ID ADCY2_DROME Reviewed; 1307 AA. AC Q9VW60; O77247; Q8MRK9; DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 3. DT 23-OCT-2007, entry version 49. DE Adenylate cyclase type 2 (EC 4.6.1.1) (ATP pyrophosphate-lyase 2) DE (Adenylyl cyclase 76E). GN Name=Ac76E; ORFNames=CG7978; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Canton-S; RX MEDLINE=92154664; PubMed=1739965; DOI=10.1016/0092-8674(92)90185-F; RA Levin L.R., Han P.-L., Hwang P.M., Feinstein P.G., Davis R.L., RA Reed R.R.; RT "The Drosophila learning and memory gene rutabaga encodes a RT Ca2+/Calmodulin-responsive adenylyl cyclase."; RL Cell 68:479-489(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., RA Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP GENOME REANNOTATION. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 434-1307. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: This is a membrane-bound, calmodulin-insensitive CC adenylyl cyclase (By similarity). CC -!- CATALYTIC ACTIVITY: ATP = 3',5'-cyclic AMP + diphosphate. CC -!- COFACTOR: Binds 2 magnesium ions per subunit (By similarity). CC -!- ENZYME REGULATION: Insensitive to calcium/calmodulin. Stimulated CC by the G protein beta and gamma subunit complex (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein CC (Potential). CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl CC cyclase family. CC -!- SIMILARITY: Contains 2 guanylate cyclase domains. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF093454; AAC62509.1; -; mRNA. DR EMBL; AE014296; AAF49089.3; -; Genomic_DNA. DR EMBL; AY119547; AAM50201.1; ALT_INIT; mRNA. DR PIR; B42088; B42088. DR PIR; T13158; T13158. DR RefSeq; NP_524173.2; -. DR UniGene; Dm.2181; -. DR HSSP; P26769; 1AB8. DR Ensembl; CG7978; Drosophila melanogaster. DR GeneID; 40180; -. DR FlyBase; FBgn0004852; Ac76E. DR ArrayExpress; Q9VW60; -. DR GermOnline; CG7978; Drosophila melanogaster. DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB. DR GO; GO:0004016; F:adenylate cyclase activity; ISS:UniProtKB. DR GO; GO:0007190; P:adenylate cyclase activation; ISS:UniProtKB. DR GO; GO:0006171; P:cAMP biosynthetic process; ISS:UniProtKB. DR InterPro; IPR001054; A/G_cyclase. DR InterPro; IPR009398; Aden_cycl_like. DR Pfam; PF06327; DUF1053; 1. DR Pfam; PF00211; Guanylate_cyc; 2. DR SMART; SM00044; CYCc; 2. DR PROSITE; PS00452; GUANYLATE_CYCLASE_1; 2. DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 2. PE 2: Evidence at transcript level; KW cAMP biosynthesis; Complete proteome; Glycoprotein; Lyase; Magnesium; KW Membrane; Metal-binding; Repeat; Transmembrane. FT CHAIN 1 1307 Adenylate cyclase type 2. FT /FTId=PRO_0000195713. FT