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Database: UniProt
Entry: A0A4Y0BGD5_ANOFN
LinkDB: A0A4Y0BGD5_ANOFN
Original site: A0A4Y0BGD5_ANOFN 
ID   A0A4Y0BGD5_ANOFN        Unreviewed;       546 AA.
AC   A0A4Y0BGD5;
DT   18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2019, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=Potassium channel domain-containing protein {ECO:0000259|Pfam:PF07885};
OS   Anopheles funestus (African malaria mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=62324 {ECO:0000313|EnsemblMetazoa:AFUN020044-PA, ECO:0000313|Proteomes:UP000075900};
RN   [1] {ECO:0000313|Proteomes:UP000075900}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FUMOZ {ECO:0000313|Proteomes:UP000075900};
RX   PubMed=21129198; DOI=10.1186/1756-3305-3-117;
RA   Sinka M.E., Bangs M.J., Manguin S., Coetzee M., Mbogo C.M., Hemingway J.,
RA   Patil A.P., Temperley W.H., Gething P.W., Kabaria C.W., Okara R.M.,
RA   Van Boeckel T., Godfray H.C., Harbach R.E., Hay S.I.;
RT   "The dominant Anopheles vectors of human malaria in Africa, Europe and the
RT   Middle East: occurrence data, distribution maps and bionomic precis.";
RL   Parasit. Vectors 3:117-117(2010).
RN   [2] {ECO:0000313|Proteomes:UP000075900}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FUMOZ {ECO:0000313|Proteomes:UP000075900};
RX   PubMed=31157884; DOI=10.1093/gigascience/giz063;
RA   Ghurye J., Koren S., Small S.T., Redmond S., Howell P., Phillippy A.M.,
RA   Besansky N.J.;
RT   "A chromosome-scale assembly of the major African malaria vector Anopheles
RT   funestus.";
RL   Gigascience 8:0-0(2019).
RN   [3] {ECO:0000313|EnsemblMetazoa:AFUN020044-PA}
RP   IDENTIFICATION.
RC   STRAIN=FUMOZ {ECO:0000313|EnsemblMetazoa:AFUN020044-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the two pore domain potassium channel (TC
CC       1.A.1.8) family. {ECO:0000256|ARBA:ARBA00006666,
CC       ECO:0000256|RuleBase:RU003857}.
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DR   AlphaFoldDB; A0A4Y0BGD5; -.
DR   STRING; 62324.A0A4Y0BGD5; -.
DR   EnsemblMetazoa; AFUN020044-RA; AFUN020044-PA; AFUN020044.
DR   VEuPathDB; VectorBase:AFUN020044; -.
DR   VEuPathDB; VectorBase:AFUN2_006931; -.
DR   Proteomes; UP000075900; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005267; F:potassium channel activity; IEA:InterPro.
DR   Gene3D; 1.10.287.70; -; 2.
DR   InterPro; IPR003280; 2pore_dom_K_chnl.
DR   InterPro; IPR013099; K_chnl_dom.
DR   PANTHER; PTHR11003:SF327; BCDNA.GH04802-RELATED; 1.
DR   PANTHER; PTHR11003; POTASSIUM CHANNEL, SUBFAMILY K; 1.
DR   Pfam; PF07885; Ion_trans_2; 2.
DR   PRINTS; PR01333; 2POREKCHANEL.
DR   SUPFAM; SSF81324; Voltage-gated potassium channels; 2.
PE   3: Inferred from homology;
KW   Ion channel {ECO:0000256|RuleBase:RU003857};
KW   Ion transport {ECO:0000256|RuleBase:RU003857};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU003857};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU003857}.
FT   TRANSMEM        46..69
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        81..99
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        439..459
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        471..492
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        498..521
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          47..102
FT                   /note="Potassium channel"
FT                   /evidence="ECO:0000259|Pfam:PF07885"
FT   DOMAIN          447..524
FT                   /note="Potassium channel"
FT                   /evidence="ECO:0000259|Pfam:PF07885"
FT   REGION          125..174
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          192..291
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          321..354
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          372..394
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        136..167
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        207..224
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        259..285
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   546 AA;  62235 MW;  715E458301112ACA CRC64;
     MTNDRPVLHQ QNWTSAAIMH LQSFEKEILT AMKKDGWDGN EDVDQIQWTF FGALFYSIIV
     ITTIGYGHIA PKTYMGKIST IFYAILGIPL MLLCLSNIGD IMASSFRFLY WRVCCYVCTR
     EPKRSNSRRS RSSRGTVRQG RSSVRSGQAA GTNLRRSVRN SQRSADSGFD PYYEPGLSHS
     YSDTDCRYNA AMDDPYYPDN DRGMRQQAKY DNSNPNNSGG MRPQIRGPPN SDAFMNEEYM
     AGSPQVKRPP PGGHSRAESI GLDQSQRSLQ KPRQNDGQYR KQQGMRAQSL DRRMFRQDSQ
     MIDMDDDSPC KTPILCNKYA LDDVDDQDGR PTRPNPRSQS MPRQTGRYGD RLMPDRMPYY
     TEDNEMAENM HTVRKSAPQR RREPRPVPAP SPRIMSPMGF AVHRQARHLQ NVIDDNSLYD
     DEWDIHSGEL PPSSIVRPVP IWLCVFLVVS YIIAGAFMFS EWEEWSFLDS AYFCFITLTT
     IGFGDFVPAQ GVKNDSEISI ALCSLYLLFG IALLAMSFNL VQEEVISNVK SVARRLGILK
     EEEMDD
//
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