ID A0A1S3N5E2_SALSA Unreviewed; 1430 AA.
AC A0A1S3N5E2;
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_014010530.1};
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_014010530.1};
RN [1] {ECO:0000313|RefSeq:XP_014010530.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014010530.1};
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_014010530.1; XM_014155055.1.
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_014010530.1};
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 1198..1318
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 800..869
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 890..929
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1327..1394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 893..907
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 908..928
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1327..1360
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1430 AA; 159983 MW; 3012744112D4689A 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 NLVKDEVRSS
LQNPSIKISN CTAPSSCITS NAIHPQAPPR PSRHKDPLVP RDADPAVPLV NNRKGSLLPP
RMGLGLRFSI SGPSRGDGTG RALAEQSRLN RARSLPVKYR YHPSNAALHD YSSSRAFEDE
HPSTLSPKKK QRNGGMRNSP NNSPNMMSRH DPLVIPGNEQ MENMDMNMKQ YDSTGMFHWC
PSKEIEKVIL TRSEASMTVL SGHVVVCIFG DVTSALVGLR NLVMPLRASN FHYHELKPIV
FVGSLEYLRR EWETLHNFPK VSILPGTPLS RADLRAVNIN LCDMCVILSA NQNNIDDASL
QDKECILASL NIKSMQFDDS IGLLQANSQG FTPPGMDRSS PDSSPVHGLA RQASVTTGAN
IPIITELVND SNVQFLDQDD DDDPDTELYL TQPFACGTAF AVSVLDSLMS ATYFNDNILT
LIRTLVTGGA TPELEALLAE ENALQGGYST PQTLANRDRC RVAQLALYDG PFADLGDGGC
YGDLFCKALK TYNMLCFGIY RLRDAHLATP SQCTKRYVIT NPPYEFELVP TDLIFCLMQF
DHNAGQSRTS LSHSSHSSHS SSKKSSSVHS IPTTNRQNRS SKAREAGHKQ NATRMNRMSQ
ERKWFTDEPE NAYPRNIQIK PMSTHMANQV NQYKSTSSLI PPIREVEDEC
//
