ID L1JCR4_GUITC Unreviewed; 1141 AA.
AC L1JCR4;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=BK channel {ECO:0000256|ARBA:ARBA00029579};
GN ORFNames=GUITHDRAFT_138739 {ECO:0000313|EMBL:EKX45914.1};
OS Guillardia theta (strain CCMP2712) (Cryptophyte).
OC Eukaryota; Cryptophyceae; Pyrenomonadales; Geminigeraceae; Guillardia.
OX NCBI_TaxID=905079 {ECO:0000313|EMBL:EKX45914.1};
RN [1] {ECO:0000313|EMBL:EKX45914.1, ECO:0000313|Proteomes:UP000011087}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCMP2712 {ECO:0000313|EMBL:EKX45914.1,
RC ECO:0000313|Proteomes:UP000011087};
RX PubMed=23201678; DOI=10.1038/nature11681;
RG DOE Joint Genome Institute;
RA Curtis B.A., Tanifuji G., Burki F., Gruber A., Irimia M., Maruyama S.,
RA Arias M.C., Ball S.G., Gile G.H., Hirakawa Y., Hopkins J.F., Kuo A.,
RA Rensing S.A., Schmutz J., Symeonidi A., Elias M., Eveleigh R.J.,
RA Herman E.K., Klute M.J., Nakayama T., Obornik M., Reyes-Prieto A.,
RA Armbrust E.V., Aves S.J., Beiko R.G., Coutinho P., Dacks J.B.,
RA Durnford D.G., Fast N.M., Green B.R., Grisdale C.J., Hempel F.,
RA Henrissat B., Hoppner M.P., Ishida K., Kim E., Koreny L., Kroth P.G.,
RA Liu Y., Malik S.B., Maier U.G., McRose D., Mock T., Neilson J.A.,
RA Onodera N.T., Poole A.M., Pritham E.J., Richards T.A., Rocap G., Roy S.W.,
RA Sarai C., Schaack S., Shirato S., Slamovits C.H., Spencer D.F., Suzuki S.,
RA Worden A.Z., Zauner S., Barry K., Bell C., Bharti A.K., Crow J.A.,
RA Grimwood J., Kramer R., Lindquist E., Lucas S., Salamov A., McFadden G.I.,
RA Lane C.E., Keeling P.J., Gray M.W., Grigoriev I.V., Archibald J.M.;
RT "Algal genomes reveal evolutionary mosaicism and the fate of
RT nucleomorphs.";
RL Nature 492:59-65(2012).
RN [2] {ECO:0000313|Proteomes:UP000011087}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCMP2712 {ECO:0000313|Proteomes:UP000011087};
RA Kuo A., Curtis B.A., Tanifuji G., Burki F., Gruber A., Irimia M.,
RA Maruyama S., Arias M.C., Ball S.G., Gile G.H., Hirakawa Y., Hopkins J.F.,
RA Rensing S.A., Schmutz J., Symeonidi A., Elias M., Eveleigh R.J.,
RA Herman E.K., Klute M.J., Nakayama T., Obornik M., Reyes-Prieto A.,
RA Armbrust E.V., Aves S.J., Beiko R.G., Coutinho P., Dacks J.B.,
RA Durnford D.G., Fast N.M., Green B.R., Grisdale C., Hempe F., Henrissat B.,
RA Hoppner M.P., Ishida K.-I., Kim E., Koreny L., Kroth P.G., Liu Y.,
RA Malik S.-B., Maier U.G., McRose D., Mock T., Neilson J.A., Onodera N.T.,
RA Poole A.M., Pritham E.J., Richards T.A., Rocap G., Roy S.W., Sarai C.,
RA Schaack S., Shirato S., Slamovits C.H., Spencer D.F., Suzuki S.,
RA Worden A.Z., Zauner S., Barry K., Bell C., Bharti A.K., Crow J.A.,
RA Grimwood J., Kramer R., Lindquist E., Lucas S., Salamov A., McFadden G.I.,
RA Lane C.E., Keeling P.J., Gray M.W., Grigoriev I.V., Archibald J.M.;
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblProtists:EKX45914}
RP IDENTIFICATION.
RG EnsemblProtists;
RL Submitted (MAR-2016) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; JH992997; EKX45914.1; -; Genomic_DNA.
