KVAP_AERPE
ID KVAP_AERPE Reviewed; 295 AA.
AC Q9YDF8;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 129.
DE RecName: Full=Voltage-gated potassium channel;
DE AltName: Full=KvAP;
GN OrderedLocusNames=APE_0955;
OS Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS K1).
OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Aeropyrum.
OX NCBI_TaxID=272557;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT Aeropyrum pernix K1.";
RL DNA Res. 6:83-101(1999).
RN [2]
RP FUNCTION.
RX PubMed=12629550; DOI=10.1038/nature01473;
RA Ruta V., Jiang Y., Lee A., Chen J., MacKinnon R.;
RT "Functional analysis of an archaebacterial voltage-dependent K+ channel.";
RL Nature 422:180-185(2003).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 31-253.
RX PubMed=12721618; DOI=10.1038/nature01580;
RA Jiang Y., Lee A., Chen J., Ruta V., Cadene M., Chait B.T., MacKinnon R.;
RT "X-ray structure of a voltage-dependent K(+) channel.";
RL Nature 423:33-41(2003).
CC -!- FUNCTION: Mediates a strong voltage-dependent potassium ion
CC permeability of excitable membranes. Assuming opened or closed
CC conformations in response to the voltage difference across the
CC membrane, the protein forms a potassium-selective channel through which
CC potassium ions may pass in accordance with their electrochemical
CC gradient. {ECO:0000269|PubMed:12629550}.
CC -!- INTERACTION:
CC Q9YDF8; Q9YDF8: APE_0955; NbExp=2; IntAct=EBI-15692219, EBI-15692219;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- DOMAIN: Contains a central ion-conduction pore surrounded by four
CC voltage sensors which form the voltage-sensor paddles that move in
CC response to membrane voltage changes through the fluid membrane
CC interior, each voltage-sensor carrying their four positive charges
CC across the membrane. It is thought that the S4 arginine residues move
CC through the membrane's electric field to open the pore.
CC -!- SIMILARITY: Belongs to the potassium channel family. {ECO:0000305}.
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DR EMBL; BA000002; BAA79939.1; -; Genomic_DNA.
DR PIR; C72692; C72692.
DR PDB; 1ORQ; X-ray; 3.20 A; C=31-253.
DR PDB; 1ORS; X-ray; 1.90 A; C=33-161.
DR PDB; 2A0L; X-ray; 3.90 A; A/B=20-259.
DR PDB; 2KYH; NMR; -; A=18-160.
DR PDB; 6UWM; EM; 5.90 A; A/B/C/D=25-295.
DR PDBsum; 1ORQ; -.
DR PDBsum; 1ORS; -.
DR PDBsum; 2A0L; -.
DR PDBsum; 2KYH; -.
DR PDBsum; 6UWM; -.
DR AlphaFoldDB; Q9YDF8; -.
DR BMRB; Q9YDF8; -.
DR SMR; Q9YDF8; -.
DR DIP; DIP-29648N; -.
DR STRING; 272557.APE_0955; -.
DR TCDB; 1.A.1.17.1; the voltage-gated ion channel (vic) superfamily.
DR ABCD; Q9YDF8; 2 sequenced antibodies.
DR EnsemblBacteria; BAA79939; BAA79939; APE_0955.
DR KEGG; ape:APE_0955; -.
DR eggNOG; arCOG01964; Archaea.
DR OMA; FYYMEVN; -.
DR EvolutionaryTrace; Q9YDF8; -.
DR Proteomes; UP000002518; Chromosome.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR028325; VG_K_chnl.
DR PANTHER; PTHR11537; PTHR11537; 1.
DR Pfam; PF00520; Ion_trans; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Ion channel; Ion transport; Membrane;
KW Potassium; Potassium channel; Potassium transport; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..295
FT /note="Voltage-gated potassium channel"
FT /id="PRO_0000054097"
FT TOPO_DOM 1..38
FT /note="Cytoplasmic"
FT TRANSMEM 39..63
FT /note="Helical; Name=Segment S1"
FT TOPO_DOM 64..67
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..92
FT /note="Helical; Name=Segment S2"
FT TOPO_DOM 93..96
FT /note="Cytoplasmic"
FT INTRAMEM 97..105
FT /note="Helical; Name=Segment S3A"
FT TOPO_DOM 106..108
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 109..125
FT /note="Helical; Voltage-sensor; Name=Segment S3B"
FT TOPO_DOM 126..128
FT /note="Cytoplasmic"
FT TRANSMEM 129..145
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT TOPO_DOM 146..159
FT /note="Cytoplasmic"
FT TRANSMEM 160..184
FT /note="Helical; Name=Segment S5"
FT TOPO_DOM 185..195
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 196..208
FT /note="Pore-forming"
FT /evidence="ECO:0000255"
FT TOPO_DOM 209..221
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..253
FT /note="Helical; Name=Segment S6"
FT TOPO_DOM 254..295
FT /note="Cytoplasmic"
FT MOTIF 209..214
FT /note="Selectivity filter"
FT TURN 32..34
FT /evidence="ECO:0007829|PDB:1ORQ"
FT HELIX 38..60
FT /evidence="ECO:0007829|PDB:1ORS"
FT HELIX 66..92
FT /evidence="ECO:0007829|PDB:1ORS"
FT TURN 96..102
FT /evidence="ECO:0007829|PDB:1ORS"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:1ORS"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:1ORS"
FT HELIX 113..125
FT /evidence="ECO:0007829|PDB:1ORS"
FT HELIX 129..161
FT /evidence="ECO:0007829|PDB:1ORS"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:1ORQ"
FT HELIX 196..207
FT /evidence="ECO:0007829|PDB:1ORQ"
FT HELIX 220..251
FT /evidence="ECO:0007829|PDB:1ORQ"
SQ SEQUENCE 295 AA; 32535 MW; 1EC8CE1E39E24D0F CRC64;
MSVERWVFPG CSVMARFRRG LSDLGGRVRN IGDVMEHPLV ELGVSYAALL SVIVVVVEYT
MQLSGEYLVR LYLVDLILVI ILWADYAYRA YKSGDPAGYV KKTLYEIPAL VPAGLLALIE
GHLAGLGLFR LVRLLRFLRI LLIISRGSKF LSAIADAADK IRFYHLFGAV MLTVLYGAFA
IYIVEYPDPN SSIKSVFDAL WWAVVTATTV GYGDVVPATP IGKVIGIAVM LTGISALTLL
IGTVSNMFQK ILVGEPEPSC SPAKLAEMVS SMSEEEFEEF VRTLKNLRRL ENSMK
