ID A0A1S3N566_SALSA Unreviewed; 1334 AA.
AC A0A1S3N566;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=BK channel {ECO:0000256|ARBA:ARBA00029579};
DE AltName: Full=Slowpoke homolog {ECO:0000256|ARBA:ARBA00033447};
GN Name=LOC106577193 {ECO:0000313|RefSeq:XP_014010537.1};
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_014010537.1};
RN [1] {ECO:0000313|RefSeq:XP_014010537.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014010537.1};
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}.
CC -!- SIMILARITY: Belongs to the potassium channel family. Calcium-activated
CC (TC 1.A.1.3) subfamily. KCa1.1/KCNMA1 sub-subfamily.
CC {ECO:0000256|ARBA:ARBA00008648}.
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DR RefSeq; XP_014010537.1; XM_014155062.1.
DR OrthoDB; 2902976at2759; -.
DR Proteomes; UP000087266; Chromosome ssa18.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005216; F:monoatomic ion channel activity; IEA:InterPro.
DR GO; GO:0006813; P:potassium ion transport; IEA:InterPro.
DR Gene3D; 1.10.287.70; -; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR003929; K_chnl_BK_asu.
DR InterPro; IPR047871; K_chnl_Slo-like.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR048735; Slowpoke-like_C.
DR PANTHER; PTHR10027; CALCIUM-ACTIVATED POTASSIUM CHANNEL ALPHA CHAIN; 1.
DR PANTHER; PTHR10027:SF33; CALCIUM-ACTIVATED POTASSIUM CHANNEL SUBUNIT ALPHA-1; 1.
DR Pfam; PF03493; BK_channel_a; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF21014; Slowpoke_C; 1.
DR PRINTS; PR01449; BKCHANNELA.
DR PRINTS; PR00169; KCHANNEL.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Ion channel {ECO:0000256|ARBA:ARBA00023303,
KW ECO:0000313|RefSeq:XP_014010537.1};
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}.
FT TRANSMEM 56..78
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 152..170
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 190..208
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 273..294
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 310..328
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 340..358
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 153..369
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 519..606
FT /note="Calcium-activated potassium channel BK alpha
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF03493"
FT DOMAIN 1102..1222
FT /note="Ca2+-activated K+ channel Slowpoke-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21014"
FT REGION 102..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 775..807
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1231..1298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 784..804
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1231..1264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1334 AA; 149618 MW; FD5652684A6FA337 CRC64;
MLAEADATVP HGSGNSMMSR NNYFNKNPDS SISMSKMDVI IPFSPDVPCD NNGQRMWWAF
LASSMVTFFG GLFIILLWRT LKYLWTVCCH CNIKKKEAQK VNNPANSQVA DGTAKGPDEK
DEVVPASEVG WMTSVKDWAG VMISAQTLTG RVLVVLVFAL SIGALGIYFI DSSDPIESCQ
NFYKDFTLQI DMFFNVFFLL YFGLRFIAAN DKLWFWLEVN SVVDFFTVPP VFVSVYLNRS
WLGLRFLRAL RLIQFSEILQ FLNILKTSNS IKLVNLCSIF ISTWLTAAGF IHLVENSGDP
WENFQNSQSL SYWECVYLLM VTMSTVGYGD VYAKTTLGRL FMVFFILGGL AMFASYVPEI
IELIGNRKKY GGSYSAVNGR KHIVVCGHIT LESVSNFLKD FLHKDRDDVN VEIVFLHNIS
PNLELEALFK RHFTQVEFYQ GSVLNPHDLA RVKIESADAC LILANKYCPD PDAEDASNIM
RVISIKNYSP KIRIITQMLQ YHNKAHLLNI PSWNWKEGDD AICLAELKAG FIAQSCLAQG
LSTMLANLFS MRSFIEIEED TWQKYYLEGV ANEMYTEYLS SAFVGLSFPA VCELCYVKLK
LLLIAIENKS ELGESRSRKR ILINPGNHVK MQEGTLGFFI ASDAKEVKRA FFYCKACHDD
ITDPKRIKKC GCKRLIYSKM SAYKQMKLAC CFDCGRSERD CSCMSGSVHS NMDTLQRAYP
LSSVSVHDCA TTLRASKYKY NGYVRSPEGA TTPGKTGSQK ETGVRFKADC NLVEDEHPST
LSPKKKQRNG GMRNSPNNSP NMMSRHDPLV IPGNEQMENM DMNMKQYDST GMFHWCPSKE
IEKVILTRSE ASMTVLSGHV VVCIFGDVTS ALVGLRNLVM PLRASNFHYH ELKPIVFVGS
LEYLRREWET LHNFPKVSIL PGTPLSRADL RAVNINLCDM CVILSANQNN IDDASLQDKE
CILASLNIKS MQFDDSIGLL QANSQGFTPP GMDRSSPDSS PVHGLARQAS VTTGANIPII
TELAKPGKIL PLVSFSQEKK LGINIQMITE LVNDSNVQFL DQDDDDDPDT ELYLTQPFAC
GTAFAVSVLD SLMSATYFND NILTLIRTLV TGGATPELEA LLAEENALQG GYSTPQTLAN
RDRCRVAQLA LYDGPFADLG DGGCYGDLFC KALKTYNMLC FGIYRLRDAH LATPSQCTKR
YVITNPPYEF ELVPTDLIFC LMQFDHNAGQ SRTSLSHSSH SSHSSSKKSS SVHSIPTTNR
QNRSSKAREA GHKQNATRMN RMSQERKWFT DEPENAYPRN IQIKPMSTHM ANQVNQYKST
SSLIPPIREV EDEC
//
