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Database: UniProt
Entry: B4HXE7_DROSE
LinkDB: B4HXE7_DROSE
Original site: B4HXE7_DROSE 
ID   B4HXE7_DROSE            Unreviewed;       524 AA.
AC   B4HXE7;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   18-SEP-2019, entry version 74.
DE   SubName: Full=GM15477 {ECO:0000313|EMBL:EDW51727.1};
DE   Flags: Fragment;
GN   Name=Dsec\GM15477 {ECO:0000313|EMBL:EDW51727.1};
GN   ORFNames=Dsec_GM15477 {ECO:0000313|EMBL:EDW51727.1};
OS   Drosophila sechellia (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7238 {ECO:0000313|Proteomes:UP000001292};
RN   [1] {ECO:0000313|EMBL:EDW51727.1, ECO:0000313|Proteomes:UP000001292}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rob3c / Tucson 14021-0248.25
RC   {ECO:0000313|Proteomes:UP000001292};
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 Genomes Consortium;
RA   Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B.,
RA   Markow T.A., Kaufman T.C., Kellis M., Gelbart W., Iyer V.N.,
RA   Pollard D.A., Sackton T.B., Larracuente A.M., Singh N.D., Abad J.P.,
RA   Abt D.N., Adryan B., Aguade M., Akashi H., Anderson W.W.,
RA   Aquadro C.F., Ardell D.H., Arguello R., Artieri C.G., Barbash D.A.,
RA   Barker D., Barsanti P., Batterham P., Batzoglou S., Begun D.,
RA   Bhutkar A., Blanco E., Bosak S.A., Bradley R.K., Brand A.D.,
RA   Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C.,
RA   Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S.,
RA   Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A.,
RA   Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A.,
RA   Daub J., David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H.,
RA   Edwards K., Eickbush T., Evans J.D., Filipski A., Findeiss S.,
RA   Freyhult E., Fulton L., Fulton R., Garcia A.C., Gardiner A.,
RA   Garfield D.A., Garvin B.E., Gibson G., Gilbert D., Gnerre S.,
RA   Godfrey J., Good R., Gotea V., Gravely B., Greenberg A.J.,
RA   Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A., Haerty W.,
RA   Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V.,
RA   Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A.,
RA   Hubisz M.J., Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S.,
RA   Jeck W.R., Johnson J., Jones C.D., Jordan W.C., Karpen G.H.,
RA   Kataoka E., Keightley P.D., Kheradpour P., Kirkness E.F.,
RA   Koerich L.B., Kristiansen K., Kudrna D., Kulathinal R.J., Kumar S.,
RA   Kwok R., Lander E., Langley C.H., Lapoint R., Lazzaro B.P., Lee S.J.,
RA   Levesque L., Li R., Lin C.F., Lin M.F., Lindblad-Toh K., Llopart A.,
RA   Long M., Low L., Lozovsky E., Lu J., Luo M., Machado C.A.,
RA   Makalowski W., Marzo M., Matsuda M., Matzkin L., McAllister B.,
RA   McBride C.S., McKernan B., McKernan K., Mendez-Lago M., Minx P.,
RA   Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E., Negre B.,
RA   Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L.,
RA   Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S.,
RA   Pesole G., Phillippy A.M., Ponting C.P., Pop M., Porcelli D.,
RA   Powell J.R., Prohaska S., Pruitt K., Puig M., Quesneville H.,
RA   Ram K.R., Rand D., Rasmussen M.D., Reed L.K., Reenan R., Reily A.,
RA   Remington K.A., Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H.,
RA   Rohde C., Rozas J., Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L.,
RA   Sanchez-Gracia A., Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C.,
RA   Schlenke T., Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M.,
RA   Sisneros N.B., Smith C.D., Smith T.F., Spieth J., Stage D.E.,
RA   Stark A., Stephan W., Strausberg R.L., Strempel S., Sturgill D.,
RA   Sutton G., Sutton G.G., Tao W., Teichmann S., Tobari Y.N.,
