ID A0A068Y2K5_ECHMU Unreviewed; 1088 AA.
AC A0A068Y2K5;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Potassium voltage gated channel subfamily H {ECO:0000313|EMBL:CUT99305.1};
OS Echinococcus multilocularis (Fox tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Cyclophyllidea; Taeniidae; Echinococcus.
OX NCBI_TaxID=6211 {ECO:0000313|EMBL:CUT99305.1};
RN [1] {ECO:0000313|EMBL:CUT99305.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23485966; DOI=10.1038/nature12031;
RA Tsai I.J., Zarowiecki M., Holroyd N., Garciarrubio A., Sanchez-Flores A.,
RA Brooks K.L., Tracey A., Bobes R.J., Fragoso G., Sciutto E., Aslett M.,
RA Beasley H., Bennett H.M., Cai J., Camicia F., Clark R., Cucher M.,
RA De Silva N., Day T.A., Deplazes P., Estrada K., Fernandez C., Holland P.W.,
RA Hou J., Hu S., Huckvale T., Hung S.S., Kamenetzky L., Keane J.A., Kiss F.,
RA Koziol U., Lambert O., Liu K., Luo X., Luo Y., Macchiaroli N., Nichol S.,
RA Paps J., Parkinson J., Pouchkina-Stantcheva N., Riddiford N., Rosenzvit M.,
RA Salinas G., Wasmuth J.D., Zamanian M., Zheng Y., Cai X., Soberon X.,
RA Olson P.D., Laclette J.P., Brehm K., Berriman M., Garciarrubio A.,
RA Bobes R.J., Fragoso G., Sanchez-Flores A., Estrada K., Cevallos M.A.,
RA Morett E., Gonzalez V., Portillo T., Ochoa-Leyva A., Jose M.V., Sciutto E.,
RA Landa A., Jimenez L., Valdes V., Carrero J.C., Larralde C.,
RA Morales-Montor J., Limon-Lason J., Soberon X., Laclette J.P.;
RT "The genomes of four tapeworm species reveal adaptations to parasitism.";
RL Nature 496:57-63(2013).
RN [2] {ECO:0000313|EMBL:CUT99305.1}
RP NUCLEOTIDE SEQUENCE.
RA Zhang Y., Guo Z.;
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; LN902845; CUT99305.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A068Y2K5; -.
DR STRING; 6211.A0A068Y2K5; -.
DR eggNOG; KOG0498; Eukaryota.
DR OMA; YRLESRM; -.
DR GO; GO:0034702; C:monoatomic ion channel complex; IEA:UniProtKB-KW.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR CDD; cd00038; CAP_ED; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.1200.260; -; 1.
DR Gene3D; 1.10.287.70; -; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR018490; cNMP-bd_dom_sf.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR003938; K_chnl_volt-dep_EAG/ELK/ERG.
DR InterPro; IPR003967; K_chnl_volt-dep_ERG.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR PANTHER; PTHR10217:SF548; POTASSIUM VOLTAGE-GATED CHANNEL SUBFAMILY H MEMBER 7-LIKE; 1.
DR PANTHER; PTHR10217; VOLTAGE AND LIGAND GATED POTASSIUM CHANNEL; 1.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR PRINTS; PR01463; EAGCHANLFMLY.
DR PRINTS; PR01470; ERGCHANNEL.
DR SMART; SM00100; cNMP; 1.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
PE 4: Predicted;
KW Ion channel {ECO:0000256|ARBA:ARBA00023303};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Potassium {ECO:0000256|ARBA:ARBA00022958};
KW Potassium channel {ECO:0000256|ARBA:ARBA00022826};
KW Potassium transport {ECO:0000256|ARBA:ARBA00022538};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448};
KW Voltage-gated channel {ECO:0000256|ARBA:ARBA00022882}.
FT TRANSMEM 393..414
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 533..557
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 625..649
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 728..806
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT REGION 246..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 971..1006
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 983..1003
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1088 AA; 121845 MW; 9158625E215FD647 CRC64;
MPVRRGHIAP KNTYIDTLIK KFDNQYAAFV ITNSKIALHP IIYCSADFCD LFCFTKAQLL
LKSSNFPFLC GEKTSSESIQ ALANGLVCDR ETKLQLSLYT RKDEVKQCEV TITPLTDEFG
RVSLHIIFFE AVEGTHLEKR QTRCASARRI SSIATMIFHR GKEPPRNNLK RIHQMSQSVR
HELLPKEVVL SRRPSENIPA GNNHKISISS LFINDLKSPS EPANTEKSAR FDSISVETAN
SVTLRSSVQT SRASMANEPI KKSEVRPKSC SNAPPLWSDH QSSETESTTD RARPASAVLG
GRCSRYALPS LLARGSRLIS APASQTSIVL SDAGTLQVVL GKHGDQAKSH VTDTFAKILS
LDKDLHEKRK LESKRMHKYT IKHYSPIRAV WDWFILLLVI YTVIFTPYMT AFLLNYKGFN
CTHPHRRSPG HRTILGTVDI MVDIMFVCDI IINFRTTYVN KNDEVVSNPK KIATHYLKGW
FFIDLVAAIP FDALFFRSQE KQPTALIGLL KSARLLRLIN VARKLDRYSE YGTAILVLLT
SVFVLIAHWL ACIWYAIGNA EHQHSSTKIG WLATLAEQTR QFYNESPCSG PTLQTKYITA
LYFTFSSLTS IGFGNVSPNT NAEKIFSIVV MLVGSLMYAS IFGNVSAIIQ RLYSGTARYH
AQMLRIKEFI RFHQIPGPLR QRLEEYFIHA WAYTYGIDMS VVQRSFPECL QSDICMHVYK
TMLKTTRAFE GLTEGCLRTF ALRIRTVHLP PGDTLIHAGG LLTCLYFVEQ GSLEVLDPQD
GAILAVLSKG DFFGGLPPLQ EQPQNSLSTM AHGLIAAKSR FIVRALTYCD LHYVEQEELA
GLLHNYPELI GNLVAHFELT MPLAGIGKYL TEADLFCLSR DQKQQQQQDQ QQLHSPHGGT
SPVCLHKTTS SSCVFTETPL LQVPPRAQMQ SRARLPDTWL GDCRRRKLCS WELERLQRLL
EHSATAMVAD SASAPNIDGD GGGGIDSSTS STATTTTTAS PPPSHMDLEE RLSAQMAQRF
NKMEMNLLEL EEKMTTTFVS LLSHLQCLQT PLRPGVNAST MTEMEESGDE EEIEVNVRVI
EASNGNDL
//
