ID A0A1S3STD1_SALSA Unreviewed; 1337 AA.
AC A0A1S3STD1;
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=LOC106611671 {ECO:0000313|RefSeq:XP_014067594.1};
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_014067594.1};
RN [1] {ECO:0000313|RefSeq:XP_014067594.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014067594.1};
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_014067594.1; XM_014212119.1.
DR PaxDb; 8030-ENSSSAP00000108122; -.
DR KEGG; sasa:106611671; -.
DR OrthoDB; 2902976at2759; -.
DR Proteomes; UP000087266; Chromosome ssa01.
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:SF41; 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_014067594.1};
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 39..61
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 130..148
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 168..186
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 251..272
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 287..306
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 318..336
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 131..347
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 497..584
FT /note="Calcium-activated potassium channel BK alpha
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF03493"
FT DOMAIN 1156..1279
FT /note="Ca2+-activated K+ channel Slowpoke-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21014"
FT REGION 766..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 856..888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1289..1337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..791
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 866..881
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1289..1319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1320..1337
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1337 AA; 149663 MW; EB57A6CCEACA9590 CRC64;
MPKGKHSYYP DSPSIRISKM DVIIPFSPDV PCDSNGQRMW WAFLASSMVT FFGGLFIILL
WRTLKYLWTV CCHCNTKKKN AQRVHNPTSH GDGIKHTKET VAALSEVGWM TSVKDWAGVM
ISAQTLTGRV LVVLVFALSI GALVIYFIDS SDPIESCQNF YKDFTLQIDM AFNVFFLLYF
GLRFIAANDK LWFWLEVNSV VDFFTVPPVF VSVYLNRSWL GLRFLRALRL IQFSEILQFL
NILKTSNSIK LVNLCSIFIS TWLTAAGFIH LVENSGDPWE NFQNSQALSY WECVYLLMVT
MSTVGYGDVY AKTTLGRLFM VFFILGGLAM FASYVPEIIE LIGNRKKYGG SYSAVNGRKH
IVVCGHITLE SVSNFLKDFL HKDRDDVNVE IVFLHNISPN LELEALFKRH FTQVEFYQGS
VLNPHDLARV KIESADACLI LANKYCADPD AEDASNIMRV ISIKNYHPKI RIITQMLQYH
NKAHLLNIPS WNWKEGDDAI CLAELKLGFI AQSCLAQGLS TMLANLFSMR SFIKIEEDTW
QKYYLEGVAN EMYTEYLSSA FVGLSFPTIC ELCYVKLKLL LIAIEYKSDI RESSTLINPG
NHVKMQEGTL GFFIASDAKE VKRALFYCKA CHDDITDPKR IKKCGCKRLL YSKMSVYKRM
MLACCFDCGH SECDCSCMSA NVHHDSSTKD TLQQRGFPLS PVSLNDFSTT LSASKNNYNG
YIKSIKDNTH IKRSTYQNKS IKLNHNSTAN AAHHKVATPH SGVVLPGSGS GSGSVPLVNN
RKGSLQPSRG PSVLRRSLLG SRELVEVARG PGGPGGLAAE EASRLQRARS LPVKYRYQLS
HSSNATLLNM RHCTFEEEQH STLSPKKKQR NGNTRNSPNG SPKMMRHDPL LMPGNEQIEN
MDMNVKKYDS TGMFHWCQSK DIEKVILTRS EAAMTVLSGH VVVCIFGDAK SALVGLRNLV
MPLRASNFHY HELKPIVFVG SLEYLKREWE TLHNFPKVSI LPGTPLSRAD LRAVNINLCD
MCVILSANQN NIDDASLQDK ECILASLNIK SMQFDDSIGV LQANSQGFTP PGMDRSSPEN
SPLHGGLVRQ ASITTGANIP IITELVNDSN VQFLDQDDDD DPDTELYLTQ PFACGTAFAV
SVLDSLMSAT YFNDNILTLI RTLVTGGATP ELEGLLAEEN ALRGGYSTPQ TLANRDRCRV
AQLALYDGPF ADLGDGGCYG DLFCKALKTY NMLCFGIYRL RDAHLNTQSH TSQCTKRYVI
TNPPYGFELV PSDLIFCLMQ FDHNAGQSRA SLSHSSHSSH SSSKKSSSVH SLTATNRTNR
AKNRDSRDKQ KKDMVYR
//
