ID A0A1S3NWH8_SALSA Unreviewed; 1230 AA.
AC A0A1S3NWH8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Potassium voltage-gated channel subfamily H member 7-like isoform X2 {ECO:0000313|RefSeq:XP_014019606.1};
GN Name=LOC106581803 {ECO:0000313|RefSeq:XP_014019606.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014019606.1};
RN [1] {ECO:0000313|RefSeq:XP_014019606.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014019606.1};
RG RefSeq;
RL Submitted (NOV-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 RefSeq; XP_014019606.1; XM_014164131.1.
DR AlphaFoldDB; A0A1S3NWH8; -.
DR OrthoDB; 66005at2759; -.
DR Proteomes; UP000087266; Chromosome ssa21.
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; IPR003967; K_chnl_volt-dep_ERG.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR10217:SF466; POTASSIUM VOLTAGE-GATED CHANNEL SUBFAMILY H MEMBER 7; 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; PR01470; ERGCHANNEL.
DR SMART; SM00100; cNMP; 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; PS50112; PAS; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
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:UP000087266};
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 414..435
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 551..575
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 616..635
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 647..668
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 41..89
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 748..848
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT REGION 171..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 953..972
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1138..1167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1186..1230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1068..1095
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 190..238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1186..1219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1230 AA; 138140 MW; D58FCDF79DFB3A90 CRC64;
MPVRRGHVAP QNTFLGIIIR KFEGQNRKFV IANARVQNCA IIYCNDGFCE MTGYSRPDVM
QKPCTCEFLH GEHTDTHAIS QVDQALMGSE ERKVEITYHR KDGTDFQCYT HIIPVKNEEG
VVMLFILNFD YVLEEGSSDS TEKLNHSSPE RTDSRKGRFF RFRQAAFSLV SNKQSLPQED
PDAVMVDSPS PKQNEDSVAL TNFQSPPTED NCSPTDANDT RALISSSHHS SQASVHGPGP
LDHSSPKQHP WDRLYQTEAH QSTTCLAHTI SRGSISGSSM RRASSVQDIE GFNNSKSMFR
DRHASEGPFN HLKSSLLGST SESNINKYST INKIPLIALN FAERNNENKA HSPPSSENTI
IAPKVKDRTH NVTEKVTQVL SLGADVLPEY KLQTPRMDRF TILHYSPFKA MWDWLILLLV
IYTAILTPYS AAFLLNDREE QMRRECGYSC NPLNVVDFMV DIMFIVDIVI NFRTTYVNLN
EEVVSQPGKI AIHYFKGWFL IDMVAAIPFD LLIFGSGSDE TTTLIGLLKT ARLLRLVRVA
RKLDRYSEYG AAVLILLMCI FALIAHWLAC IWYAIGNVEK PYLEHNIGWL DNLGVSIGKR
YNFSDPSSGP SIKDKYVTAL YFTFSSLTSV GFGNVSPNTN SEKIFSICVM LIGSLMYASI
FGNVSAIIQR LYSGTARYHT QMLRVREFIR FHQIPNPLKQ RLEEYFQHSW TYTNGIDMNT
EVLKGFPECL QADICLHLNQ ALLESCKAFH GATKGCLRAL AMRFQTTHAP PGDTLVHSGD
VLTALYFLSR GSIEILKDDI VVAILGKNDI FGEMIHLYAK PGKSNADVRA LSYCDLHTIQ
RDDLLEVLDM YPEFADFFLT NLELTFNLRD ENGKAAYSHA SDSDPEEDVK STKITRRISF
TPHPTKGEFC VHTLHEHFLL SFFTEQLSQS QRSSVLSLCN TRARCVPLPR LDYNSTGGSN
KETENDSGRE RESYLCLKRT SVDLKQSGKE EQMSKGSAIQ GCPSVEDLAL GLDSNPPGDI
MERTPSYDDN IDLCNDKWVC KKPRDYLDES AQLQDLRGED GDASEITYGE VEQRLDQLEE
HLNRLESQMT SDIQTILQLL QRQSTLGPPA YSTVTASPDY QRPAVRVQPI AALTSTHCFS
HSSSQSPELN LERSHQESKD SLSGLAYMDD SPIEDSLTVL LVQRHTQNKP AGHQHSKSLF
LPIEDSSPLS DSSPNTGLHR PVSDPGPPRP
//
