ID F5HIW0_ANOGA Unreviewed; 1246 AA.
AC F5HIW0;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE SubName: Full=AGAP002150-PB {ECO:0000313|EMBL:EGK96221.1};
GN ORFNames=AgaP_AGAP002150 {ECO:0000313|EMBL:EGK96221.1};
OS Anopheles gambiae (African malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7165 {ECO:0000313|EMBL:EGK96221.1};
RN [1] {ECO:0000313|EMBL:EGK96221.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PEST {ECO:0000313|EMBL:EGK96221.1};
RX PubMed=12364791; DOI=10.1126/science.1076181;
RA Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R.,
RA Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R.,
RA Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z.,
RA Kraft C.L., Abril J.F., Anthouard V., Arensburger P., Atkinson P.W.,
RA Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C.,
RA Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K.,
RA Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V.,
RA Dana A., Delcher A., Dew I., Evans C.A., Flanigan M.,
RA Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R.,
RA Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J.,
RA Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I.,
RA Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A.,
RA McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D.,
RA O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H.,
RA Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J.,
RA Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B.,
RA Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M.,
RA Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I.,
RA Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J.,
RA Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M.,
RA Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C.,
RA Collins F.H., Hoffman S.L.;
RT "The genome sequence of the malaria mosquito Anopheles gambiae.";
RL Science 298:129-149(2002).
RN [2] {ECO:0000313|EMBL:EGK96221.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PEST {ECO:0000313|EMBL:EGK96221.1};
RG The Anopheles Genome Sequencing Consortium;
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:EGK96221.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PEST {ECO:0000313|EMBL:EGK96221.1};
RX PubMed=14747013; DOI=10.1016/j.pt.2003.11.003;
RA Mongin E., Louis C., Holt R.A., Birney E., Collins F.H.;
RT "The Anopheles gambiae genome: an update.";
RL Trends Parasitol. 20:49-52(2004).
RN [4] {ECO:0000313|EMBL:EGK96221.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PEST {ECO:0000313|EMBL:EGK96221.1};
RX PubMed=17210077; DOI=10.1186/gb-2007-8-1-r5;
RA Sharakhova M.V., Hammond M.P., Lobo N.F., Krzywinski J., Unger M.F.,
RA Hillenmeyer M.E., Bruggner R.V., Birney E., Collins F.H.;
RT "Update of the Anopheles gambiae PEST genome assembly.";
RL Genome Biol. 8:R5.1-R5.13(2007).
RN [5] {ECO:0000313|EMBL:EGK96221.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PEST {ECO:0000313|EMBL:EGK96221.1};
RG VectorBase;
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the potassium channel HCN family.
CC {ECO:0000256|ARBA:ARBA00006305}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGK96221.1}.
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DR EMBL; AAAB01008799; EGK96221.1; -; Genomic_DNA.
DR RefSeq; XP_003436040.1; XM_003435992.1.
DR AlphaFoldDB; F5HIW0; -.
DR STRING; 7165.F5HIW0; -.
DR PaxDb; 7165-AGAP002150-PB; -.
DR GeneID; 1269408; -.
DR KEGG; aga:AgaP_AGAP002150; -.
DR VEuPathDB; VectorBase:AGAP002150; -.
DR eggNOG; KOG0498; Eukaryota.
DR HOGENOM; CLU_266195_0_0_1; -.
DR OrthoDB; 74296at2759; -.
DR PhylomeDB; F5HIW0; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005272; F:sodium channel activity; IEA:UniProtKB-KW.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR CDD; cd00038; CAP_ED; 1.
DR Gene3D; 1.10.287.70; -; 1.
DR Gene3D; 1.10.287.630; Helix hairpin bin; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR InterPro; IPR018488; cNMP-bd_CS.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR018490; cNMP-bd_dom_sf.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR013621; Ion_trans_N.
DR InterPro; IPR003938; K_chnl_volt-dep_EAG/ELK/ERG.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR PANTHER; PTHR45689; I[[H]] CHANNEL, ISOFORM E; 1.
DR PANTHER; PTHR45689:SF5; I[[H]] CHANNEL, ISOFORM E; 1.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF00520; Ion_trans; 2.
