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KCNS1_PAPAN
ID   KCNS1_PAPAN             Reviewed;         529 AA.
AC   A4K2M4;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 69.
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   Papio anubis (Olive baboon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Papio.
OX   NCBI_TaxID=9555;
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; DP000036; ABO52907.1; -; Genomic_DNA.
DR   RefSeq; NP_001162204.1; NM_001168733.1.
DR   RefSeq; XP_009214305.1; XM_009216041.2.
DR   AlphaFoldDB; A4K2M4; -.
DR   SMR; A4K2M4; -.
DR   STRING; 9555.ENSPANP00000017672; -.
DR   Ensembl; ENSPANT00000022653; ENSPANP00000017672; ENSPANG00000011732.
DR   GeneID; 100137164; -.
DR   KEGG; panu:100137164; -.
DR   CTD; 3787; -.
DR   eggNOG; KOG3713; Eukaryota.
DR   GeneTree; ENSGT00940000160096; -.
DR   HOGENOM; CLU_011722_4_1_1; -.
DR   OMA; FGQEAEY; -.
DR   OrthoDB; 818306at2759; -.
DR   Proteomes; UP000028761; Chromosome 16.
DR   Bgee; ENSPANG00000011732; Expressed in visual cortex and 2 other tissues.
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..529
FT                   /note="Potassium voltage-gated channel subfamily S member
FT                   1"
FT                   /id="PRO_0000289621"
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..340
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TRANSMEM        341..361
FT                   /note="Helical; Voltage-sensor; Name=Segment S4"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TOPO_DOM        362..376
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TRANSMEM        377..398
FT                   /note="Helical; Name=Segment S5"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TOPO_DOM        399..411
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   INTRAMEM        412..423
FT                   /note="Helical; Name=Pore helix"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   INTRAMEM        424..431
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TOPO_DOM        432..438
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TRANSMEM        439..467
FT                   /note="Helical; Name=Segment S6"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TOPO_DOM        468..529
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   REGION          496..529
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           424..429
FT                   /note="Selectivity filter"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
SQ   SEQUENCE   529 AA;  58385 MW;  D5A57F2CE39675CC CRC64;
     MLMLLVRGTH YESLRSKVVL PTPLGGRSTE ALVSECPIPD TGIRWRQSDE ALRVNVGGVR
     RLLSARALAR FPGTRLGRLQ AAASEEQARR LCDDYDAAAH EFYFDRHPGF FLGLLHFYRT
     GHLHVLDELC VFAFGQEADY WGLGENALAA CCRARYLERR LTQPRAWDED SDTPSSVDPC
     PDEISDVQRE LARYGAARCG RLRRRLWLTM ENPGYSLPSK LFSCVSISVV LASIAAMCIH
     SLPEYQAREA AAAVAAVAAG RSPEGVRDDP VLRRLEYFCI AWFSFEVSSR LLLAPSTRNF
     FCHPLNLIDI VSVLPFYLTL LAGVALGDQG GTGGKELGHL GKVVQVFRLM RIFRVLKLAR
     HSTGLRSLGA TLKHSYREVG ILLLYLAVGV SVFSGVAYTA EKEEDVGFNT IPACWWWGTV
     SMTTVGYGDV VPVTVAGKLA ASGCILGGIL VVALPITIIF NKFSHFYRRQ KALEAAVRNS
     NHQEFEDLLS SVDAVSEASL ETSRETSQEG RSADLETQAP SEPPHPQMY
 
 
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