KCNS1_OTOGA
ID KCNS1_OTOGA Reviewed; 528 AA.
AC A4K2Q6;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 25-MAY-2022, entry version 67.
DE RecName: Full=Potassium voltage-gated channel subfamily S member 1;
DE AltName: Full=Delayed-rectifier K(+) channel alpha subunit 1;
GN Name=KCNS1;
OS Otolemur garnettii (Small-eared galago) (Garnett's greater bushbaby).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lorisiformes;
OC Galagidae; Otolemur.
OX NCBI_TaxID=30611;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=17267810; DOI=10.1101/gr.6004607;
RG NISC comparative sequencing program;
RA Hurle B., Swanson W., Green E.D.;
RT "Comparative sequence analyses reveal rapid and divergent evolutionary
RT changes of the WFDC locus in the primate lineage.";
RL Genome Res. 17:276-286(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K., Jaffe D.B.,
RA Gnerre S., MacCallum I., Przybylski D., Ribeiro F.J., Burton J.N.,
RA Walker B.J., Sharpe T., Hall G.;
RT "Version 3 of the genome sequence of Otolemur garnettii(Bushbaby).";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
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:O35173}.
CC -!- SUBUNIT: Heteromultimer with KCNB1 and KCNB2. Does not form
CC homomultimers. {ECO:0000250|UniProtKB:O35173}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O35173};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:O35173}. 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:O35173}.
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. Kv9.1/KCNS1 sub-subfamily. {ECO:0000305}.
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DR EMBL; DP000040; ABO52941.1; -; Genomic_DNA.
DR AlphaFoldDB; A4K2Q6; -.
DR SMR; A4K2Q6; -.
DR STRING; 30611.ENSOGAP00000018307; -.
DR Ensembl; ENSOGAT00000033173; ENSOGAP00000018307; ENSOGAG00000025880.
DR eggNOG; KOG3713; Eukaryota.
DR GeneTree; ENSGT00940000160096; -.
DR HOGENOM; CLU_011722_4_1_1; -.
DR InParanoid; A4K2Q6; -.
DR OMA; FGQEAEY; -.
DR TreeFam; TF313103; -.
DR Proteomes; UP000005225; Unassembled WGS sequence.
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; IEA:Ensembl.
DR GO; GO:0005251; F:delayed rectifier potassium channel activity; IEA:Ensembl.
DR GO; GO:0015459; F:potassium channel regulator activity; IEA:Ensembl.
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 3: Inferred from homology;
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..528
FT /note="Potassium voltage-gated channel subfamily S member
FT 1"
FT /id="PRO_0000289619"
FT TOPO_DOM 1..217
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 218..239
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 240..270
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 271..293
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 294..304
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 305..322
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 323..341
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 342..362
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 363..377
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 378..399
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 400..412
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT INTRAMEM 413..424
FT /note="Helical; Name=Pore helix"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT INTRAMEM 425..432
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 433..439
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 440..468
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 469..528
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT REGION 497..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 425..430
FT /note="Selectivity filter"
FT /evidence="ECO:0000250|UniProtKB:P63142"
SQ SEQUENCE 528 AA; 57969 MW; 01F437F5175ADBCC CRC64;
MLMLLVRGTH FENNWSKLIP PATIDALGNE SPVPDSEVPN SGIPWRRSDE ALSVNVGGVR
RRLSARALAR FPGTRLGRLQ AAASEEQARR LCDDYDAAAG EFYFDRHPGF FLSLLHFYRT
GRLHVLDELC VFAFGQEADY WGLGENALAA CCRARYLERR VARPRAWDED SDTPSSVDPC
TDEISDVQRE LARYGAARCG RLRRRLWLTM ENPGYSLPSK LFSCVSIGVV LASIAAMCIH
SLPEYQAHEA AAAVATVVAG RGAEGVRDDP VLRRLEYFCI AWFSFEVSSR LLLAPSARNF
FCHPLNLIDI VSVLPFYLTL LAGVALGGNQ NGTGGEELGH FGKVVQVFRL MRIFRVLKLA
RHSTGLRSLG ATLKHSYREV GILLLYLAVG VSVFSGVAYT AEKEEDEGFA TIPACWWWGT
VSMTTVGYGD VVPVTLAGKL AASGCILGGI LVVALPITII FNKFSHFYQR QKALEAAVRN
SGHREFEDLL SSIDGVSEAS LGTSRETSQE GRSADLEAPS QSPKPQVY
