ID A0A3P8U5J0_AMPPE Unreviewed; 725 AA.
AC A0A3P8U5J0;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Potassium voltage-gated channel, subfamily H (eag-related), member 3 {ECO:0000313|Ensembl:ENSAPEP00000030578.1};
OS Amphiprion percula (Orange clownfish) (Lutjanus percula).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=161767 {ECO:0000313|Ensembl:ENSAPEP00000030578.1, ECO:0000313|Proteomes:UP000265080};
RN [1] {ECO:0000313|Ensembl:ENSAPEP00000030578.1, ECO:0000313|Proteomes:UP000265080}
RP NUCLEOTIDE SEQUENCE.
RA Lehmann R.;
RT "Finding Nemo's genes: A chromosome-scale reference assembly of the genome
RT of the orange clownfish Amphiprion percula.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPEP00000030578.1}
RP IDENTIFICATION.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A3P8U5J0; -.
DR Ensembl; ENSAPET00000031396.1; ENSAPEP00000030578.1; ENSAPEG00000021607.1.
DR GeneTree; ENSGT00940000165242; -.
DR Proteomes; UP000265080; Chromosome 12.
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: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 Reference proteome {ECO:0000313|Proteomes:UP000265080};
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 228..250
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 270..290
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 325..347
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 359..385
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 450..474
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 552..669
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT REGION 136..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 725 AA; 81627 MW; C5293569DD3ACADB CRC64;
MPVMRGLLAP QNTFLDTIAT RFDGTHSNFV LGNAQVQSLY PIVYCSDGFC ELTGYARAEL
MQKSCACHFL YGPETSDRST AQIQGALDDR REFKTELVFY KKEGTQFWCL LDIVPIKNEK
GEVVLFLVSH KDITDKKKDQ DPEQGPDTGK FMEKTVTRPP GFNANRRRSR AVLYHLSGHL
QKQDKSKLKI NNNMFGEKPP IPEYKVAAIQ KSRFILLHYG TFKAGWDWLI LLATFYVAVT
VPYNVCFTVG GGRDEGSSSA PRSPPSVSDI LVEILFILDI LLNFRTTFVS TSGQVVYDAR
SICVHYVTTW LFVDLIAALP FDLLYAFNVS VYFGVHLLKT VRLLRLLRLL QKLERYSQYS
AVVLTLLMSM FALLAHWMAC VWYFIGRREI ESPGSWDIGW LHELAKRGGG NLGGGPSMRS
SYVTSLYFAL SSLTSVGFGN VSANTDSEKI FSICTMLIGA LMHAVVFGNV TAIIQRMYSR
RSLYHTRTKD LKDFIRVHRL PKALEQRMLE CFQTTWSVNN GIDVSELLKD FPDELRADIA
MHLNKELLQL PLFESASRGC LRSLSLIIKT SFCAPGEFLI RQGDALQAIY FVCSGSMEVL
KDNTVLAILG KGDLIGSDSL TKEQVIKTNA NVKALTYCDL QYISLKGLRE VLRLYPEYAQ
KFISEIQHDL TYNLREGHGA DVTNLSEVTQ KSSKMSSNLS KMTKTVFKMT QKVSQMTTAV
NLSTS
//