DR Pfam; PF08412; Ion_trans_N; 1.
DR PRINTS; PR01463; EAGCHANLFMLY.
DR SMART; SM00100; cNMP; 1.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
DR PROSITE; PS00888; CNMP_BINDING_1; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
PE 3: Inferred from homology;
KW cAMP {ECO:0000256|ARBA:ARBA00023149};
KW cAMP-binding {ECO:0000256|ARBA:ARBA00022566};
KW Ion channel {ECO:0000256|ARBA:ARBA00022461};
KW Ion transport {ECO:0000256|ARBA:ARBA00022461};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022566};
KW Sodium {ECO:0000256|ARBA:ARBA00023053};
KW Sodium channel {ECO:0000256|ARBA:ARBA00022461};
KW Sodium transport {ECO:0000256|ARBA:ARBA00023201};
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:ARBA00022461}.
FT TRANSMEM 674..698
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 868..889
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 943..967
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1045..1161
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT REGION 50..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 254..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 306..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1202..1221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1227..1246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..198
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..374
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1204..1221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1246 AA; 136368 MW; A3832623A3F30D3F CRC64;
MCWETELVGD RTRGMNAQEN AEFLQLSQTQ LHQSSVNIGF SNIVYNSATS EPLNSSRSGS
TSLAVIDKST TPKAESSDQK SGHKYNDLNK TSLSVEESNL NFNFVKSNGK SVSANNCSGS
YKGLAGSNGA GTSSQSQQQQ SAGSRPDGPG STFPCKKCAI SNNLSNPPTL HLGGTPSDGP
PAHYHPACHE HHDHSNQSLK SSPAHGGSGS SGRGVPAAAA AANIVASSAP TKSSGGSGKG
SALLSSCQGS FHSLQGGGSG SVDGNGSILP PYGHHSVSSS GAQTASGGSM QHACSNLLSH
HAAVQPRLSY STSSHTDSPN GSGTVLYNRS RINSNGATPG ELERGGSIPG ASSSSTNGGA
KHQQQQQQQQ QQHATNYNVF SVNYERKSAS IGGGVASGSG GGVFSGGASG SSNGNGSKTI
NNSSNKSNNS NGAINGASNS GNGYGYHASD ISQLRNIIEL NKQVNDLNSK NVEYNRQLSA
PAENNINKSS SNCYSNSVYN LFSNHILPQY HSNSPNTNSL NRAKKKRSYK LNGSRLFSAA
SSDSIRFHSN LSNQNDTDLR VSIDNTCTDS LVTALDDEAL LITDYMNDMA KSKVHFDDVS
LYGTPKEEPL PNIPPSIEKP SSNFLKNQLQ AWFQPTDNRL AMKLFGSKKA LVKERIRQKT
AGHWVIHPCS SFRFYWDLCM LLLLVANLII LPVAISFFND DLSTRWIAFN CLSDTIFLVD
IVVNFRTGIM QQDNAEQVIL DPKLIAKHYL KTWFFLDLIS SIPLDYIFLI FNQLPELLDF
SDSFQLLHAG RALRILRLAK LLSLVRLLRL SRLVRYVSQW EEVYILQNLQ KKHSNRRGRS
FQKEKAKGFS KSSLILKFLN MASVFMRIFN LICMMLLIGH WSGCLQFLVP MLQGFPSNSW
VAINELQESY WLEQYSWALF KAMSHMLCIG YGRFPPQSLT DMWLTMLSMI SGATCYALFL
GHATNLIQSL DSSRRQYREK VKQVEEYMAY RKLPRDMRQR ITEYFEHRYQ GKFFDEECIL
GELSEKLRED VINYNCRSLV ASVPFFANAD SNFVSDVVTK LRYEVFQPGD IIIKEGTIGS
KMYFIQEGIV DIVMANGEVA TSLSDGSYFG EICLLTNARR VASVRAETYC NLFSLSVDHF
NAVLDQYPLM RKTMETVAAE RLNKIGKNPN IMAQKEESES GNTETNQISA VVNALAAEAD
NVDNLSDGNG SMKKGTSQSS LNELNQSLKM SLPRPKSGEF RALFEG
//