RA   Tomimura Y., Tsolas J.M., Valente V.L., Venter E., Venter J.C.,
RA   Vicario S., Vieira F.G., Vilella A.J., Villasante A., Walenz B.,
RA   Wang J., Wasserman M., Watts T., Wilson D., Wilson R.K., Wing R.A.,
RA   Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G., Yamamoto D.,
RA   Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E., Zhang P.,
RA   Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA   Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A.,
RA   An P., Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P.,
RA   Barry A., Bayul T., Berlin A., Bessette D., Bloom T., Blye J.,
RA   Boguslavskiy L., Bonnet C., Boukhgalter B., Bourzgui I., Brown A.,
RA   Cahill P., Channer S., Cheshatsang Y., Chuda L., Citroen M.,
RA   Collymore A., Cooke P., Costello M., D'Aco K., Daza R., De Haan G.,
RA   DeGray S., DeMaso C., Dhargay N., Dooley K., Dooley E., Doricent M.,
RA   Dorje P., Dorjee K., Dupes A., Elong R., Falk J., Farina A., Faro S.,
RA   Ferguson D., Fisher S., Foley C.D., Franke A., Friedrich D.,
RA   Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA   Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA   Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA   Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA   Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F.,
RA   LeVine R., Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T.,
RA   Lokyitsang Y., Lubonja R., Lui A., MacDonald P., Magnisalis V.,
RA   Maru K., Matthews C., McCusker W., McDonough S., Mehta T., Meldrim J.,
RA   Meneus L., Mihai O., Mihalev A., Mihova T., Mittelman R., Mlenga V.,
RA   Montmayeur A., Mulrain L., Navidi A., Naylor J., Negash T., Nguyen T.,
RA   Nguyen N., Nicol R., Norbu C., Norbu N., Novod N., O'Neill B.,
RA   Osman S., Markiewicz E., Oyono O.L., Patti C., Phunkhang P.,
RA   Pierre F., Priest M., Raghuraman S., Rege F., Reyes R., Rise C.,
RA   Rogov P., Ross K., Ryan E., Settipalli S., Shea T., Sherpa N., Shi L.,
RA   Shih D., Sparrow T., Spaulding J., Stalker J., Stange-Thomann N.,
RA   Stavropoulos S., Stone C., Strader C., Tesfaye S., Thomson T.,
RA   Thoulutsang Y., Thoulutsang D., Topham K., Topping I., Tsamla T.,
RA   Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J.,
RA   Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D., Zimmer A.,
RA   Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J., Chin C.,
RA   Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
CC   -!- SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell
CC       membrane {ECO:0000256|SAAS:SAAS00569352}; Multi-pass membrane
CC       protein {ECO:0000256|SAAS:SAAS00569352}. Cell membrane
CC       {ECO:0000256|SAAS:SAAS00569391}; Multi-pass membrane protein
CC       {ECO:0000256|SAAS:SAAS00569391}.
CC   -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9)
CC       family. {ECO:0000256|RuleBase:RU000687,
CC       ECO:0000256|SAAS:SAAS00978283}.
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DR   EMBL; CH480818; EDW51727.1; -; Genomic_DNA.
DR   RefSeq; XP_002035804.1; XM_002035768.1.
DR   GeneID; 6611249; -.
DR   KEGG; dse:Dsec_GM15477; -.
DR   KO; K05312; -.
DR   OMA; EYFATTM; -.
DR   PhylomeDB; B4HXE7; -.
DR   Proteomes; UP000001292; Unassembled WGS sequence.
DR   GO; GO:0005892; C:acetylcholine-gated channel complex; IEA:EnsemblMetazoa.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042166; F:acetylcholine binding; IEA:EnsemblMetazoa.
DR   GO; GO:0022848; F:acetylcholine-gated cation-selective channel activity; IEA:EnsemblMetazoa.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR   Gene3D; 2.70.170.10; -; 1.
DR   InterPro; IPR006202; Neur_chan_lig-bd.
DR   InterPro; IPR036734; Neur_chan_lig-bd_sf.
DR   InterPro; IPR006201; Neur_channel.
