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Database: UniProt
Entry: A0A2D0R3A5_ICTPU
LinkDB: A0A2D0R3A5_ICTPU
Original site: A0A2D0R3A5_ICTPU 
ID   A0A2D0R3A5_ICTPU        Unreviewed;      1198 AA.
AC   A0A2D0R3A5;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2023, sequence version 2.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Potassium voltage-gated channel subfamily H member 8 isoform X1 {ECO:0000313|RefSeq:XP_017325083.2, ECO:0000313|RefSeq:XP_053536906.1};
GN   Name=kcnh3 {ECO:0000313|RefSeq:XP_017325083.2,
GN   ECO:0000313|RefSeq:XP_053536906.1};
OS   Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC   Ictaluridae; Ictalurus.
OX   NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017325083.2};
RN   [1] {ECO:0000313|RefSeq:XP_017325083.2, ECO:0000313|RefSeq:XP_053536906.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_017325083.2,
RC   ECO:0000313|RefSeq:XP_053536906.1};
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_017325083.2; XM_017469594.3.
DR   RefSeq; XP_053536906.1; XM_053680931.1.
DR   STRING; 7998.ENSIPUP00000035402; -.
DR   Ensembl; ENSIPUT00000036791; ENSIPUP00000035402; ENSIPUG00000023740.
DR   KEGG; ipu:108266388; -.
DR   OrthoDB; 66005at2759; -.
DR   Proteomes; UP000221080; Chromosome 6.
DR   GO; GO:0034702; C:monoatomic ion channel complex; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0106151; F:CNBH domain intrinsic ligand binding; IEA:Ensembl.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:Ensembl.
DR   GO; GO:1990573; P:potassium ion import across plasma membrane; IEA:Ensembl.
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:SF641; POTASSIUM VOLTAGE-GATED CHANNEL SUBFAMILY H MEMBER 3 ISOFORM X1; 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   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        231..255
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        267..285
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        316..339
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        360..386
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        515..539
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          42..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          617..734
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   REGION          758..884
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          989..1051
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1068..1117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1176..1198
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        759..777
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        836..857
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        864..884
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1023..1051
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1198 AA;  131656 MW;  3ACA7EFCCDFFA1B8 CRC64;
     MPVMRGLLAP QNTFLDTIAT RFDGTHSNFV LGNAQVQSLY PIVYCSDGFC ELTGYARAEL
     MQKSCACNFL YGPETSDRLT AQIQSALDDR REFKTELVFY KKGGTQFWCL LDIVPIKNEK
     GEVVLFLVSH KDITDNKKDQ DEEQCPEIDE ETGLEVHKVT RPQSFNANRR RSRAVLYQLS
     GHLQKQDKSK LKINNNMFGE KPPIPEYKVA AIQKSRFILL HYGTFKAGWD WLILLATFYV
     AVTVPYNVCF AVVGVRDDMP TPRSPPSVSD ILVEILFMLD IVLNFRTTFV STSGQVVYDA
     RSICVHYVTT WLFVDLIAAL PFDLLYAFNV SVFFGVHLLK TVRLLRLLRL LQKLERYSQY
     SAVVLTLLMS MFALLAHWMA CVWYFIGRCE IENNTPGSWD IGWLHELAKR LGTPYFLSPL
     TSVLPESLRP NNLDGLSGNV SQWNSSSSDI VGQDSVANST QLNGTGAGPV DGVDSVLGGG
     PSVRSSYVTS LYFALSSLTS VGFGNVSANT DSEKIFSICT MLIGALMHAV VFGNVTAIIQ
     RMYSRRSLYH TRTKDLKDFI RVHRLPKALE QRMLECFQTT WSVNNGIDVS ELLKDFPDEL
     RADIAMHLNK ELLLLPLFES ASHGCLRSLS LIIKTSFCAP GEFLIRQGDA LQAIYFVCSG
     SMEVLKDNTV LAILGKGDLI GSDSLTREQV IKTNANVKAL TYCDLQYISL KGLREVLRLY
     PEYAQKFVSE IQHDLTYNLR EGNNTDVDWE SNGGLVKKLP SIREDEENDE EQHSVSRAPR
     SPLRLTRGLS SPLRSPLMPP RPFRPPSDHS RPATLQIPVV SFSSAPPELS PRFVDGIETE
     SNSGSAQRFE FSSNLPHSGP PSPSPVSQEQ VETRQSISKL SEEMNSLSKQ VSQLSEELQE
     MTRLLRPLFL TAAQPLLSTP PPPMTLPGSG PSMNSPAAPY PPAPPCSLLD ITDPVGVVGL
     PSCLIPTSPP QRLQSQVVCS NGSPHASLSH LETIKKDGTG TGQHDIPLGP TNGYGQVAPD
     RLASRATSPS LSFSMSISSS RSQSPSLTPC QGPHPSCPTS CTQGLLFPIS SQDIPPASQD
     NPPPPHSHCS APASLSNSPG DPRLRDGPSL ASSSSTPILQ TLPCSSPSCP HPSPLLLCSL
     RDGQGSMGFP WHRQTSSCAQ AASGTEQPQL ELEMQEWDAG GKSSTEHISF IDEEGPPL
//
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