ID M3ZF64_XIPMA Unreviewed; 1025 AA.
AC M3ZF64;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=Potassium voltage-gated channel subfamily H member 8 {ECO:0000313|Ensembl:ENSXMAP00000000856.1};
OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000000856.1, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000000856.1}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000000856.1};
RG Ensembl;
RL Submitted (NOV-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 AlphaFoldDB; M3ZF64; -.
DR STRING; 8083.ENSXMAP00000000856; -.
DR Ensembl; ENSXMAT00000000859.2; ENSXMAP00000000856.1; ENSXMAG00000000864.2.
DR eggNOG; KOG0498; Eukaryota.
DR GeneTree; ENSGT00940000156869; -.
DR HOGENOM; CLU_005746_6_0_1; -.
DR InParanoid; M3ZF64; -.
DR OMA; SWDREGM; -.
DR OrthoDB; 66005at2759; -.
DR Proteomes; UP000002852; Unassembled WGS sequence.
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; 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.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
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:UP000002852};
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 223..241
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 261..281
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 316..332
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 353..376
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 421..439
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 451..475
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 38..90
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 93..145
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 553..670
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT REGION 689..801
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 969..994
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..703
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 729..748
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..784
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 973..989
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1025 AA; 114520 MW; A6EA90BA76CD7DE8 CRC64;
MPVMKGLLAP QNTFLDTIAT RFDGTHSNFI LANAQMSKGF PIVYCSDGFC ELTGFSRTEV
MQKSCACKFL YGPETSESII LSIDEALEER KEFKNEIMFY TKTAALFWCL LDIVPIKNEK
GDVVLFLASF KDITDTKAKA IQEDKKEERR RGRVKTGSSF SSTRLRGSTV LYHISGHLHS
REKSKIKINK NVFGDPPALP EYKVADAKKS KFILLHYSTF KAGWDWLILL ATFYVAVTVP
YNVCFIGDDD DLTRSTTVSD IGVEILFIID IIFNFRTTFV SKSGQVIFDA RQICIHYLTT
WFIIDLVAAL PFDLLYAVKV SVVSVVHLLK TVRLLRLLRL LQKMDRYSQH STVVLTLLMS
MFALLAHWMA CIWYIIGKME MEANAYNWDI GWLHELGKRL ESPYAGMADV NTTGSGPSIR
SVYIASLYFT LSSLTSVGFG NVSANTDAEK IFSVCIMLIG ALMHALVFGN VTAIIQRMYS
RWSQYHTRTK DLKDFIRVHH LPQSLKQRML EYFQTTWSVN NGIDCNELLK DFPDELRSDI
TMHLNKEILE LSLFASASRG CLRSLSLHIK TSFCTPGEYL LRQGDALQAV FFVCSGSMEV
LKDGMVLAIL GKGDLIGANL SLDNRVIKTN ADVKALTYCD LQCINLKGLY EVLDLYPEYS
HHFVQDIQQD LTYNLREGHE THVKTRLSTA AQESQSGVRR NGRVVQGQPT VAEVREEHEG
DSDEDEHDNT ESVSLLTEHH RPEDLRDTVG KSPLCQPRQK TVTRSLGRSQ KNLQDFTPTA
LDPSNLSPRI VDGTEDSEGT ETSQMFSFST GLGCPVSEPT SASTSATDML HISTTELAAK
AEETRGQLRH LDQQVSTLRR EVADLGQVMK RMATLMEALT PSVPQPAIIC PTRYSPAHQT
YLHCPSPPQP CHSPSKAAPI WTDPPMPLPC SSLTISQQHS AMCYADSLTH RPQSLQLVCP
AIIPKSTPPL TPDLSSRQPP PPLSVIPEPP LPSSSIRLRV HSSLPLDGGV RSLTRAPDAL
LKLDP
//
