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Database: UniProt
Entry: D7FRQ7_ECTSI
LinkDB: D7FRQ7_ECTSI
Original site: D7FRQ7_ECTSI 
ID   D7FRQ7_ECTSI            Unreviewed;      1161 AA.
AC   D7FRQ7;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CBJ30848.1};
GN   ORFNames=Esi_0217_0029 {ECO:0000313|EMBL:CBJ30848.1};
OS   Ectocarpus siliculosus (Brown alga) (Conferva siliculosa).
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; PX clade; Phaeophyceae;
OC   Ectocarpales; Ectocarpaceae; Ectocarpus.
OX   NCBI_TaxID=2880 {ECO:0000313|EMBL:CBJ30848.1, ECO:0000313|Proteomes:UP000002630};
RN   [1] {ECO:0000313|EMBL:CBJ30848.1, ECO:0000313|Proteomes:UP000002630}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ec32 / CCAP1310/4 {ECO:0000313|Proteomes:UP000002630};
RX   PubMed=20520714; DOI=10.1038/nature09016;
RA   Cock J.M., Sterck L., Rouze P., Scornet D., Allen A.E., Amoutzias G.,
RA   Anthouard V., Artiguenave F., Aury J.M., Badger J.H., Beszteri B.,
RA   Billiau K., Bonnet E., Bothwell J.H., Bowler C., Boyen C., Brownlee C.,
RA   Carrano C.J., Charrier B., Cho G.Y., Coelho S.M., Collen J., Corre E.,
RA   Da Silva C., Delage L., Delaroque N., Dittami S.M., Doulbeau S., Elias M.,
RA   Farnham G., Gachon C.M., Gschloessl B., Heesch S., Jabbari K., Jubin C.,
RA   Kawai H., Kimura K., Kloareg B., Kupper F.C., Lang D., Le Bail A.,
RA   Leblanc C., Lerouge P., Lohr M., Lopez P.J., Martens C., Maumus F.,
RA   Michel G., Miranda-Saavedra D., Morales J., Moreau H., Motomura T.,
RA   Nagasato C., Napoli C.A., Nelson D.R., Nyvall-Collen P., Peters A.F.,
RA   Pommier C., Potin P., Poulain J., Quesneville H., Read B., Rensing S.A.,
RA   Ritter A., Rousvoal S., Samanta M., Samson G., Schroeder D.C., Segurens B.,
RA   Strittmatter M., Tonon T., Tregear J.W., Valentin K., von Dassow P.,
RA   Yamagishi T., Van de Peer Y., Wincker P.;
RT   "The Ectocarpus genome and the independent evolution of multicellularity in
RT   brown algae.";
RL   Nature 465:617-621(2010).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; FN648395; CBJ30848.1; -; Genomic_DNA.
DR   AlphaFoldDB; D7FRQ7; -.
DR   STRING; 2880.D7FRQ7; -.
DR   EnsemblProtists; CBJ30848; CBJ30848; Esi_0217_0029.
DR   eggNOG; KOG1420; Eukaryota.
DR   InParanoid; D7FRQ7; -.
DR   OrthoDB; 51137at2759; -.
DR   Proteomes; UP000002630; Unplaced LGUn.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; 1.
DR   Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 1.
DR   InterPro; IPR003929; K_chnl_BK_asu.
DR   InterPro; IPR013099; K_chnl_dom.
DR   InterPro; IPR047871; K_chnl_Slo-like.
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; PF07885; Ion_trans_2; 1.
DR   PRINTS; PR00169; KCHANNEL.
DR   SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
PE   4: Predicted;
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
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:UP000002630};
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        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        53..74
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        94..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        119..139
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        159..178
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        199..220
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        232..250
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        262..283
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          219..285
FT                   /note="Potassium channel"
FT                   /evidence="ECO:0000259|Pfam:PF07885"
FT   DOMAIN          442..545
FT                   /note="Calcium-activated potassium channel BK alpha
FT                   subunit"
FT                   /evidence="ECO:0000259|Pfam:PF03493"
FT   REGION          641..664
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          788..816
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          852..920
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1007..1026
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1137..1161
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        644..664
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        856..904
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1161 AA;  125889 MW;  ACBC1FA761DA0F82 CRC64;
     MGGAASETPV TLSAAGSFLV FFCYFSYVLF SVPRHGEVPY TNRLNRHITT SRCGLFIEIL
     NALFSLATCV LFVLETYSFG NNYGFIVMSF SMEMVFNGFF LFNFLLHLYL AVDKLTHLVS
     LQAVVDIVTV FPSYLILFMN DGWRTSDGGF ADAYLGLKIT RVIRVARLLV TISFFVQGPS
     LAFDHSRQLL VLRSQLVRWS LKTVLVIFTM AGLTNFLVVV QDADWGLGYG RMPFHEALYF
     VVVSFSTVGY GDISPSTALS RVVITGLILT LFFCVPLVTN ALVNLTKLTP KHGGCLSKSW
     GTGHIVVGCD ASCLRVVSVL LRDLLAADSM AYHHEHVVLV IPQEPTLAWD ALLCLQPSFA
     VTYLNGDLSS AKDLRRARVA NARACFVLSD RLANDTEAQD KTALLRALST NQASPPGSSV
     LCLVTHSRSK GRLVRLGMPE ASVVCYDEVM EGLVTQACLN PGFSTVWTNM LSCMPEADYL
     LKTRGAEQDV TRDPESTALF ETETEYLRSL RRVTLRFRLT CFAGECTGDA AIELHEKCGC
     ILFALICNIC SGGHKSRVKC GAGKRRRRCV RVHPDYGTII SKDDVGVFIS ANHESADLLA
     RYCTGRATSG AAATAAPSKA SGTSLRREGW VENAFLVAEN PPVGNRQHGT QENRQRNASS
     GDGRFERTIW SDVHDAGGGA STPSVFPLGE SLVGTPPGAV LVIAQSLSFA LGVVLSLCEA
     DDDLDVEGSP ALSVVCSPTW WDPVADERAE RELAARFPCV RLVKRETEYE CLLEVGADKA
     DLVCVVSSRP EDEPTTPKTG GGGGDGDVLG DHSGRGQGSD VWAMGVVVDV LGLVPESTRV
     VVRFDDSASA EQHQVISAHV RRREDAQETG RRERAAAESG EKQGEENLFD GRKEQTDRAT
     QQQRDAPRNE NAGTTVEDSV DFGYSARSGV GGGGVYFDDT RGVVREGFDD FFGTMSGYVS
     GDVVVGNAAE LLLLQTMLAP DIQSLMSDVM HLVSRVPIEV LWPEHSPNAR GTAVGDNNDN
     RGDGDIRRSR IRPVTYGEAF RLLLEDRDLL ALGLHRPPTH GRGPRKMGGR ERWRCPGGSR
     YVAINSPSAS FALRDGDCFF VLRRRSRPVS AFNSEPAVDP LVTGTCVSSG GRATAALAAT
     AADPTEGTTT PGKDTPERLH G
//
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