KCNS3_RAT
ID KCNS3_RAT Reviewed; 491 AA.
AC O88759; O54900;
DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Potassium voltage-gated channel subfamily S member 3;
DE AltName: Full=Delayed-rectifier K(+) channel alpha subunit 3;
DE AltName: Full=Voltage-gated potassium channel subunit Kv9.3;
GN Name=Kcns3;
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], FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Brain, and Kidney;
RX PubMed=9362476; DOI=10.1093/emboj/16.22.6615;
RA Patel A.J., Lazdunski M., Honore E.;
RT "Kv2.1/Kv9.3, a novel ATP-dependent delayed-rectifier K+ channel in oxygen-
RT sensitive pulmonary artery myocytes.";
RL EMBO J. 16:6615-6625(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=9704029; DOI=10.1006/bbrc.1998.9072;
RA Stocker M., Kerschensteiner D.;
RT "Cloning and tissue distribution of two new potassium channel alpha-
RT subunits from rat brain.";
RL Biochem. Biophys. Res. Commun. 248:927-934(1998).
CC -!- FUNCTION: Potassium channel subunit that does not form functional
CC channels by itself. Can form functional heterotetrameric channels with
CC KCNB1; modulates the delayed rectifier voltage-gated potassium channel
CC activation and deactivation rates of KCNB1 (By similarity).
CC Heterotetrameric channel activity formed with KCNB1 show increased
CC current amplitude with the threshold for action potential activation
CC shifted towards more negative values in hypoxic-treated pulmonary
CC artery smooth muscle cells (PubMed:9362476).
CC {ECO:0000250|UniProtKB:Q9BQ31, ECO:0000269|PubMed:9362476}.
CC -!- SUBUNIT: Heterotetramer with KCNB1 (PubMed:9362476). Does not form
CC homomultimers (By similarity). {ECO:0000250|UniProtKB:Q9BQ31,
CC ECO:0000269|PubMed:9362476}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9BQ31};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9BQ31}. Note=May
CC not reach the plasma membrane but remain in an intracellular
CC compartment in the absence of KCNB1. {ECO:0000250|UniProtKB:Q9BQ31}.
CC -!- TISSUE SPECIFICITY: Expressed in myocytes (PubMed:9362476). Detected in
CC lung, spleen, brain and heart (PubMed:9704029).
CC {ECO:0000269|PubMed:9362476, ECO:0000269|PubMed:9704029}.
CC -!- DOMAIN: The transmembrane segment S4 functions as voltage-sensor and is
CC characterized by a series of positively charged amino acids at every
CC third position. Channel opening and closing is effected by a
CC conformation change that affects the position and orientation of the
CC voltage-sensor paddle formed by S3 and S4 within the membrane. A
CC transmembrane electric field that is positive inside would push the
CC positively charged S4 segment outwards, thereby opening the pore, while
CC a field that is negative inside would pull the S4 segment inwards and
CC close the pore. Changes in the position and orientation of S4 are then
CC transmitted to the activation gate formed by the inner helix bundle via
CC the S4-S5 linker region. {ECO:0000250|UniProtKB:P63142}.
CC -!- MISCELLANEOUS: Inhibited by 4-aminopyridine (4-AP). Channel activity is
CC reversibly inhibited by hypoxia and down-regulated in the absence of
CC intracellular ATP.
CC -!- SIMILARITY: Belongs to the potassium channel family. S (TC 1.A.1.2)
CC subfamily. Kv9.3/KCNS3 sub-subfamily. {ECO:0000305}.
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DR EMBL; AF029056; AAB94882.1; -; mRNA.
DR EMBL; Y17607; CAA76805.1; -; mRNA.
DR PIR; JE0276; JE0276.
DR RefSeq; NP_113966.2; NM_031778.2.
DR AlphaFoldDB; O88759; -.
DR SMR; O88759; -.
DR IntAct; O88759; 2.
DR STRING; 10116.ENSRNOP00000006499; -.
