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Database: UniProt
Entry: KCNS3_RAT
LinkDB: KCNS3_RAT
Original site: 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   22-NOV-2017, entry version 126.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, SUBCELLULAR LOCATION,
RP   AND 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
RT   oxygen-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
CC       with KCNB1; modulates the delayed rectifier voltage-gated
CC       potassium channel activation and deactivation rates of KCNB1 (By
CC       similarity). Heterotetrameric channel activity formed with KCNB1
CC       show increased current amplitude with the threshold for action
CC       potential activation shifted towards more negative values in
CC       hypoxic-treated pulmonary artery smooth muscle cells
CC       (PubMed:9362476). {ECO:0000250|UniProtKB:Q9BQ31,
CC       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
CC       {ECO:0000250|UniProtKB:Q9BQ31}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q9BQ31}. Note=May not reach the plasma
CC       membrane but remain in an intracellular compartment in the absence
CC       of KCNB1. {ECO:0000250|UniProtKB:Q9BQ31}.
CC   -!- TISSUE SPECIFICITY: Expressed in myocytes (PubMed:9362476).
CC       Detected in 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
CC       and is characterized by a series of positively charged amino acids
CC       at every third position. Channel opening and closing is effected
CC       by a conformation change that affects the position and orientation
CC       of the voltage-sensor paddle formed by S3 and S4 within the
CC       membrane. A transmembrane electric field that is positive inside
CC       would push the positively charged S4 segment outwards, thereby
CC       opening the pore, while a field that is negative inside would pull
CC       the S4 segment inwards and close the pore. Changes in the position
CC       and orientation of S4 are then transmitted to the activation gate
CC       formed by the inner helix bundle via the S4-S5 linker region.
CC       {ECO:0000250|UniProtKB:P63142}.
CC   -!- MISCELLANEOUS: Inhibited by 4-aminopyridine (4-AP). Channel
CC       activity is reversibly inhibited by hypoxia and down-regulated in
CC       the absence of intracellular ATP.
CC   -!- SIMILARITY: Belongs to the potassium channel family. S (TC
CC       1.A.1.2) subfamily. Kv9.3/KCNS3 sub-subfamily. {ECO:0000305}.
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   UniGene; Rn.10878; -.
DR   ProteinModelPortal; O88759; -.
DR   SMR; O88759; -.
DR   IntAct; O88759; 2.
DR   STRING; 10116.ENSRNOP00000006499; -.
DR   PaxDb; O88759; -.
DR   PRIDE; O88759; -.
DR   Ensembl; ENSRNOT00000006499; ENSRNOP00000006499; ENSRNOG00000004899.
DR   GeneID; 83588; -.
DR   KEGG; rno:83588; -.
DR   CTD; 3790; -.
DR   RGD; 621527; Kcns3.
DR   eggNOG; KOG3713; Eukaryota.
DR   eggNOG; COG1226; LUCA.
DR   GeneTree; ENSGT00760000118981; -.
DR   HOGENOM; HOG000231016; -.
DR   HOVERGEN; HBG052230; -.
DR   InParanoid; O88759; -.
DR   KO; K04933; -.
DR   OMA; WDQKSND; -.
DR   OrthoDB; EOG091G0FP3; -.
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; -.
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; IEA:InterPro.
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   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   PANTHER; PTHR11537; PTHR11537; 1.
DR   Pfam; PF02214; BTB_2; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   PRINTS; PR00169; KCHANNEL.
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; Complete proteome; Ion channel; Ion transport;
KW   Membrane; Potassium; Potassium channel; Potassium transport;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport;
KW   Voltage-gated channel.
FT   CHAIN         1    491       Potassium voltage-gated channel subfamily
FT                                S member 3.
FT                                /FTId=PRO_0000054089.
FT   TOPO_DOM      1    182       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:P63142}.
FT   TRANSMEM    183    204       Helical; Name=Segment S1.
FT                                {ECO:0000250|UniProtKB:P63142}.
FT   TOPO_DOM    205    220       Extracellular.
FT                                {ECO:0000250|UniProtKB:P63142}.
FT   TRANSMEM    221    243       Helical; Name=Segment S2.
FT                                {ECO:0000250|UniProtKB:P63142}.
FT   TOPO_DOM    244    254       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:P63142}.
FT   TRANSMEM    255    275       Helical; Name=Segment S3.
FT                                {ECO:0000250|UniProtKB:P63142}.
FT   TOPO_DOM    276    285       Extracellular.
FT                                {ECO:0000250|UniProtKB:P63142}.
FT   TRANSMEM    286    306       Helical; Voltage-sensor; Name=Segment S4.
FT                                {ECO:0000250|UniProtKB:P63142}.
FT   TOPO_DOM    307    321       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:P63142}.
FT   TRANSMEM    322    343       Helical; Name=Segment S5.
FT                                {ECO:0000250|UniProtKB:P63142}.
FT   TOPO_DOM    344    357       Extracellular.
FT                                {ECO:0000250|UniProtKB:P63142}.
FT   INTRAMEM    358    369       Helical; Name=Pore helix.
FT                                {ECO:0000250|UniProtKB:P63142}.
FT   INTRAMEM    370    377       {ECO:0000250|UniProtKB:P63142}.
FT   TOPO_DOM    378    384       Extracellular.
FT                                {ECO:0000250|UniProtKB:P63142}.
FT   TRANSMEM    385    413       Helical; Name=Segment S6.
FT                                {ECO:0000250|UniProtKB:P63142}.
FT   TOPO_DOM    414    491       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:P63142}.
FT   MOTIF       370    375       Selectivity filter.
FT                                {ECO:0000250|UniProtKB:P63142}.
FT   CONFLICT    113    113       I -> F (in Ref. 1; AAB94882).
FT                                {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
//
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