GenomeNet

Database: UniProt
Entry: B3M0A6_DROAN
LinkDB: B3M0A6_DROAN
Original site: B3M0A6_DROAN 
ID   B3M0A6_DROAN            Unreviewed;       883 AA.
AC   B3M0A6;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 2.
DT   24-JAN-2024, entry version 95.
DE   RecName: Full=Glutamate receptor ionotropic, kainate 2 {ECO:0008006|Google:ProtNLM};
GN   Name=Dana\GF18326 {ECO:0000313|EMBL:EDV43112.2};
GN   Synonyms=dana_GLEANR_19584 {ECO:0000313|EMBL:EDV43112.2};
GN   ORFNames=GF18326 {ECO:0000313|EMBL:EDV43112.2};
OS   Drosophila ananassae (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7217 {ECO:0000313|EMBL:EDV43112.2, ECO:0000313|Proteomes:UP000007801};
RN   [1] {ECO:0000313|EMBL:EDV43112.2, ECO:0000313|Proteomes:UP000007801}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 14024-0371.13 {ECO:0000313|Proteomes:UP000007801};
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., Markow T.A.,
RA   Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B.,
RA   Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M.,
RA   Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R.,
RA   Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P.,
RA   Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K.,
RA   Brand A.D., 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., Daub J.,
RA   David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K.,
RA   Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L.,
RA   Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G.,
RA   Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B.,
RA   Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A.,
RA   Haerty W., 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., Hubisz M.J.,
RA   Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R.,
RA   Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E.,
RA   Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K.,
RA   Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H.,
RA   Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F.,
RA   Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M.,
RA   Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L.,
RA   McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M.,
RA   Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E.,
RA   Negre B., 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., Pesole G.,
RA   Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R.,
RA   Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D.,
RA   Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A.,
RA   Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J.,
RA   Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A.,
RA   Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T.,
RA   Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B.,
RA   Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W.,
RA   Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W.,
RA   Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L.,
RA   Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J.,
RA   Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D.,
RA   Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G.,
RA   Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E.,
RA   Zhang P., 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., An P.,
RA   Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA   Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L.,
RA   Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA   Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA   D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA   Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA   Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA   Friedrich D., 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., LeVine R.,
RA   Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA   Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA   McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA   Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA   Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA   Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA   Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA   Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA   Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA   Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA   Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA   Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA   Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA   Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA   Chin C., 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 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 glutamate-gated ion channel (TC 1.A.10.1)
CC       family. {ECO:0000256|ARBA:ARBA00008685}.
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DR   EMBL; CH902617; EDV43112.2; -; Genomic_DNA.
DR   RefSeq; XP_001954551.2; XM_001954515.2.
DR   AlphaFoldDB; B3M0A6; -.
DR   SMR; B3M0A6; -.
DR   STRING; 7217.B3M0A6; -.
DR   EnsemblMetazoa; FBtr0123026; FBpp0121518; FBgn0095344.
DR   GeneID; 6501102; -.
DR   KEGG; dan:6501102; -.
DR   eggNOG; KOG1052; Eukaryota.
DR   HOGENOM; CLU_007257_1_1_1; -.
DR   InParanoid; B3M0A6; -.
DR   OrthoDB; 1011589at2759; -.
DR   Proteomes; UP000007801; Unassembled WGS sequence.
DR   GO; GO:0008328; C:ionotropic glutamate receptor complex; IEA:EnsemblMetazoa.
DR   GO; GO:0097482; C:muscle cell postsynaptic specialization; IEA:EnsemblMetazoa.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
DR   GO; GO:0022849; F:glutamate-gated calcium ion channel activity; IEA:EnsemblMetazoa.
DR   GO; GO:0007274; P:neuromuscular synaptic transmission; IEA:EnsemblMetazoa.
DR   CDD; cd06382; PBP1_iGluR_Kainate; 1.
DR   CDD; cd13714; PBP2_iGluR_Kainate; 1.
DR   Gene3D; 1.10.287.70; -; 1.
DR   Gene3D; 3.40.50.2300; -; 2.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR   InterPro; IPR001828; ANF_lig-bd_rcpt.
