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Protein

Adenylate cyclase type 2

Gene

Ac76E

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Catalyzes the formation of the signaling molecule cAMP in response to G-protein signaling.By similarity

Catalytic activityi

ATP = 3',5'-cyclic AMP + diphosphate.By similarity

Cofactori

Mg2+By similarity, Mn2+By similarityNote: Binds 2 magnesium ions per subunit. Is also active with manganese (in vitro).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi322 – 3221Magnesium 1; catalyticPROSITE-ProRule annotationBy similarity
Metal bindingi322 – 3221Magnesium 2; catalyticPROSITE-ProRule annotationBy similarity
Metal bindingi323 – 3231Magnesium 2; via carbonyl oxygen; catalyticPROSITE-ProRule annotation
Metal bindingi366 – 3661Magnesium 1; catalyticPROSITE-ProRule annotationBy similarity
Metal bindingi366 – 3661Magnesium 2; catalyticPROSITE-ProRule annotationBy similarity
Binding sitei410 – 4101ATPBy similarity
Binding sitei1162 – 11621ATPBy similarity
Binding sitei1289 – 12891ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi322 – 3276ATPBy similarity
Nucleotide bindingi364 – 3663ATPBy similarity
Nucleotide bindingi1242 – 12443ATPBy similarity
Nucleotide bindingi1249 – 12535ATPBy similarity

GO - Molecular functioni

  • adenylate cyclase activity Source: FlyBase
  • ATP binding Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • cAMP biosynthetic process Source: FlyBase
  • instar larval or pupal development Source: FlyBase
  • intracellular signal transduction Source: InterPro
  • negative regulation of multicellular organism growth Source: FlyBase
  • response to starvation Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

cAMP biosynthesis

Keywords - Ligandi

ATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-DME-163359. Glucagon signaling in metabolic regulation.
R-DME-163615. PKA activation.
R-DME-164378. PKA activation in glucagon signalling.
R-DME-170660. Adenylate cyclase activating pathway.
R-DME-170670. Adenylate cyclase inhibitory pathway.
R-DME-418555. G alpha (s) signalling events.
R-DME-418597. G alpha (z) signalling events.
R-DME-432040. Vasopressin regulates renal water homeostasis via Aquaporins.

Names & Taxonomyi

Protein namesi
Recommended name:
Adenylate cyclase type 2 (EC:4.6.1.1By similarity)
Alternative name(s):
ATP pyrophosphate-lyase 2
Adenylyl cyclase 76E
Gene namesi
Name:Ac76EImported
ORF Names:CG7978
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0004852. Ac76E.

Subcellular locationi

  • Membrane By similarity; Multi-pass membrane protein By similarity
  • Cell membrane By similarity; Multi-pass membrane protein By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei85 – 10521HelicalSequence analysisAdd
BLAST
Transmembranei113 – 13321HelicalSequence analysisAdd
BLAST
Transmembranei137 – 15721HelicalSequence analysisAdd
BLAST
Transmembranei178 – 19821HelicalSequence analysisAdd
BLAST
Transmembranei211 – 23121HelicalSequence analysisAdd
BLAST
Topological domaini232 – 828597CytoplasmicSequence analysisAdd
BLAST
Transmembranei829 – 84921HelicalSequence analysisAdd
BLAST
Transmembranei851 – 87121HelicalSequence analysisAdd
BLAST
Transmembranei900 – 92021HelicalSequence analysisAdd
BLAST
Transmembranei963 – 98321HelicalSequence analysisAdd
BLAST
Transmembranei987 – 100721HelicalSequence analysisAdd
BLAST
Transmembranei1024 – 104421HelicalSequence analysisAdd
BLAST
Topological domaini1045 – 1307263CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13071307Adenylate cyclase type 2PRO_0000195713Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi934 – 9341N-linked (GlcNAc...)Sequence analysis
Glycosylationi941 – 9411N-linked (GlcNAc...)Sequence analysis
Glycosylationi948 – 9481N-linked (GlcNAc...)Sequence analysis
Glycosylationi1019 – 10191N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ9VW60.

Expressioni

Gene expression databases

BgeeiQ9VW60.
ExpressionAtlasiQ9VW60. differential.
GenevisibleiQ9VW60. DM.

Interactioni

Protein-protein interaction databases

IntActiQ9VW60. 1 interaction.
STRINGi7227.FBpp0293288.

