Swiss-Prot entry
ID KVAP_AERPE STANDARD; PRT; 295 AA.
AC Q9YDF8;
DT 29-MAR-2004 (Rel. 43, Created)
DT 29-MAR-2004 (Rel. 43, Last sequence update)
DT 10-MAY-2005 (Rel. 47, Last annotation update)
DE Voltage-gated potassium channel (KvAP).
GN OrderedLocusNames=APE0955;
OS Aeropyrum pernix.
OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Aeropyrum.
OX NCBI_TaxID=56636;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K1;
RX MEDLINE=99310339; PubMed=10382966 [NCBI, ExPASy, EBI, Israel, Japan];
RA Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y.,
RA Jin-no K., Takahashi M., Sekine M., Baba S.-I., Ankai A., Kosugi H.,
RA Hosoyama A., Fukui S., Nagai Y., Nishijima K., Nakazawa H.,
RA Takamiya M., Masuda S., Funahashi T., Tanaka T., Kudoh Y.,
RA Yamazaki J., Kushida N., Oguchi A., Aoki K.-I., Kubota K.,
RA Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT "Complete genome sequence of an aerobic hyper-thermophilic
RT crenarchaeon, Aeropyrum pernix K1.";
RL DNA Res. 6:83-101(1999).
RN [2]
RP FUNCTION.
RX PubMed=12629550 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1038/nature01473;
RA Ruta V., Jiang Y., Lee A., Chen J., MacKinnon R.;
RT "Functional analysis of an archaebacterial voltage-dependent K+
RT channel.";
RL Nature 422:180-185(2003).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 31-253.
RX PubMed=12721618 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1038/nature01580;
RA Jiang Y., Lee A., Chen J., Ruta V., Cadene M., Chait B.T.,
RA 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
CC which potassium ions may pass in accordance with their
CC electrochemical gradient.
CC -!- SUBCELLULAR LOCATION: Integral 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 accross the membrane. It is thought that the S4 arginine residues
CC move through the membrane's electric field to open the pore.
CC -!- SIMILARITY: Belongs to the potassium channel family.
CC --------------------------------------------------------------------------
CC This Swiss-Prot entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use as long as its content is in no way modified and this statement is not
CC removed.
CC --------------------------------------------------------------------------
DR EMBL; BA000002; BAA79939.1; -; Genomic_DNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR PDB; 1ORQ; X-ray; C=31-253. [ExPASy / RCSB]
DR PDB; 1ORS; X-ray; C=33-160. [ExPASy / RCSB]
DR InterPro; IPR001622; K+channel_pore.
DR InterPro; IPR005820; M+channel_nlg.
DR CMR; Q9YDF8.
DR ProDom [Domain structure / List of seq. sharing at least 1 domain]
DR HOGENOM [Family / Alignment / Tree]
DR BLOCKS; Q9YDF8.
DR ProtoNet; Q9YDF8.
DR ProtoMap; Q9YDF8.
DR PRESAGE; Q9YDF8.
DR DIP; Q9YDF8.
DR ModBase; Q9YDF8.
DR SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW 3D-structure; Complete proteome; Ion transport; Ionic channel;
KW Potassium; Potassium channel; Potassium transport; Transmembrane;
KW Transport; Voltage-gated channel.
FT TOPO_DOM 1 38 Cytoplasmic.
FT TRANSMEM 39 63 Segment S1.
FT TRANSMEM 68 92 Segment S2.
FT TOPO_DOM 93 96 Cytoplasmic.
FT TRANSMEM 97 105 Segment S3A.
FT TRANSMEM 109 125 Segment S3B; voltage-sensor paddle.
FT TRANSMEM 129 145 Segment S4; voltage-sensor paddle.
FT TOPO_DOM 146 159 Cytoplasmic.
FT TRANSMEM 160 184 Segment S5.
FT TRANSMEM 222 253 Segment S6.
FT TOPO_DOM 254 295 Cytoplasmic.
FT REGION 196 208 Pore-forming helix.
FT MOTIF 209 214 Selectivity filter.
FT CONFLICT 59 59 Y -> C (in Ref. 3).
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
//