ID A0A3B3QCX0_9TELE Unreviewed; 966 AA.
AC A0A3B3QCX0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Potassium voltage-gated channel subfamily H member 1-like {ECO:0000313|Ensembl:ENSPKIP00000004572.1};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000004572.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000004572.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR AlphaFoldDB; A0A3B3QCX0; -.
DR Ensembl; ENSPKIT00000028556.1; ENSPKIP00000004572.1; ENSPKIG00000021606.1.
DR GeneTree; ENSGT00940000155793; -.
DR Proteomes; UP000261540; Unplaced.
DR GO; GO:0034702; C:monoatomic ion channel complex; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; 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; IPR003949; K_chnl_volt-dep_EAG.
DR InterPro; IPR003938; K_chnl_volt-dep_EAG/ELK/ERG.
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:SF530; POTASSIUM VOLTAGE-GATED CHANNEL SUBFAMILY H MEMBER 1; 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; PR01464; EAGCHANNEL.
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 Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860};
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 227..246
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 356..380
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 428..446
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 458..482
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 100..152
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 574..661
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT REGION 752..866
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 943..966
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 752..790
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 812..826
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 836..866
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 966 AA; 109201 MW; A342BB234F3EA991 CRC64;
MAGGRRGLVA PQNTFLENIV RRSNVWTLSH RQTDTNFVLG NAQIVDWPIV YSNDGFCKLS
GYHRAEVMQK SSTCSFMYGE LTDKETTEKV RLTFENYEMN SFEILMYKKN RTPVWFFVKI
APIRNEQDKV VLFLCTFSDI TAFKQPIEDD SSKGWGKFAR LTRALTSSRG VLQQLQPTVH
KGENVHKHSR LAEVLQLGSD ILPQYKQETP KTPPHIILHY CAFKTTWDWV ILILTFYTAI
MVPYNVSFKT KQNNVTWLVV DSIVDVIFLV DIVLNFHTTF VGPAGEVISD PKLIRMNYLK
TWFVIDLLSC LPYDVINAFE NVDEGISSLF SSLKVVRLLR LGRVARKLDH YIEYGAAVLV
LLVCVFGLAA HWLACIWYSI GDYEVIDEDT NSVRTDSWLY MLAETVGSPY RFNASGLGRW
EGGPSKDSVY ITSLYFTMTS LTSIGFGNIA PTTDGEKIFA VAMMMIGSLL YATIFGNVTT
IFQQMYANTN RYHEMLNSVR DFLKLYQVPK GLSERVMDYI ASTWSMSRGI DTEKVLQICP
KDMRADICVH LNRKVFKEHP AFRLASDGCL RALAMEFQTI HCAPGDLIYH AGESVDSLCF
VVSGSLEVIQ DDEVVAILGK GDVFGDVFWK EVTLAQACAN VRALTYCDLH VIKRDALQKV
LEFYTAFSNH FSRNLLLTYN LRKRIVFRKI SDVKREEEEL LRRKNEAPLN LPPDHPVRRL
FQRFRQQKEA RLAAERTFDE LDVEKGVVQI EQATTHDITP PPTSIVTVTE SPATPVPSVT
AASTSGASDR AKLQAPALGS HPNSKSTEPT RGKGWGRFKE AVGKSDGWSK VSKAESMETL
PERTKSHEET SLKKTDSCDS GITKSDLRLD NVGDARTPQD RSPIQPEVKH TFYPIPEHSI
QASILELKHE LKEDIKALGT RMSILEAQLG EMVRMLKAKR PLDSPQPIFD ISHPGSPESD
KEDIFS
//
