KCNS1_PANTR
ID KCNS1_PANTR Reviewed; 526 AA.
AC A4K2N8;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 89.
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 Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
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; DP000037; ABO52923.1; -; Genomic_DNA.
DR RefSeq; NP_001129322.1; NM_001135850.1.
DR RefSeq; XP_009435499.1; XM_009437224.2.
DR AlphaFoldDB; A4K2N8; -.
DR SMR; A4K2N8; -.
DR STRING; 9598.ENSPTRP00000023246; -.
DR PaxDb; A4K2N8; -.
DR Ensembl; ENSPTRT00000025188; ENSPTRP00000023246; ENSPTRG00000013534.
DR GeneID; 469951; -.
DR KEGG; ptr:469951; -.
DR CTD; 3787; -.
DR VGNC; VGNC:9876; KCNS1.
DR eggNOG; KOG3713; Eukaryota.
DR GeneTree; ENSGT00940000160096; -.
DR HOGENOM; CLU_011722_4_1_1; -.
DR InParanoid; A4K2N8; -.
DR OMA; FGQEAEY; -.
DR OrthoDB; 818306at2759; -.
DR TreeFam; TF313103; -.
DR Proteomes; UP000002277; Chromosome 20.
DR Bgee; ENSPTRG00000013534; Expressed in primary visual cortex and 12 other tissues.
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; IBA:GO_Central.
DR GO; GO:0005251; F:delayed rectifier potassium channel activity; IBA:GO_Central.
DR GO; GO:0015459; F:potassium channel regulator activity; IEA:Ensembl.
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 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..526
FT /note="Potassium voltage-gated channel subfamily S member
FT 1"
FT /id="PRO_0000289620"
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..337
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 338..358
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 359..373
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 374..395
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 396..408
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT INTRAMEM 409..420
FT /note="Helical; Name=Pore helix"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT INTRAMEM 421..428
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 429..435
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 436..464
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 465..526
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT REGION 491..526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 421..426
FT /note="Selectivity filter"
FT /evidence="ECO:0000250|UniProtKB:P63142"
SQ SEQUENCE 526 AA; 58414 MW; 7E44767873B53759 CRC64;
MLMLLVRGTH YENLRSKVVL PTPLGGRSTE TFVSEFPGPD TGIRWRRSDE ALRVNVGGVR
RQLSARALAR FPGTRLGRLQ AAASEEQARR LCDDYDEAAR EFYFDRHPGF FLSLLHFYRT
GHLHVLDELC VFAFGQEADY WGLGENALAA CCRARYLERR LTQPHAWDED SDTPSSVDPC
PDEISDVQRE LARYGAARCG RLRRRLWLTM ENPGYSLPSK LFSCVSISVV LASIAAMCIH
SLPEYQAREA AAAVAAVAAG RSPEGVRDDP VLRRLEYFCI AWFSFEVSSR LLLAPSTRNF
FCHPLNLIDI VSVLPFYLTL LAGVALGDQG GKEFGHLGKV VQVFRLMRIF RVLKLARHST
GLRSLGATLK HSYREVGILL LYLAVGVSVF SGVAYTAEKE EDVGFNTIPA CWWWGTVSMT
TVGYGDVVPV TVAGKLAASG CILGGILVVA LPITIIFNKF SHFYRRQKAL EAAVRNSNHR
EFEDLLSSVD GVSEASLETS RETSQEGRSA DLESQAPSEP PHPQMY