DR   InterPro; IPR019594; Glu/Gly-bd.
DR   InterPro; IPR001508; Iono_Glu_rcpt_met.
DR   InterPro; IPR015683; Ionotropic_Glu_rcpt.
DR   InterPro; IPR001320; Iontro_rcpt_C.
DR   InterPro; IPR028082; Peripla_BP_I.
DR   InterPro; IPR001638; Solute-binding_3/MltF_N.
DR   PANTHER; PTHR18966:SF349; FI04462P-RELATED; 1.
DR   PANTHER; PTHR18966; IONOTROPIC GLUTAMATE RECEPTOR; 1.
DR   Pfam; PF01094; ANF_receptor; 1.
DR   Pfam; PF00060; Lig_chan; 1.
DR   Pfam; PF10613; Lig_chan-Glu_bd; 1.
DR   Pfam; PF00497; SBP_bac_3; 1.
DR   PRINTS; PR00177; NMDARECEPTOR.
DR   SMART; SM00918; Lig_chan-Glu_bd; 1.
DR   SMART; SM00079; PBPe; 1.
DR   SUPFAM; SSF53822; Periplasmic binding protein-like I; 1.
DR   SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Ion channel {ECO:0000256|ARBA:ARBA00023303};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW   Ligand-gated ion channel {ECO:0000256|ARBA:ARBA00023286};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00023257};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007801};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Synapse {ECO:0000256|ARBA:ARBA00023018};
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        538..556
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        614..636
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        803..827
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          407..777
FT                   /note="Ionotropic glutamate receptor C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00079"
FT   DOMAIN          418..482
FT                   /note="Ionotropic glutamate receptor L-glutamate and
FT                   glycine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00918"
SQ   SEQUENCE   883 AA;  100254 MW;  C4093905CFF39E2D CRC64;
     MNFYLINAQY GGYGSYNNFE NMASVPIGLL TDQNTEQMNI IFDHAIDVAN QEVGTTLTSL
     KAEVNYGDAY QSYGRLCQML ETGIAGVFGP SSRHSALHLM SICDAMDIPH IYSYMSDYAE
     GFNLHPHPAD LAKALHSLIT EFNWSRFIFL YESADYLKIL NELTTLFGMN GPVVTVLRYD
     MQLNGNYKQV LRRVRKSQDN RIVVVGSSDT MPEFLNQAQQ VGIINEDYKY IIGNLDFHSF
     DLEEYKYSEA NITGLRLFSP EKMAVKELLM KLGYPTDQDE FRNGSCPITV EMALTYDAVQ
     LFAETLKNLP FKPISQNCSQ RTESVRDDGS SFKNYMRTLR LSEHLLTGPI YFEGNVRKGY
     HLDVIELQPS GIVKVGSWDE NRGYRPQRLA PTTSQFDGLD NSLANKTFIV LLSVPNKPYA
     QLVESYKQLE GNNQYEGYGV DLIKELADKL GFNFTFVNGG NDYGTFNKTS NESTGMLREI
     MMGRADLAVT DLTITAEREQ AIDFSIPFMN LGIAILYLKP QKATPELFTF MDPFSEEVWM
     FLGFSFLGVS LSFFILGRLS PSEWDNPYPC IEEPEELENQ FTLGNSIWFT TGALLQQGSE
     IGPKALSTRT VATFWWFFTL IVVSSYTANL AAFLTIEKPQ SLINSVEDLA NNKDGVVYGA
     KRTGSTRTFF LTTEDERYKR MNQFMLEHPE HLTQDNMEGV NRVKSSTHYA FLMESTSIEY
     NTKRECNLKK IGDALDEKCY GIAMRKNWPH RNKFNNALLE LQEQGVLEKM KNKWWNEVGT
     GICATKEEAP DATPLDMNNL EGVFFVLTVG SCLALLYGIV SWAFFVIKKA HHYRVPVKEA
     LKEEFQFIID INNYVRVLKN SASIYSRSRQ SSMSVASMAQ DDS
//
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