ID A0A1S3Q8V1_SALSA Unreviewed; 1002 AA.
AC A0A1S3Q8V1;
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=LOC106589905 {ECO:0000313|RefSeq:XP_014035819.1};
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_014035819.1};
RN [1] {ECO:0000313|RefSeq:XP_014035819.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014035819.1};
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_014035819.1; XM_014180344.1.
DR AlphaFoldDB; A0A1S3Q8V1; -.
DR OrthoDB; 2902976at2759; -.
DR Proteomes; UP000087266; Chromosome ssa28.
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_014035819.1};
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 37..57
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 122..143
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 159..177
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 189..207
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 5..210
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 368..455
FT /note="Calcium-activated potassium channel BK alpha
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF03493"
FT DOMAIN 821..944
FT /note="Ca2+-activated K+ channel Slowpoke-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21014"
FT REGION 526..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 954..1002
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..546
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 954..984
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 985..1002
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1002 AA; 112752 MW; 98209F9F2F98A456 CRC64;
MNVVLVFALS IGALVIYFID SSDPIESCQN FYKDFTLQID MAFNVFFLLY FGLRFIAAND
KLWFWLEVNS VVDFFTVPPV FVSVYLNRSW LGLRFLRALR LIQFSEILQF LNILKTSNSI
KLVNLCSIFI STWLTAAGFI HLVENSGDPW ENFQNSQSLS YWECVYLLMV TMSTVGYGDV
YAKTTLGRLF MVFFILGGLA MFARYVPEIA ALILNRKKYG GSYNSTRGRK HIVVCGHITL
ESVSNFLKDF LHKDRDDVNV EIVFLHNISP NLELEALFKR HFTQVEFYQG SVLNPHDLAR
VKIESADACL ILANKYCADP DAEDASNIMR VISIKNYHPK IRIITQMLQY HNKAHLLNIP
SWNWKEGDDA ICLAELKLGF IAQSCLAQGL STMLANLFSM RSFIKIEEDT WQKYYLEGVA
NEMYTEYLSS AFVGLSFPTI CELCYVKLKL LLIAIEYKSD IRESSTLINP GNHVKMQEGT
LGFFIASDAK EVKRALFYCK ACHDDITDPK RIKKCGCKRL EEEQQSAVSP KKKQVNGNTR
NSPNGSPKMM RHDPLLMPGK EQIENMDVNV KKYDSTGMFH WCQSKDIEKV ILTRSEAAMT
VLSGHVVVCI FGDAKSALVG LRNLVMPLRA SNFHYHELKP IVFVGSLEYL KREWETLHNF
PKVSILPGTP LSRADLRAVN INLCDMCVIL SANQSNIDDA SLQDKECILA SLNIKSMQFD
DSIGVLQATS QGFTLPGMDR SSPENSPVHG GLVRQASITT GANVPIITEL VNDSNVQFLD
QDDDDDPDTE LYLTQPFACG TAFAVSVLDS LMSATYFNDN ILTLIRTLVT GGATPELEGL
LAEENALRGG YSTPQTLANR DRCRVAQLAL YDGPFADLGD GGCYGDLFCK ALKTYNMLCF
GIYRLRDAHL NTQSHTSQCT KRYVITNPPY GFELVPSDLI FCLMQFDHNA GQSQASLTHS
SHSSHSSSKK SSSVHSIPAT NRTNRAKSRD SRDKQKKDML YR
//