Structurei

3D structure databases

ProteinModelPortaliQ9VW60.
SMRiQ9VW60. Positions 305-491, 1102-1301.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini317 – 444128Guanylate cyclase 1PROSITE-ProRule annotationAdd
BLAST
Domaini1110 – 1255146Guanylate cyclase 2PROSITE-ProRule annotationAdd
BLAST

Domaini

The protein contains two modules with six transmembrane helices each; both are required for catalytic activity. Isolated N-terminal or C-terminal guanylate cyclase domains have no catalytic activity, but when they are brought together, enzyme activity is restored. The active site is at the interface of the two domains. Both contribute substrate-binding residues, but the catalytic metal ions are bound exclusively via the N-terminal guanylate cyclase domain.By similarity

Sequence similaritiesi

Belongs to the adenylyl cyclase class-4/guanylyl cyclase family.PROSITE-ProRule annotationBy similarity
Contains 2 guanylate cyclase domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3619. Eukaryota.
COG2114. LUCA.
GeneTreeiENSGT00760000119042.
InParanoidiQ9VW60.
KOiK08042.
OrthoDBiEOG76X5ZC.
PhylomeDBiQ9VW60.

Family and domain databases

Gene3Di3.30.70.1230. 2 hits.
InterProiIPR001054. A/G_cyclase.
IPR018297. A/G_cyclase_CS.
IPR032628. AC_N.
IPR029787. Nucleotide_cyclase.
[Graphical view]
PfamiPF16214. AC_N. 1 hit.
PF00211. Guanylate_cyc. 2 hits.
[Graphical view]
SMARTiSM00044. CYCc. 2 hits.
[Graphical view]
SUPFAMiSSF55073. SSF55073. 2 hits.
PROSITEiPS00452. GUANYLATE_CYCLASE_1. 2 hits.
PS50125. GUANYLATE_CYCLASE_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9VW60-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVNHNAETAK TGNGTNATAN LIVKADGNAT QPKAMTSSAA RMNDALSASL
60 70 80 90 100
ADLSEQENGT TAEDIHLNDL YTRYRQRLRK SLFRSGLLTS LLACVVSIII
110 120 130 140 150
GIVYGQHLVQ TMLLVLAALI SGSILTALQF PAVLSSPAAA LAFAIVTTFS
160 170 180 190 200
LGTIAAITGD ELAPLPMYAL FLCIHSMLPI SWPVSVVLAL FMTAIHIVYR
210 220 230 240 250
IGTSPDYAPN LPMLFGEIVM LASASVSGLY YRIMSDAAHN RTVDGTRTGI
260 270 280 290 300
EQRVKLECER EQQEQLLLSV IPAYIAAEVK RSIMLKMADA CQRAGGQAST
310 320 330 340 350
SATRFHELHV QRHTNVTILF ADIVNFTPLS SSLTASDLVK TLNDLFGRFD
360 370 380 390 400
QIAQENQCLR IKILGDCYYC VSGLPISRPQ HATNCVNMGL QMIDAIRHVR
410 420 430 440 450
EATGINVDMR IGIHTGNVLC GVLGLRKWQF DVWSDDVTLA NHMESGGVAG
460 470 480 490 500
RVHITKQTLD FLGDKFEVEQ GEGGNRDAYL ADHKVESYLI VPPKPAYTYS
510 520 530 540 550
VPRVVECIEQ NDPSPTTEET KEIKETDQSH EATDVADVLL PVTVAPPPAI
560 570 580 590 600
VDEKMSPTSI NSQEAPLHAP LASAASMSIK ELSEEEDEAD EATAVTEPLM
610 620 630 640 650
HRDQDGKNDK EPKANGGHRG SGDSAASESV AKSAALSLPA DDLLSMSGSE
660 670 680 690 700
SGISNSGAQA QSSNPASVTP TAAAPAGGAA SNSLTVAEAP ERSRRKLSVQ
710 720 730 740 750
GLMSFADRRR SSGAFIEGRK LSIHSGESFR SHAGHVTRNR PSSKMTKYVE
760 770 780 790 800
CWGADRPFAN IAESKLVKNI GLASIAMIES NLLPPERKCF NFNFFGPPTE
810 820 830 840 850
LKPFTMWYRN TPREAMYRAQ PDTHFRFDLI CAFVLFLSLA VVQLIVIELN
860 870 880 890 900
LALLGSLLAS FVSLALFLYL SNMSVPDVHA STTERNGPGQ VVASSRYLRL
910 920 930 940 950
AMFVVVNILI SSCAVFSVIN YTVPDGVSKE PSSNQTILES NFSSVFVNST
960 970 980 990 1000
LEDVQLWEID YAIPIAPVFL YCCAISLAAI SAFLRSGFIL KLIAMLVAVI
1010 1020 1030 1040 1050
AQVTVLGYSD LFEMYNDANI THGLPLEIKG FLLLLVIILV LHTLDRQGEY
1060 1070 1080 1090 1100
VARTDFLWKA KLKVEQEEVE TMRGINKILL ENILPAHVAT HFLHLERSTE
1110 1120 1130 1140 1150
LYHESYSCVA VMFASIPNYK EFYDETDVNK QGLECLRLLN EIICDFDKLL
1160 1170 1180 1190 1200
LKPKFSGIEK IKTIASTYMC ASGLRPGKED GATDEKRTEE HNVVILVEFA
1210 1220 1230 1240 1250
IALMSILDSI NRESFQRFRL RIGLNHGPVI AGVIGAQKPQ YDIWSNTVNV
1260 1270 1280 1290 1300
ASRMDSCGVM GRLQTTENTA KILMTAGYEC ECRGLTYVKG KGNLVTYFVK

