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Database: UniProt
Entry: A0A2Y9S459_PHYMC
LinkDB: A0A2Y9S459_PHYMC
Original site: A0A2Y9S459_PHYMC 
ID   A0A2Y9S459_PHYMC        Unreviewed;      1106 AA.
AC   A0A2Y9S459;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Potassium voltage-gated channel subfamily H member 8 {ECO:0000313|RefSeq:XP_023970955.1};
GN   Name=KCNH8 {ECO:0000313|RefSeq:XP_023970955.1};
OS   Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Physeteridae; Physeter.
OX   NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_023970955.1};
RN   [1] {ECO:0000313|RefSeq:XP_023970955.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_023970955.1};
RG   RefSeq;
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   RefSeq; XP_023970955.1; XM_024115187.1.
DR   AlphaFoldDB; A0A2Y9S459; -.
DR   STRING; 9755.ENSPCTP00005002791; -.
DR   Ensembl; ENSPCTT00005003065; ENSPCTP00005002791; ENSPCTG00005002008.
DR   KEGG; pcad:102974028; -.
DR   InParanoid; A0A2Y9S459; -.
DR   OrthoDB; 66005at2759; -.
DR   Proteomes; UP000248484; Chromosome 1.
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; 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.
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:UP000248484};
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..792
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          824..849
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1073..1106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          854..888
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        684..699
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"
SQ   SEQUENCE   1106 AA;  123693 MW;  BF3687D0B040CE6A CRC64;
     MPVMKGLLAP QNTFLDTIAT RFDGTHSNFI LANAQVAKGF PIVYCSDGFC ELAGFARTEV
     MQKSCSCKFL FGVETNEQLM LQIEKSLEEK TEFKGEIMFY KKNGSPFWCL LDIVPIKNEK
     GDVVLFLASF KDITDTKVKI TPEDKKEDKA KGRSRTGTHF 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 VISRLSNKSM VSQSEPKGNG SIKKRLPSIV EDEEEEEDRE
     EEETASLSPI YTRGSSSSRG KKLGSSKSYL GLSLKQLASG TVPFHSPIRV SSSNSPKTRQ
     EADAPNHGKR KEKNLKLQLS TLNNAGPPDL SPRIVDGIED GNYSEESQSF DFGSERVRPE
     PRISPPLGDP EIGAAVLFIK AEETKQQINK LNSEVTTLTQ EVSQLGKDMR TVMQLLEHVV
     SPQQPARFCS LHTTSVCPSS LQTRMTWSTH QPCLHLQAGG AAYTQAQICH GNVNPDTWSV
     DPSSVGSSPQ RTGVYEQNPA GGELYHSPNL DYSPAHYQVV QEGHLQFLRC ISPQSDTTLM
     PLQSISATLS SSVCSSSETS LHLVLPSRSE EGSLGQGAMS SFSLENLPGS WDREGRASIS
     TEPSENFPLE VVTSPAEVKD TNSINV
//
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