KCNS1_LEMCA
ID KCNS1_LEMCA Reviewed; 529 AA.
AC A4K2S2;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 25-MAY-2022, entry version 46.
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 Lemur catta (Ring-tailed lemur).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC Lemuridae; Lemur.
OX NCBI_TaxID=9447;
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).
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; DP000042; ABO52957.1; -; Genomic_DNA.
DR AlphaFoldDB; A4K2S2; -.
DR SMR; A4K2S2; -.
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:InterPro.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
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; Transmembrane; Transmembrane helix;
KW Transport; Voltage-gated channel.
FT CHAIN 1..529
FT /note="Potassium voltage-gated channel subfamily S member
FT 1"
FT /id="PRO_0000289617"
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..342
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 343..363
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 364..378
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 379..400
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 401..413
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT INTRAMEM 414..425
FT /note="Helical; Name=Pore helix"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT INTRAMEM 426..433
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 434..440
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 441..469
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 470..529
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT REGION 498..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 426..431
FT /note="Selectivity filter"
FT /evidence="ECO:0000250|UniProtKB:P63142"
SQ SEQUENCE 529 AA; 58430 MW; D023176BE8CAD661 CRC64;
MLMLLVRGTH FENNWSKLIP PAPLDATVSE PPVPDSGEPD SGVPWRRSDE ALRVNVGGVR
RRLSARALAR FPGTRLGRLQ AAKSEEQARR LCDDYDAAAR EFYFDRHPGF FLSLLHFYRT
GRLHVLDELC VFAFGQEADY WGLGENALAA CCRARYLERR VARPRAWDED SDTPSSVDPN
PDEISDVQRE LARYGAARCG RLRRRLWLTM ENPGYSLPSK LFSCVSIGVV LASIAAMCIH
SLPEYQAREA AAAVATVAAG RSAEDVRDDP VLRRLEYFCI AWFSFEVSSR LLLAPSTRNF
FCHPLNLIDI VSVLPFYLTL LASVALGGNN HGGTSGEELG HLGKVVQVFR LMRIFRVLKL
ARHSTGLRSL GATLKHSYRE VGILLLYLAV GVSVFSGVAY TAEKEEDVGF DTIPACWWWG
TVSMTTVGYG DVVPVTLAGK LAASGCILGG ILVVALPITI IFNKFSHFYQ RQKALEAAVR
NSGHREFEDL LSSVDGVSDA SLETSRETSQ EGRSADLEAP SESPKPQIY
