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Database: UniProt
Entry: A0A2U4B9U6_TURTR
LinkDB: A0A2U4B9U6_TURTR
Original site: A0A2U4B9U6_TURTR 
ID   A0A2U4B9U6_TURTR        Unreviewed;      1106 AA.
AC   A0A2U4B9U6;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   07-OCT-2020, sequence version 2.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Potassium voltage-gated channel subfamily H member 8 {ECO:0000313|RefSeq:XP_019789988.2};
GN   Name=KCNH8 {ECO:0000313|RefSeq:XP_019789988.2};
OS   Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Delphinidae; Tursiops.
OX   NCBI_TaxID=9739 {ECO:0000313|Proteomes:UP000245320, ECO:0000313|RefSeq:XP_019789988.2};
RN   [1] {ECO:0000313|RefSeq:XP_019789988.2}
RP   IDENTIFICATION.
RC   TISSUE=Spleen {ECO:0000313|RefSeq:XP_019789988.2};
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_019789988.2; XM_019934429.2.
DR   AlphaFoldDB; A0A2U4B9U6; -.
DR   STRING; 9739.ENSTTRP00000008021; -.
DR   InParanoid; A0A2U4B9U6; -.
DR   OrthoDB; 66005at2759; -.
DR   Proteomes; UP000245320; Chromosome 4.
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.
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:UP000245320};
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..748
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          764..791
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   COILED          854..888
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        728..748
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;  123494 MW;  3363596E6002A321 CRC64;
     MPVMKGLLAP QNTFLDTIAT RFDGTHSNFI LANAQVAKGF PIVYCSDGFC ELAGFARTEV
     MQKSCSCKFL FGVETNEQLM LQIEKSLEEK AEFKGEIMFY 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 EMEDNSLLKW EVGWLPELGK 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 VSQPEPKGNG SIKKRLPSIV EDEEEEENRE
     EEETASLSPI YTRGSSSSRS KRPGSSKSYL GLSLKQLASG TVPFHSPVRV SSSNSPKSKQ
     EADAPNHGKR KEKNLKLQLS ALNNAGPPDL SPRVVDGIED GNCSEESQSF DFGSERVRPE
     PRISPPLGDP EIGAAVLFIK AEETKQQINK LNSEVTTLTQ EVSQLGKDMR TVMQLLEHVV
     SPQQPARFCS LHTTSVCPSS LQTRMTWSTH QPCLHLQAGG AAYTQAQLCH GNVTPDIWSV
     DPSSVGSSPQ RTGVYEQNPA GGELYHSPNL DYSPARYQVV QEGRLQFLRC ISPQSDTTLM
     PLQSISATLS SSVCSSSETS LHLVLPSRSE EGSLGQGAMS SFSLENLPGS WDREGRASIT
     TEPSENFPLE VVTSPAEVND TKAINV
//
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