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Database: UniProt
Entry: A0A4Y0BMR9_ANOFN
LinkDB: A0A4Y0BMR9_ANOFN
Original site: A0A4Y0BMR9_ANOFN 
ID   A0A4Y0BMR9_ANOFN        Unreviewed;       575 AA.
AC   A0A4Y0BMR9;
DT   18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2019, sequence version 1.
DT   27-MAR-2024, entry version 18.
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:AFUN021934-PB, 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:AFUN021934-PB}
RP   IDENTIFICATION.
RC   STRAIN=FUMOZ {ECO:0000313|EnsemblMetazoa:AFUN021934-PB};
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; A0A4Y0BMR9; -.
DR   STRING; 62324.A0A4Y0BMR9; -.
DR   EnsemblMetazoa; AFUN021934-RB; AFUN021934-PB; AFUN021934.
DR   VEuPathDB; VectorBase:AFUN021934; -.
DR   VEuPathDB; VectorBase:AFUN2_011272; -.
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; -; 1.
DR   InterPro; IPR003280; 2pore_dom_K_chnl.
DR   InterPro; IPR013099; K_chnl_dom.
DR   PANTHER; PTHR11003; POTASSIUM CHANNEL, SUBFAMILY K; 1.
DR   PANTHER; PTHR11003:SF345; TWIK FAMILY OF POTASSIUM CHANNELS; 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        146..170
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        244..265
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        277..298
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        421..442
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        449..468
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        474..497
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          223..299
FT                   /note="Potassium channel"
FT                   /evidence="ECO:0000259|Pfam:PF07885"
FT   DOMAIN          429..498
FT                   /note="Potassium channel"
FT                   /evidence="ECO:0000259|Pfam:PF07885"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          347..412
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          551..575
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        347..364
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        365..385
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   575 AA;  64373 MW;  A02FF62D38D14CEC CRC64;
     MTQGTDPKAS TNAAGSRPRI NLTMPPVYVA PPPHTPAKYS PAHYFQQLHQ QQQQHQMLQN
     PLYQPGIPVT PGSPTRISLG ADGTVTEQPD YTDYYSMYPA KAGEFMFKQF EGFRDFTVNT
     AKSGLGVGEK SVFWMYTKIT RWSRSWFTHF FLFLILFLYS VAGAALFIAV EGTHEKKMET
     NVNHAKRMLA KNLRILALDR EKLENPDPDI WEGRAINLVE EYSAVLYQSY KEGSFENKQN
     KKTWSFWNAV FYCGTIYTTI GYGHISPSTT TGRALTILYA IIGIPIFLIV LADFGKLFTR
     GIKFMWAYVR RLYYTGSFRK VRKTAQVQEV MKGLNVVYDM VRRPSTDNEL QGATTTTAVP
     TQQPQQPPLS APAQPPQPQA SQRPPSEPQP AGGTGIETIP MPDTPTTPVP ETFEIDDEFN
     LPISVAIVIL VAYMLFGANI YCRWENWSFF EAFYFVFISI STIGFGDYVP QHPIYMMCSI
     LYLIFGLALT SMCINVVQLK LSDSFRQASA KIGATIGLQM AEAASQHQHS PVHTPIELAA
     VHTSTPTSAV NVSLKDTPTL PARPSTSVPK PEKKE
//
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