DR RefSeq; XP_005832894.1; XM_005832837.1.
DR AlphaFoldDB; L1JCR4; -.
DR STRING; 905079.L1JCR4; -.
DR PaxDb; 55529-EKX45914; -.
DR EnsemblProtists; EKX45914; EKX45914; GUITHDRAFT_138739.
DR GeneID; 17302428; -.
DR KEGG; gtt:GUITHDRAFT_138739; -.
DR eggNOG; KOG1420; Eukaryota.
DR HOGENOM; CLU_008855_0_0_1; -.
DR OMA; AWNQSRT; -.
DR OrthoDB; 5479588at2759; -.
DR Proteomes; UP000011087; Unassembled WGS sequence.
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 Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 1.
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; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR10027; CALCIUM-ACTIVATED POTASSIUM CHANNEL ALPHA CHAIN; 1.
DR PANTHER; PTHR10027:SF10; SLOWPOKE 2, ISOFORM D; 1.
DR Pfam; PF03493; BK_channel_a; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR PRINTS; PR00169; KCHANNEL.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
PE 4: Predicted;
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:UP000011087};
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 29..56
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 76..98
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 110..129
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 179..200
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 247..265
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 38..261
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 437..523
FT /note="Calcium-activated potassium channel BK alpha
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF03493"
FT REGION 998..1026
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1059..1141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1059..1126
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1141 AA; 128150 MW; DE379C143A1EB849 CRC64;
MGNYWGKFKL AFAAASEEAE RTRKDFASWL LSSFWGLLFD LSTCIFSLLS VGIYIYQTYF
PDLSVVSESQ KNVLSSLEQI ELIITFIFLS DFVIYLYAAE SRLKHLIQPL IVVDFVTIMP
ALVIFAVKQS MNAQSSPVDK ASKLNFLRFV RVLKLLRVLR LIRTTRGRPQ VGTEVTRQIF
TMVLTALSLI FCFAGLIQVV ELTFRSPEDL ADIWNHPEPG FSFHDAVYFT IITVSTVGYG
DFYPTTVLGK FLTMIMILSS LATITDQINK LMELLSMASP WARATYQSAK YPHVLLCGNV
THSSIRDFLE EFFHPDHGMS DTKVVILGNQ VPSASLLSLL SSANYSLRTV YLEGSALVDK
DLQRADIINC LCVFILCDKF AEDPFAEDSS NIIRAISIKK YVSARRPGED IRIILQLLRP
ENRHHLNVST CGGTDVQIIC MDEIKMNLLG KSCLCPGFST LISNLMISSG QSGDECERWM
TEYLSGSGKE IYCTTLSPSF GGMTFNEVCS QLYRVTGATL FAVEITDTLG YSRVILNPAR
YRIPPNTSPV VFLIAEDVED ADSVRTFGLE EEEDNLSEEL GSAQLTTTGK YPQDDSTIVY
TSQLMSRLER VYHVTSDPVS IESRTMSTLE TMTGHVLICG MHNDLHHFVA TLRPKHISRD
LLPPIVILNP ELPPPKLWNE LCHFPGVYYI QGSPLETQDL VRAGLLGLSK VIILSNSNGL
VNRNDLEAHS YLVDADALFV YQSITKVRPE VHIVCEIVNS KNLGFLDIDG AVPFAAGMVY
VNSVLDKLAV QAYYNVNLVR ILRELVVNNC DTPIYSVPNL HPSQLSFFPV PVDFEGKPYI
QLFQYLVLKC MTLPLGIYRK SEKSNPVPYV ITSPSADMLV HREDYVYSLQ SPEMDGKTEG
FLEVWVMRGK HLSPSSDGIP LAYSCEISIA PITLSTNEVE GRGTSVHWNQ RMNFSLNRES
RRMSLRIVQY RTRPQLVSSS TVHRQEVEYA TGEVDITEHV KSQHRSSIWS EEEEEQEAED
KGKTGGEIWL PLELKGGSRS KNPPAVCVKF SYYASKIRNR SETPERPGNL PGGKEEEGTK
AEDGNGAKTE QREEVEKAER EERKEERRGK KGERKEGRRE EGASMENGSF EGEQRDGTFA
D
//
