ID M3WGP9_FELCA Unreviewed; 1108 AA.
AC M3WGP9;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 3.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=Potassium voltage-gated channel subfamily H member 8 {ECO:0000313|Ensembl:ENSFCAP00000011420.5};
GN Name=KCNH8 {ECO:0000313|Ensembl:ENSFCAP00000011420.5,
GN ECO:0000313|VGNC:VGNC:63039};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000011420.5, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000011420.5, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000011420.5,
RC ECO:0000313|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2] {ECO:0000313|Ensembl:ENSFCAP00000011420.5, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000011420.5,
RC ECO:0000313|Proteomes:UP000011712};
RA Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT "Sequence assembly of the Felis catus genome version 6.2.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFCAP00000011420.5}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000011420.5};
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBUNIT: The potassium channel is probably composed of a homo- or
CC heterotetrameric complex of pore-forming alpha subunits that can
CC associate with modulating beta subunits.
CC {ECO:0000256|ARBA:ARBA00011552}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; AANG04001816; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003992205.1; XM_003992156.3.
DR AlphaFoldDB; M3WGP9; -.
DR STRING; 9685.ENSFCAP00000011420; -.
DR PaxDb; 9685-ENSFCAP00000011420; -.
DR Ensembl; ENSFCAT00000012310.6; ENSFCAP00000011420.5; ENSFCAG00000012306.6.
DR VGNC; VGNC:63039; KCNH8.
DR eggNOG; KOG0498; Eukaryota.
DR GeneTree; ENSGT00940000156869; -.
DR HOGENOM; CLU_005746_6_0_1; -.
DR InParanoid; M3WGP9; -.
DR OMA; SWDREGM; -.
DR OrthoDB; 66005at2759; -.
DR Proteomes; UP000011712; Chromosome C2.
DR Bgee; ENSFCAG00000012306; Expressed in brain and 3 other cell types or tissues.
DR GO; GO:0034702; C:monoatomic ion channel complex; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
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:0042391; P:regulation of membrane potential; IBA:GO_Central.
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; IPR003950; K_chnl_volt-dep_ELK.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR10217:SF380; POTASSIUM VOLTAGE-GATED CHANNEL SUBFAMILY H MEMBER 8; 1.
DR PANTHER; PTHR10217; VOLTAGE AND LIGAND GATED POTASSIUM CHANNEL; 1.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF13426; PAS_9; 1.
DR PRINTS; PR01463; EAGCHANLFMLY.
DR PRINTS; PR01465; ELKCHANNEL.
DR SMART; SM00100; cNMP; 1.
DR SMART; SM00086; PAC; 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.
DR PROSITE; PS50113; PAC; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
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 Reference proteome {ECO:0000313|Proteomes:UP000011712};
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 212..237
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 257..276
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 315..333
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 354..377
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 419..437
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 449..473
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 93..145
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 551..668
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT REGION 684..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 764..849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 962..989
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 854..888
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 684..701
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 728..744
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..781
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 782..796
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 962..979
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1108 AA; 123706 MW; 482DCA1E38121CCA CRC64;
MPVMKGLLAP QNTFLDTIAT RFDGTHSNFI LANAQVAKGF PIVYCSDGFC ELAGFARTEV
MQKSCSCKFL FGVETNEQLM LQIEKSLEEK TEFKGEIMFY KKNGSPFWCL LDIVPIKNEK
GDVVLFLASF KDITDTKVKI TPEDKKEDKA KGRSRAGTHF DSARRRSRAV LYHISGHLQR
REKNKLKINN NVFVDKPAFP EYKVSDAKKS KFILLHFSTF KAGWDWLILL ATFYVAVTVP
YNVCFIGNDD LSTTRSTTVS DIAVEILFII DIILNFRTTY VSKSGQVIFE ARSICIHYVT
TWFIIDLIAA LPFDLLYAFN VTVVSLVHLL KTVRLLRLLR LLQKLDRYSQ HSTIVLTLLM
SMFALLAHWM ACIWYVIGKM EREDNSLLKW EVGWLHELGK RLESPYYGNN TLGGPSIRSA
YIAALYFTLS SLTSVGFGNV SANTDAEKIF SICTMLIGAL MHALVFGNVT AIIQRMYSRW
SLYHTRTKDL KDFIRVHHLP QQLKQRMLEY FQTTWSVNNG IDSNELLKDF PDELRSDITM
HLNKEILQLS LFECASRGCL RSLSLHIKTS FCAPGEYLLR QGDALQAIYF VCSGSMEVLK
DSMVLAILGK GDLIGANLSI KDQVIKTNAD VKALTYCDLQ CIILKGLFEV LDLYPEYAHK
FVEDIQHDLT YNLREGHESD VISRLSNKST VSQSEPKGNG SINKRLPSIV EDEEEEEEGE
EEETASLSPI YTRGSSSSRS KKVGSSKSYL GLSLKQLASG TVPFHSPIRV SSSNSPKNKQ
ETDPPNHGKR KERNLKLQLS ALNSSGPPDL SPRIVDGIED GNSSEESQTF DFGSERLRPE
PRVSPPLGDS EIGAAVLFIK AEETKQQINK LNSEVTTLTQ EVSQLGKDMR NVMQLLENVL
SPQPPSRFCS LHTTSVCPPR DSLQTRMTWS AHQPCLHLQA GGAAYTQAQL CHGNVTSDIW
SVDPSSVGSS PQRTGAHEQN PADSELYHSP NLDYSPAHCQ VVQEGHLQFL RCISPHSDST
LTPLQSISAT LSSSVCSSSE TSLHLVLPSR SEEGSFSQGA TSPFSLENLP GSWDREGAAS
ISTEPLENFP LEVVTSTAEM KDNKAINV
//
