MVP_METJA
ID MVP_METJA Reviewed; 209 AA.
AC Q57603;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 25-MAY-2022, entry version 114.
DE RecName: Full=Hyperpolarization-activated voltage-gated potassium channel;
DE AltName: Full=MVP;
GN Name=mvp; OrderedLocusNames=MJ0139;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RX PubMed=12640457; DOI=10.1038/nn1028;
RA Sesti F., Rajan S., Gonzalez-Colaso R., Nikolaeva N., Goldstein S.A.N.;
RT "Hyperpolarization moves S4 sensors inward to open MVP, a methanococcal
RT voltage-gated potassium channel.";
RL Nat. Neurosci. 6:353-361(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [3]
RP FUNCTION.
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=12860407; DOI=10.1016/s0014-5793(03)00706-3;
RA Hellmer J., Zeilinger C.;
RT "MjK1, a K+ channel from M. jannaschii, mediates K+ uptake and K+
RT sensitivity in E. coli.";
RL FEBS Lett. 547:165-169(2003).
CC -!- FUNCTION: Voltage-gated potassium-selective channel opened by
CC hyperpolarization. {ECO:0000269|PubMed:12860407}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- DOMAIN: The segment S4 is probably the voltage-sensor and is
CC characterized by a series of positively charged amino acids.
CC -!- MISCELLANEOUS: Inhibited by barium.
CC -!- SIMILARITY: Belongs to the potassium channel family. {ECO:0000305}.
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DR EMBL; AY268105; AAP31055.1; -; mRNA.
DR EMBL; L77117; AAB98122.1; -; Genomic_DNA.
DR PIR; C64317; C64317.
DR RefSeq; WP_010869632.1; NC_000909.1.
DR AlphaFoldDB; Q57603; -.
DR SMR; Q57603; -.
DR STRING; 243232.MJ_0139; -.
DR TCDB; 1.A.1.6.1; the voltage-gated ion channel (vic) superfamily.
DR PRIDE; Q57603; -.
DR EnsemblBacteria; AAB98122; AAB98122; MJ_0139.
DR GeneID; 1450980; -.
DR KEGG; mja:MJ_0139; -.
DR eggNOG; arCOG01964; Archaea.
DR HOGENOM; CLU_1313152_0_0_2; -.
DR InParanoid; Q57603; -.
DR OrthoDB; 91207at2157; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:InterPro.
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:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR Gene3D; 1.20.120.350; -; 1.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR028325; VG_K_chnl.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR11537; PTHR11537; 1.
DR Pfam; PF00520; Ion_trans; 1.
PE 1: Evidence at protein level;
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..209
FT /note="Hyperpolarization-activated voltage-gated potassium
FT channel"
FT /id="PRO_0000054098"
FT TOPO_DOM 1..10
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 11..31
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..38
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 39..59
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 60..71
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..92
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 93..96
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..117
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 118..125
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 147..181
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..202
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 203..209
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOTIF 170..175
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
SQ SEQUENCE 209 AA; 24183 MW; FC91E7320F34D90F CRC64;
MNLKDRRLKK IMEVLSLIFT FEIVASFILS TYNPPYQDLL IKLDYISIMF FTFEFIYNFY
YVEDKAKFFK DIYNIVDAIV VIAFLLYSLQ VFYSKAFLGL RVINLLRILV LLRIIKLRKL
EENQALINFL TLLTICFIAS CLIWIVESGV NPAINNFFDA FYFTTISITT VGYGDITPKT
DAGKLIIIFS VLFFISGLIT SLQKALKGD
