ID A0A3Q3E842_9LABR Unreviewed; 1095 AA.
AC A0A3Q3E842;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=BK channel {ECO:0000256|ARBA:ARBA00029579};
DE AltName: Full=Slowpoke homolog {ECO:0000256|ARBA:ARBA00033447};
GN Name=KCNMA1 {ECO:0000313|Ensembl:ENSLBEP00000003233.1};
OS Labrus bergylta (ballan wrasse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Labriformes; Labridae; Labrus.
OX NCBI_TaxID=56723 {ECO:0000313|Ensembl:ENSLBEP00000003233.1, ECO:0000313|Proteomes:UP000261660};
RN [1] {ECO:0000313|Ensembl:ENSLBEP00000003233.1}
RP IDENTIFICATION.
RG Ensembl;
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 AlphaFoldDB; A0A3Q3E842; -.
DR STRING; 56723.ENSLBEP00000003233; -.
DR Ensembl; ENSLBET00000003404.1; ENSLBEP00000003233.1; ENSLBEG00000002458.1.
DR GeneTree; ENSGT00940000154935; -.
DR InParanoid; A0A3Q3E842; -.
DR Proteomes; UP000261660; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:Ensembl.
DR GO; GO:0015269; F:calcium-activated potassium channel activity; IEA:Ensembl.
DR GO; GO:0010996; P:response to auditory stimulus; IEA:Ensembl.
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:SF42; 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 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:UP000261660};
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 57..78
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 98..114
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 134..152
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 217..238
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 254..272
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 284..302
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 100..313
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 463..550
FT /note="Calcium-activated potassium channel BK alpha
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF03493"
FT DOMAIN 916..1036
FT /note="Ca2+-activated K+ channel Slowpoke-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21014"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 616..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1045..1095
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..641
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1045..1077
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1078..1095
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1095 AA; 123259 MW; B2D67055F1E919FE CRC64;
MLAEADGTVP HGSDSSMRTS NINNNINPDS SILISKMEDV VIPFSSEVPC DNNGQRMWWA
FLASSMVTFF GGLFIILLWR TLKYLWTVCC HCNIKPKVVL VFALSIGALG IYFIDSSDPI
ESCQNFYKDF TLQIDMAFNV FFLLYFGLRF IAANDKLWFW LEVNSVVDFF TVPPVFVSVY
LNRSWLGLRF LRALRLIQFS EILQFLNILK TSNSIKLVNL CSIFISTWLT AAGFIHLVEN
SGDPWENFQN SQSLSYWECV YLLMVTMSTV GYGDVYAKTT LGRLFMVFFI LGGLAMFASY
VPEIIELIGN RKKYGGSYSA VNGRKHIVVC GHITLESVSN FLKDFLHKDR DDVNVEIVFL
HNISPNLELE ALFKRHFTQV EFYQGSVLNP HDLARVKIES ADACLILANK YCADPDAEDA
SNIMRVISIK NYSPKIRIIT QMLQYHNKAH LLNIPSWNWR EGDDAICLAE LKAGFIAQSC
LAQGLSTMLA NLFSMRSFIE IEEDTWQKYY LEGVANEMYT EYLSSAFVGL SFPTVCELCY
VKLKLLLIAI EYKSEQRESS ILINPGNHVK LQEGTLGFFI ASDAKEVKRA FFYCKACHDD
ITDPKRIKKC GCKRLEDEHP STLSPKKKQR NGGMRNSPNC SPKMMSRHDP LLIPGNEQIE
NMDMNVKRYD STGMFHWCPS KEIEKVILTR SEASMTVLSG HVVVCIFGDV TSALVGLRNL
VMPLRASNFH YHELKPIVFV GSLDYLRREW ETLHNFPKVS ILPGTPLSRA DLRAVNINLC
DMCVILSANQ NNIEDASLQD KECILASLNI KSMQFDDSIG VLQANSQGFT PPGMDRSSPD
SSPVHGFVRQ ASVTTGSNIP IITELVNDSN VQFLDQDDDD DPDTELYLTQ PFACGTAFAV
SVLDSLMSAT YFNDNILTLI RTLVTGGATP ELEGLLAEEN ALRGGYSTPQ TLANRDRCRV
AQLALYDGPF ADLGDGGCYG DLFCKALKTY NMLCFGIYRL RDAHLGSPSQ CTKRYVITNP
PYEFELVPSD LIFCLMQFDH NAGQSRTSLS HSSHSSHSSS KKSSSVHSIP PSNRQNRSSK
TREGRDKQKK EMVYR
//