TPFDGKL
Length:1,307
Mass (Da):142,817
Last modified:October 1, 2002 - v3
Checksum:iD7EE45CF93F80161
GO

Sequence cautioni

The sequence AAM50201.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti538 – 5381V → G in AAC62509 (PubMed:1739965).Curated
Sequence conflicti679 – 6791A → VSS in AAC62509 (PubMed:1739965).Curated
Sequence conflicti1037 – 10371I → T in AAC62509 (PubMed:1739965).Curated
Sequence conflicti1183 – 11831T → TSRSFA in AAM50201 (PubMed:12537569).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF093454 mRNA. Translation: AAC62509.1.
AE014296 Genomic DNA. Translation: AAF49089.3.
AY119547 mRNA. Translation: AAM50201.1. Different initiation.
PIRiB42088.
T13158.
RefSeqiNP_524173.2. NM_079449.4.
UniGeneiDm.2181.

Genome annotation databases

EnsemblMetazoaiFBtr0074897; FBpp0074666; FBgn0004852.
GeneIDi40180.
KEGGidme:Dmel_CG7978.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF093454 mRNA. Translation: AAC62509.1.
AE014296 Genomic DNA. Translation: AAF49089.3.
AY119547 mRNA. Translation: AAM50201.1. Different initiation.
PIRiB42088.
T13158.
RefSeqiNP_524173.2. NM_079449.4.
UniGeneiDm.2181.

3D structure databases

ProteinModelPortaliQ9VW60.
SMRiQ9VW60. Positions 305-491, 1102-1301.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9VW60. 1 interaction.
STRINGi7227.FBpp0293288.

Proteomic databases

PaxDbiQ9VW60.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0074897; FBpp0074666; FBgn0004852.
GeneIDi40180.
KEGGidme:Dmel_CG7978.

Organism-specific databases

CTDi40180.
FlyBaseiFBgn0004852. Ac76E.

Phylogenomic databases

eggNOGiKOG3619. Eukaryota.
COG2114. LUCA.
GeneTreeiENSGT00760000119042.
InParanoidiQ9VW60.
KOiK08042.
OrthoDBiEOG76X5ZC.
PhylomeDBiQ9VW60.

Enzyme and pathway databases

ReactomeiR-DME-163359. Glucagon signaling in metabolic regulation.
R-DME-163615. PKA activation.
R-DME-164378. PKA activation in glucagon signalling.
R-DME-170660. Adenylate cyclase activating pathway.
R-DME-170670. Adenylate cyclase inhibitory pathway.
R-DME-418555. G alpha (s) signalling events.
R-DME-418597. G alpha (z) signalling events.
R-DME-432040. Vasopressin regulates renal water homeostasis via Aquaporins.

Miscellaneous databases

GenomeRNAii40180.
PROiQ9VW60.

Gene expression databases

BgeeiQ9VW60.
ExpressionAtlasiQ9VW60. differential.
GenevisibleiQ9VW60. DM.

Family and domain databases

Gene3Di3.30.70.1230. 2 hits.
InterProiIPR001054. A/G_cyclase.
IPR018297. A/G_cyclase_CS.
IPR032628. AC_N.
IPR029787. Nucleotide_cyclase.
[Graphical view]
PfamiPF16214. AC_N. 1 hit.
PF00211. Guanylate_cyc. 2 hits.
[Graphical view]
SMARTiSM00044. CYCc. 2 hits.
[Graphical view]
SUPFAMiSSF55073. SSF55073. 2 hits.
PROSITEiPS00452. GUANYLATE_CYCLASE_1. 2 hits.
PS50125. GUANYLATE_CYCLASE_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The Drosophila learning and memory gene rutabaga encodes a Ca2+/Calmodulin-responsive adenylyl cyclase."
    Levin L.R., Han P.-L., Hwang P.M., Feinstein P.G., Davis R.L., Reed R.R.
    Cell 68:479-489(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Canton-SImported.
  2. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley1 Publication.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. "A Drosophila full-length cDNA resource."
    Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
    Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 434-1307.
    Strain: BerkeleyImported.
    Tissue: Head1 Publication.

Entry informationi

Entry nameiADCY2_DROME
AccessioniPrimary (citable) accession number: Q9VW60
Secondary accession number(s): O77247, Q8MRK9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: October 1, 2002
Last modified: June 8, 2016
This is version 113 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.