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Database: UniProt
Entry: A0A3P8Y4M4_ESOLU
LinkDB: A0A3P8Y4M4_ESOLU
Original site: A0A3P8Y4M4_ESOLU 
ID   A0A3P8Y4M4_ESOLU        Unreviewed;      1154 AA.
AC   A0A3P8Y4M4;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   02-DEC-2020, sequence version 2.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=BK channel {ECO:0000256|ARBA:ARBA00029579};
DE   AltName: Full=Slowpoke homolog {ECO:0000256|ARBA:ARBA00033447};
GN   Name=KCNMA1 {ECO:0000313|Ensembl:ENSELUP00000011627.2};
OS   Esox lucius (Northern pike).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC   Esocidae; Esox.
OX   NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000011627.2, ECO:0000313|Proteomes:UP000265140};
RN   [1] {ECO:0000313|Ensembl:ENSELUP00000011627.2, ECO:0000313|Proteomes:UP000265140}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=25069045;
RA   Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA   von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT   "The genome and linkage map of the northern pike (Esox lucius): conserved
RT   synteny revealed between the salmonid sister group and the Neoteleostei.";
RL   PLoS ONE 9:e102089-e102089(2014).
RN   [2] {ECO:0000313|Ensembl:ENSELUP00000011627.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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; A0A3P8Y4M4; -.
DR   Ensembl; ENSELUT00000000138.2; ENSELUP00000011627.2; ENSELUG00000012230.2.
DR   GeneTree; ENSGT00940000154935; -.
DR   OrthoDB; 2902976at2759; -.
DR   Proteomes; UP000265140; LG06.
DR   Bgee; ENSELUG00000012230; Expressed in liver and 14 other cell types or tissues.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:InterPro.
DR   GO; GO:0005216; F:monoatomic ion channel activity; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; 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; IPR002052; DNA_methylase_N6_adenine_CS.
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.
DR   PROSITE; PS00092; N6_MTASE; 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:UP000265140};
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..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        148..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        186..204
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        269..290
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        306..324
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        336..354
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          149..357
FT                   /note="Ion transport"
FT                   /evidence="ECO:0000259|Pfam:PF00520"
FT   DOMAIN          515..602
FT                   /note="Calcium-activated potassium channel BK alpha
FT                   subunit"
FT                   /evidence="ECO:0000259|Pfam:PF03493"
FT   DOMAIN          968..1091
FT                   /note="Ca2+-activated K+ channel Slowpoke-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21014"
FT   REGION          670..699
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          881..900
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1101..1154
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        678..692
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1101..1129
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1154 AA;  129786 MW;  2A13B007900FE261 CRC64;
     MLVTEHGNLS QGIGSLRIMS KGKHNYYPDS PSVRVSKMDV IIPFSPDVPC DSNGQRMWWA
     FLASSMVTFF GGLFIILLWR TLNYMWTVCC HCNAKKKGSQ RGQNPVSHGD GIKHTKETVA
     ALSEVGWMTS VKDWAGVMIS AQTLTGRVLV VLVFALSIGA LVIYFIDSSD PIESCQNFYK
     DFTLQIDMAF NIFFLLYFGL RFIAANDKLW FWLEVNSVVD FFTVPPVFVS VYLNRSWLGL
     RFLRALRLIQ FSEILQFLNI LKTSNSIKLV NLCSIFISTW LTAAGFIHLV ENSGDPWENF
     QNSQSLSYWE CVYLLMVTMS TVGYGDVYAK TTLGRLFMVF FILGGLAMFA RYVPEIAALI
     LNRKKYGGSY NSTRGRKHIV VCGHITLESV SNFLKDFLHK DRDDVNVEIV FLHNISPNLE
     LEALFKRHFT QVEFYQGSVL NPHDLARVKI ESADACLILA NKYCADPDAE DASNIMRVIS
     IKNYHPKIRI ITQMLQYHNK AHLLNIPSWN WKEGDDAICL AELKLGFIAQ SCLAQGLSTM
     LANLFSMRSF IKIEEDTWQK YYLEGVANEM YTEYLSSAFV GLSFPTICEL CYVKLKLLLI
     AIEYKSDIRE SSTLINPGNH VKMQEGTLGF FIASDAKEVK RALFYCKACH DDITDPKRIK
     KCGCKRVEEE QHSTLSPKRK QRNGNTRNSP HGSPKMMRHD PLLMPGNEQI ENMDVNVKKY
     DSTGMFHWCQ SKDIERVILT RSEAAMTVLS GHVVVCIFGD AKSALVGLRN LVMPLRASNF
     HYHELKPIVF VGSLEYLKRE WETLHNFPKV SILPGTPLSR ADLRAVNINL CDMCVILSAN
     QNNIDDASLQ DKECILASLN IKSMQFDDSI GVLQATSQGF TPPGMDRSSP ENSPAHGGLA
     RQASITTGAN IPIITELVND SNVQFLDQDD DDDPDTELYL TQPFACGTAF AVSVLDSLMS
     ATYFNDNILT LIRTLVTGGA TPELEGLLAE ENALRGGYST PQTLANRDRC RVAQLALYDG
     PFADLGDGGC YGDLFCKALK TYNMLCFGIY RLRDAHLNTQ SHTSLCTKRY VITNPPYGFE
     LVTSDLIFCL MQFDHNAGQS RASLSHSSHS SHTSSRKSVH SIPATNRTNR AKSRDLRDKQ
     KYVPLQTRFP PTRA
//
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