DR PaxDb; O88759; -.
DR Ensembl; ENSRNOT00000006499; ENSRNOP00000006499; ENSRNOG00000004899.
DR Ensembl; ENSRNOT00000095301; ENSRNOP00000095367; ENSRNOG00000004899.
DR Ensembl; ENSRNOT00000108088; ENSRNOP00000080054; ENSRNOG00000004899.
DR Ensembl; ENSRNOT00000112607; ENSRNOP00000091305; ENSRNOG00000004899.
DR Ensembl; ENSRNOT00000113996; ENSRNOP00000094251; ENSRNOG00000004899.
DR GeneID; 83588; -.
DR KEGG; rno:83588; -.
DR CTD; 3790; -.
DR RGD; 621527; Kcns3.
DR eggNOG; KOG3713; Eukaryota.
DR GeneTree; ENSGT00940000155979; -.
DR HOGENOM; CLU_011722_4_1_1; -.
DR InParanoid; O88759; -.
DR OMA; EYICIGW; -.
DR OrthoDB; 818306at2759; -.
DR PhylomeDB; O88759; -.
DR TreeFam; TF313103; -.
DR Reactome; R-RNO-1296072; Voltage gated Potassium channels.
DR Reactome; R-RNO-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
DR PRO; PR:O88759; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000004899; Expressed in lung and 19 other tissues.
DR Genevisible; O88759; RN.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IBA:GO_Central.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IBA:GO_Central.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR Gene3D; 1.20.120.350; -; 1.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR003968; K_chnl_volt-dep_Kv.
DR InterPro; IPR003971; K_chnl_volt-dep_Kv9.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR003131; T1-type_BTB.
DR InterPro; IPR028325; VG_K_chnl.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR11537; PTHR11537; 1.
DR Pfam; PF02214; BTB_2; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR PRINTS; PR01494; KV9CHANNEL.
DR PRINTS; PR01491; KVCHANNEL.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Ion channel; Ion transport; Membrane; Potassium;
KW Potassium channel; Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..491
FT /note="Potassium voltage-gated channel subfamily S member
FT 3"
FT /id="PRO_0000054089"
FT TOPO_DOM 1..182
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 183..204
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 205..220
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 221..243
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 244..254
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 255..275
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 276..285
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 286..306
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 307..321
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 322..343
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 344..357
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT INTRAMEM 358..369
FT /note="Helical; Name=Pore helix"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT INTRAMEM 370..377
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 378..384
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 385..413
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 414..491
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT MOTIF 370..375
FT /note="Selectivity filter"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT CONFLICT 113
FT /note="I -> F (in Ref. 1; AAB94882)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 491 AA; 55866 MW; 6157BC7EFE94CC2B CRC64;
MVFGEFFHRP GQDEELVNLN VGGFKQSVDQ STLLRFPHTR LGKLLTCHSE EAILELCDDY
SVADKEYYFD RNPSLFRYVL NFYYTGKLHV MEELCVFSFC QEIEYWGINE LFIDSCCSSR
YQERKEESHE KDWDQKSNDV STDSSFEESS LFEKELEKFD ELRFGQLRKK IWIRMENPAY
CLSAKLIAIS SLSVVLASIV AMCVHSMSEF QNEDGEVDDP VLEGVEIACI AWFTGELAIR
LVAAPSQKKF WKNPLNIIDF VSIIPFYATL AVDTKEEESE DIENMGKVVQ ILRLMRIFRI
LKLARHSVGL RSLGATLRHS YHEVGLLLLF LSVGISIFSV LIYSVEKDEL ASSLTSIPIC
WWWATISMTT VGYGDTHPVT LAGKIIASTC IICGILVVAL PITIIFNKFS KYYQKQKDMD
VDQCSEDPPE KCHELPYFNI RDVYAQQVHA FITSLSSIGI VVSDPDSTDA SSVEDNEDAY
NTASLENCTA K
