ID A0A1S3S3E9_SALSA Unreviewed; 1100 AA.
AC A0A1S3S3E9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Potassium voltage-gated channel subfamily KQT member 5-like isoform X6 {ECO:0000313|RefSeq:XP_014058897.1};
GN Name=LOC106606915 {ECO:0000313|RefSeq:XP_014058897.1};
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_014058897.1};
RN [1] {ECO:0000313|RefSeq:XP_014058897.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014058897.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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DR RefSeq; XP_014058897.1; XM_014203422.1.
DR AlphaFoldDB; A0A1S3S3E9; -.
DR GeneID; 106606915; -.
DR OrthoDB; 2911641at2759; -.
DR Proteomes; UP000087266; Chromosome ssa01.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR Gene3D; 1.10.287.70; -; 1.
DR Gene3D; 6.10.140.1910; -; 2.
DR Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 1.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR003937; K_chnl_volt-dep_KCNQ.
DR InterPro; IPR013821; K_chnl_volt-dep_KCNQ_C.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR47735; POTASSIUM VOLTAGE-GATED CHANNEL SUBFAMILY KQT MEMBER 4; 1.
DR PANTHER; PTHR47735:SF8; POTASSIUM VOLTAGE-GATED CHANNEL SUBFAMILY KQT MEMBER 5; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF03520; KCNQ_channel; 2.
DR PRINTS; PR00169; KCHANNEL.
DR PRINTS; PR01459; KCNQCHANNEL.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
PE 4: Predicted;
KW Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..1100
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010380446"
FT TRANSMEM 144..166
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 178..200
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 221..240
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 288..307
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 345..371
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 144..375
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 486..614
FT /note="Potassium channel voltage dependent KCNQ C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03520"
FT DOMAIN 689..751
FT /note="Potassium channel voltage dependent KCNQ C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03520"
FT REGION 424..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 509..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 778..809
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 834..953
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 986..1025
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1071..1100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..498
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 864..879
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 921..953
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 986..1016
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1071..1094
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1100 AA; 120790 MW; 24EAF524168783A4 CRC64;
MNIAVWFCFL HLCANSSTLY VHVPGTSCTS PAGVGDAMPR NHSADEAGTG LWMKTSPGRR
AQDYGLKDVE SGRRMMNNAV RVGDGMFSLG PAGADGAERQ KGARLSLLGK PLIYSAQSGR
RNVRYRRLQN YLYNVLERPR AWAFIYHAFV FILVFGCLVL SVFSTIPAHQ DLSNHCLLIL
VSEFVMIVVF GLEYIIRIWS AGCCCRYRGW QGRLRFARKP FCVIDIIVLI ASIAVVSAGS
QGNIFATSAL RSLRFLQILR MVRMDRRGGT WKLLGSVVYA HSKELVTAWY IGFLVLIFSS
FLVYLVEKEF NKDFATYADA LWWGTITLTT IGYGDKTPQT WTGRLISAGF ALMGISFFAL
PAGILGSGFA LKVQEQHRQK HFEKRRNPAA SLIQAAWRLY STDGARPYLS ATWQHYQGAL
SPFRKEQGET TSSKGHSNRR RFRSTKLSFK ERVRMASPRG QSMKSRQTSI NNDRRCSPGN
DVAGANTGTS PAKVQKSWSF NDRTRFRPSL RLKSQSRTAP SEVDTGMGND DAFGDRVCHC
DVTVEDLSAP LKAVIRAVRI MKFHVAKKKF KETLRPYDVK DVIEQYSAGH LDMLCRIKSL
QTRLDTIVGP PQQQLLSPRV KTFSSPSLHV YYNQARRKSM PGTKSVPGLA TGLGPTLSSK
PGNMSSPSLQ LYYSQARRKS APGMKSPGVD QILGKGQIPI DKKIRDKLHP DRDTLEDMSM
LGRVCKVERQ VTSIESKLDS LLDVYRQVLQ NGSSSLTLSS LPLFELEHQT SDYRSSILSK
DLSSGSPQGG EGRGGHKSGG GMSRSTTGHL SRGLQLILAP SELTLNTCPP SYPASTASLT
PSPLLPPDSP YPLLTTPSSF PRRAHFPDLP PPPPSAGAAT LQLPPMGPQQ RRPLSPTPHA
TRGGRLEQSS GLSMVVVSGV DHGEEGDREG GHSWGRVQLR GKPHLREEGP WRRHMSLEVD
PMLLLSSGCD GKPSEQEQGL GKSLSAHNLT QPSADNLPNL SFPLSNSSSS SDDCHGDPDA
SNWGETDLFI TGRDLEPQED QFDFLSQGSD LLSHPTADGT GCLDVLRTED GGSLTSLTGP
HTPTTGSAES LNQPTHVRLK
//