DR   InterPro; IPR036719; Neuro-gated_channel_TM_sf.
DR   InterPro; IPR006029; Neurotrans-gated_channel_TM.
DR   InterPro; IPR018000; Neurotransmitter_ion_chnl_CS.
DR   InterPro; IPR002394; Nicotinic_acetylcholine_rcpt.
DR   PANTHER; PTHR18945; PTHR18945; 1.
DR   Pfam; PF02931; Neur_chan_LBD; 1.
DR   Pfam; PF02932; Neur_chan_memb; 1.
DR   PRINTS; PR00254; NICOTINICR.
DR   PRINTS; PR00252; NRIONCHANNEL.
DR   SUPFAM; SSF63712; SSF63712; 1.
DR   SUPFAM; SSF90112; SSF90112; 1.
DR   TIGRFAMs; TIGR00860; LIC; 1.
DR   PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
PE   3: Inferred from homology;
KW   Cell junction {ECO:0000256|SAAS:SAAS00458005};
KW   Cell membrane {ECO:0000256|SAAS:SAAS00458000};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001292};
KW   Disulfide bond {ECO:0000256|SAAS:SAAS00081591};
KW   Ion channel {ECO:0000256|RuleBase:RU000687,
KW   ECO:0000256|SAAS:SAAS00458066};
KW   Ion transport {ECO:0000256|RuleBase:RU000687,
KW   ECO:0000256|SAAS:SAAS00457919};
KW   Ligand-gated ion channel {ECO:0000256|SAAS:SAAS00172123};
KW   Membrane {ECO:0000256|SAAS:SAAS00978300, ECO:0000256|SAM:Phobius};
KW   Postsynaptic cell membrane {ECO:0000256|SAAS:SAAS00081626};
KW   Receptor {ECO:0000256|SAAS:SAAS00469528};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001292};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Synapse {ECO:0000256|SAAS:SAAS00103537};
KW   Transmembrane {ECO:0000256|SAAS:SAAS00978734,
KW   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAAS:SAAS00978768,
KW   ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|RuleBase:RU000687,
KW   ECO:0000256|SAAS:SAAS00081549}.
FT   SIGNAL        1     25       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        26    524       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5002809530.
FT   TRANSMEM    237    256       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    268    286       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    298    321       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    333    349       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    498    522       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       29    236       Neur_chan_LBD. {ECO:0000259|Pfam:
FT                                PF02931}.
FT   DOMAIN      243    514       Neur_chan_memb. {ECO:0000259|Pfam:
FT                                PF02932}.
FT   NON_TER       1      1       {ECO:0000313|EMBL:EDW51727.1}.
SQ   SEQUENCE   524 AA;  59719 MW;  2A5346490877C663 CRC64;
     INGLNKHSWI FLLIYLNLSA KVCLAGYHEK RLLHDLLDPY NTLERPVLNE SDPLQLSFGL
     TLMQIIDVDE KNQLLVTNVW LKLEWNDMNL RWNTSDYGGV KDLRIPPHRI WKPDVLMYNS
     ADEGFDGTYQ TNVVVRNNGS CLYVPPGIFK STCKIDITWF PFDDQRCEMK FGSWTYDGFQ
     LDLQLQDETG GDISSYVLNG EWELLGVPGK RNEIYYNCCP EPYIDITFAI IIRRRTLYYF
     FNLIIPCVLI ASMALLGFTL PPDSGEKLSL GVTILLSLTV FLNMVAETMP ATSDAVPLLG
     TYFNCIMFMV ASSVVSTILI LNYHHRNADT HEMSEWIRIV FLCWLPWILR MSRPGRPLIL
     EFPTTPCSDT SSERKHQILS DVELKERSSK SLLANVLDID DDFRHNCRPM TPGGTLPHNP
     AFYRTVYGQG DDGSIGPIGS TRMPDAVTHH TCIKSSTEYE LGLILKEIRF ITDQLRKDDE
     CNDIANDWKF AAMVVDRLCL IIFTMFTILA TIAVLLSAPH IIVS
//
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