IBA:GO_Central.
DR InterPro; IPR004841; AA-permease/SLC12A_dom.
DR InterPro; IPR018491; SLC12_C.
DR InterPro; IPR004842; SLC12A_fam.
DR PANTHER; PTHR11827; PTHR11827; 1.
DR Pfam; PF00324; AA_permease; 2.
DR Pfam; PF03522; SLC12; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Chloride; Ion transport; Membrane; Potassium;
KW Potassium transport; Reference proteome; Symport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1070
FT /note="Potassium/chloride cotransporter 3"
FT /id="PRO_0000065395"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 196..216
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 228..248
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 251..271
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 400..420
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 433..453
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 473..493
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 534..554
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 557..577
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 600..620
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 791..811
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 827..847
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MUTAGEN 122
FT /note="G->D: In nj90; defects in thermotaxis."
FT /evidence="ECO:0000269|PubMed:26463820"
FT MUTAGEN 602
FT /note="G->D: In nj94; defects in thermotaxis."
FT /evidence="ECO:0000269|PubMed:26463820"
FT MUTAGEN 769
FT /note="G->E: In nj100; defects in thermotaxis."
FT /evidence="ECO:0000269|PubMed:26463820"
SQ SEQUENCE 1070 AA; 118236 MW; 890DF19EA6043D13 CRC64;
MSNARRRFST VTQINTEGLQ AMGKGGGRME TVGEDGIPAD YKGNRKFTTS LGHLALYKED
EGIGTQASFI SGYTTPGPKE RATSEHVKAN LGVMLGVYLP TIQHILGVTM FIRLFWVVGM
SGVAWTMALL AICCLSTLLT SISLSAVATN GVVESGGAYF IISRNLGAEF GSAVGILFYL
ANTVAASMYI VGGVEVILMY LWPEMAIGGA DALHDTEMFG SLYNNLRLYG TVFLLIQALI
VAMGVKFVQL LAPVSLMCVI LAIAACIGGG IEKQITMEGM KVCAIDNHLL QSSIVTHPIH
KNQTSWFNET VDFCNLCDKS LYLESVFCAN VNNDEASAED DVFCTHYTSK KMTCQLAFPG
FNMKTLNDNM WPEYMEKSEV VPGVRGKETA EVVQDESSTF FMLMAIYFPA VTGIFTGTNM
SGDLRDPQRS IPVGTIAATL TTSAIYYILA ILFGGSITRS VLRDKFGRSI GNTMVVAALS
WPHPAVVTVG AFLSTFGAAL QCLCSAPRLL QSIAKDDVIP ILAPFARVTK NNEPFLGLVL
TVIIAECGIL LGAVDKIAEV LDFFFLMCYA FVNLIAVLHS VLKSPNWRPR FKYFHWTLSL
LGAALCFFIM FASSVPLACI ACTATAVIYK YVEWKGAKKE WGDGMRGLAL TTAQYSLLKV
EDKDPHPKNW RPQVLILLTS QWSKEMIDRR AVSMLNLGAQ LKAGRGLAIA CAFLKGSVDS
QKDKNRARDV KTTLVKDMSS VRLRGFAKTM FYNNHQINGT ISGLYQSIGI GGLRPNTILL
NWPNEKNPDE LVLFAEEIIH GAANDNCLIV TKGITDFPEY SERLTGFIDI WWIVQDGGIL
MLIAYLLRQH KVWKGCTLRI FAVSEQDSTK SEDMKAGLQK YIYMLRIDAE LFIVDLLDME
VSDEVVEKAA EVERKQKERE EMRRSKSGYL NDGFMEDNGK PRQVMMRHSD SARSFSPQPG
AHTSINLDET ETSFTESLFD DFYRSGTPNE DLEGAMKLNI HKMNTSVRLN RVIRENSPDS
QLILLNLPSP PRNRLAFNNS YMTYLDVLTE DLPRVLFIGG SGREVITIDS
