KCNS2_RAT
ID KCNS2_RAT Reviewed; 477 AA.
AC Q9ER26;
DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Potassium voltage-gated channel subfamily S member 2;
DE AltName: Full=Delayed-rectifier K(+) channel alpha subunit 2;
DE AltName: Full=Voltage-gated potassium channel subunit Kv9.2;
GN Name=Kcns2;
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], AND TISSUE SPECIFICITY.
RC STRAIN=Wistar; TISSUE=Brain;
RX PubMed=11891605; DOI=10.1007/s004080000057;
RA Davies A.R., Kozlowski R.Z.;
RT "Kv channel subunit expression in rat pulmonary arteries.";
RL Lung 179:147-161(2001).
CC -!- FUNCTION: Potassium channel subunit that does not form functional
CC channels by itself. Can form functional heterotetrameric channels with
CC KCNB1 and KCNB2; modulates the delayed rectifier voltage-gated
CC potassium channel activation and deactivation rates of KCNB1 and KCNB2.
CC {ECO:0000250|UniProtKB:O35174}.
CC -!- SUBUNIT: Heterotetramer with KCNB1 and KCNB2. Does not form
CC homomultimers. {ECO:0000250|UniProtKB:O35174}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O35174};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:O35174}. Note=May
CC not reach the plasma membrane but remain in an intracellular
CC compartment in the absence of KCNB1 or KCNB2.
CC {ECO:0000250|UniProtKB:O35174}.
CC -!- TISSUE SPECIFICITY: Detected in brain, lung and in pulmonary arteries
CC (PubMed:11891605). {ECO:0000269|PubMed:11891605}.
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 -!- SIMILARITY: Belongs to the potassium channel family. S (TC 1.A.1.2)
CC subfamily. Kv9.2/KCNS2 sub-subfamily. {ECO:0000305}.
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DR EMBL; AJ296090; CAC14912.1; -; mRNA.
DR RefSeq; NP_076456.1; NM_023966.1.
DR AlphaFoldDB; Q9ER26; -.
DR SMR; Q9ER26; -.
DR STRING; 10116.ENSRNOP00000015707; -.
DR PaxDb; Q9ER26; -.
DR ABCD; Q9ER26; 1 sequenced antibody.
DR Ensembl; ENSRNOT00000115427; ENSRNOP00000088336; ENSRNOG00000066111.
DR GeneID; 66022; -.
DR KEGG; rno:66022; -.
DR UCSC; RGD:621525; rat.
DR CTD; 3788; -.
DR RGD; 621525; Kcns2.
DR eggNOG; KOG3713; Eukaryota.
DR GeneTree; ENSGT00940000160344; -.
DR HOGENOM; CLU_011722_4_1_1; -.
DR InParanoid; Q9ER26; -.
DR OMA; STIPACW; -.
DR OrthoDB; 818306at2759; -.
DR PhylomeDB; Q9ER26; -.
DR TreeFam; TF313103; -.
DR Reactome; R-RNO-1296072; Voltage gated Potassium channels.
DR PRO; PR:Q9ER26; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000011369; Expressed in frontal cortex and 3 other tissues.
DR Genevisible; Q9ER26; RN.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; ISO:RGD.
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:0006813; P:potassium ion transport; ISS:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
DR GO; GO:1902259; P:regulation of delayed rectifier potassium channel activity; ISS:UniProtKB.
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 2: Evidence at transcript 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..477
FT /note="Potassium voltage-gated channel subfamily S member
FT 2"
FT /id="PRO_0000054086"
FT TOPO_DOM 1..184
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 185..206
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 207..225
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 226..248
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 249..259
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 260..280
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 281..290
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 291..311
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 312..326
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 327..348
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 349..361
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT INTRAMEM 362..373
FT /note="Helical; Name=Pore helix"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT INTRAMEM 374..381
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 382..388
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 389..417
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 418..477
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT MOTIF 374..379
FT /note="Selectivity filter"
FT /evidence="ECO:0000250|UniProtKB:P63142"
SQ SEQUENCE 477 AA; 54317 MW; 23199B1BBE9C5D5C CRC64;
MTRQSLWDLS ETDVEDGEIR INVGGFKRRL RSHTLLRFPE TRLGRLLLCH SREAILELCD
DYDDVQREFY FDRNPELFPY VLHFYHTGKL HVMAELCVFS FSQEIEYWGI NEFFIDSCCS
YSYHGRKVEP EQEKWDEQSD QESTTSSFDE ILAFYNDASK FDGQPLGNFR RQLWLALDNP
GYSVLSRVFS VLSILVVLGS IITMCLNSLP DFQIPDSQGN PGEDPRFEIV EHFGIAWFTF
ELVARFAVAP DFLKFFKNAL NLIDLMSIVP FYITLVVNLV VESSPTLANL GRVAQVLRLM
RIFRILKLAR HSTGLRSLGA TLKYSYKEVG LLLLYLSVGI SIFSVVAYTI EKEENEGLAT
IPACWWWATV SMTTVGYGDV VPGTTAGKLT ASACILAGIL VVVLPITLIF NKFSHFYRRQ
KQLESAMRSC DFGDGMKEVP SVNLRDYYAH KVKSLMASLT NMSRSSPSEL SLDDSLH