TRANSMEM 85 105 Potential. FT TRANSMEM 113 133 Potential. FT TRANSMEM 137 157 Potential. FT TRANSMEM 178 198 Potential. FT TRANSMEM 211 231 Potential. FT TOPO_DOM 232 828 Cytoplasmic (Potential). FT TRANSMEM 829 849 Potential. FT TRANSMEM 851 871 Potential. FT TRANSMEM 900 920 Potential. FT TRANSMEM 963 983 Potential. FT TRANSMEM 987 1007 Potential. FT TRANSMEM 1024 1044 Potential. FT TOPO_DOM 1045 1307 Cytoplasmic (Potential). FT DOMAIN 317 444 Guanylate cyclase 1. FT DOMAIN 1110 1255 Guanylate cyclase 2. FT METAL 322 322 Magnesium 1 (By similarity). FT METAL 322 322 Magnesium 2 (By similarity). FT METAL 323 323 Magnesium 2 (via carbonyl oxygen) (By FT similarity). FT METAL 366 366 Magnesium 1 (By similarity). FT METAL 366 366 Magnesium 2 (By similarity). FT CARBOHYD 934 934 N-linked (GlcNAc...) (Potential). FT CARBOHYD 941 941 N-linked (GlcNAc...) (Potential). FT CARBOHYD 948 948 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1019 1019 N-linked (GlcNAc...) (Potential). FT CONFLICT 538 538 V -> G (in Ref. 1). FT CONFLICT 679 679 A -> VSS (in Ref. 1). FT CONFLICT 1037 1037 I -> T (in Ref. 1). FT CONFLICT 1183 1183 T -> TSRSFA (in Ref. 4). SQ SEQUENCE 1307 AA; 142817 MW; D7EE45CF93F80161 CRC64; MVNHNAETAK TGNGTNATAN LIVKADGNAT QPKAMTSSAA RMNDALSASL ADLSEQENGT TAEDIHLNDL YTRYRQRLRK SLFRSGLLTS LLACVVSIII GIVYGQHLVQ TMLLVLAALI SGSILTALQF PAVLSSPAAA LAFAIVTTFS LGTIAAITGD ELAPLPMYAL FLCIHSMLPI SWPVSVVLAL FMTAIHIVYR IGTSPDYAPN LPMLFGEIVM LASASVSGLY YRIMSDAAHN RTVDGTRTGI EQRVKLECER EQQEQLLLSV IPAYIAAEVK RSIMLKMADA CQRAGGQAST SATRFHELHV QRHTNVTILF ADIVNFTPLS SSLTASDLVK TLNDLFGRFD QIAQENQCLR IKILGDCYYC VSGLPISRPQ HATNCVNMGL QMIDAIRHVR EATGINVDMR IGIHTGNVLC GVLGLRKWQF DVWSDDVTLA NHMESGGVAG RVHITKQTLD FLGDKFEVEQ GEGGNRDAYL ADHKVESYLI VPPKPAYTYS VPRVVECIEQ NDPSPTTEET KEIKETDQSH EATDVADVLL PVTVAPPPAI VDEKMSPTSI NSQEAPLHAP LASAASMSIK ELSEEEDEAD EATAVTEPLM HRDQDGKNDK EPKANGGHRG SGDSAASESV AKSAALSLPA DDLLSMSGSE SGISNSGAQA QSSNPASVTP TAAAPAGGAA SNSLTVAEAP ERSRRKLSVQ GLMSFADRRR SSGAFIEGRK LSIHSGESFR SHAGHVTRNR PSSKMTKYVE CWGADRPFAN IAESKLVKNI GLASIAMIES NLLPPERKCF NFNFFGPPTE LKPFTMWYRN TPREAMYRAQ PDTHFRFDLI CAFVLFLSLA VVQLIVIELN LALLGSLLAS FVSLALFLYL SNMSVPDVHA STTERNGPGQ VVASSRYLRL AMFVVVNILI SSCAVFSVIN YTVPDGVSKE PSSNQTILES NFSSVFVNST LEDVQLWEID YAIPIAPVFL YCCAISLAAI SAFLRSGFIL KLIAMLVAVI AQVTVLGYSD LFEMYNDANI THGLPLEIKG FLLLLVIILV LHTLDRQGEY VARTDFLWKA KLKVEQEEVE TMRGINKILL ENILPAHVAT HFLHLERSTE LYHESYSCVA VMFASIPNYK EFYDETDVNK QGLECLRLLN EIICDFDKLL LKPKFSGIEK IKTIASTYMC ASGLRPGKED GATDEKRTEE HNVVILVEFA IALMSILDSI NRESFQRFRL RIGLNHGPVI AGVIGAQKPQ YDIWSNTVNV ASRMDSCGVM GRLQTTENTA KILMTAGYEC ECRGLTYVKG KGNLVTYFVK TPFDGKL //