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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)DescriptionActionsGraphical viewLength
Metal bindingi322Magnesium 1; catalyticPROSITE-ProRule annotationBy similarity1
Metal bindingi322Magnesium 2; catalyticPROSITE-ProRule annotationBy similarity1
Metal bindingi323Magnesium 2; via carbonyl oxygen; catalyticPROSITE-ProRule annotation1
Metal bindingi366Magnesium 1; catalyticPROSITE-ProRule annotationBy similarity1
Metal bindingi366Magnesium 2; catalyticPROSITE-ProRule annotationBy similarity1
Binding sitei410ATPBy similarity1
Binding sitei1162ATPBy similarity1
Binding sitei1289ATPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi322 – 327ATPBy similarity6
Nucleotide bindingi364 – 366ATPBy similarity3
Nucleotide bindingi1242 – 1244ATPBy similarity3
Nucleotide bindingi1249 – 1253ATPBy similarity5

GO - Molecular functioni

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

GO - Biological processi

  • adenylate cyclase-activating G-protein coupled receptor signaling pathway Source: GO_Central
  • adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway Source: GO_Central
  • cAMP biosynthetic process Source: FlyBase
  • cAMP-mediated signaling Source: GO_Central
  • instar larval or pupal development Source: FlyBase
  • 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-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)DescriptionActionsGraphical viewLength
Transmembranei85 – 105HelicalSequence analysisAdd BLAST21
Transmembranei113 – 133HelicalSequence analysisAdd BLAST21
Transmembranei137 – 157HelicalSequence analysisAdd BLAST21
Transmembranei178 – 198HelicalSequence analysisAdd BLAST21
Transmembranei211 – 231HelicalSequence analysisAdd BLAST21
Topological domaini232 – 828CytoplasmicSequence analysisAdd BLAST597
Transmembranei829 – 849HelicalSequence analysisAdd BLAST21
Transmembranei851 – 871HelicalSequence analysisAdd BLAST21
Transmembranei900 – 920HelicalSequence analysisAdd BLAST21
Transmembranei963 – 983HelicalSequence analysisAdd BLAST21
Transmembranei987 – 1007HelicalSequence analysisAdd BLAST21
Transmembranei1024 – 1044HelicalSequence analysisAdd BLAST21
Topological domaini1045 – 1307CytoplasmicSequence analysisAdd BLAST263

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001957131 – 1307Adenylate cyclase type 2Add BLAST1307

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi934N-linked (GlcNAc...)Sequence analysis1
Glycosylationi941N-linked (GlcNAc...)Sequence analysis1
Glycosylationi948N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1019N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ9VW60.
PRIDEiQ9VW60.

Expressioni

Gene expression databases

BgeeiFBgn0004852.
ExpressionAtlasiQ9VW60. baseline.
GenevisibleiQ9VW60. DM.

Interactioni

Protein-protein interaction databases

IntActiQ9VW60. 1 interactor.
STRINGi7227.FBpp0293288.

Structurei

3D structure databases

ProteinModelPortaliQ9VW60.
SMRiQ9VW60.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini317 – 444Guanylate cyclase 1PROSITE-ProRule annotationAdd BLAST128
Domaini1110 – 1255Guanylate cyclase 2PROSITE-ProRule annotationAdd BLAST146

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.
OrthoDBiEOG091G05JR.
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 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti538V → G in AAC62509 (PubMed:1739965).Curated1
Sequence conflicti679A → VSS in AAC62509 (PubMed:1739965).Curated1
Sequence conflicti1037I → T in AAC62509 (PubMed:1739965).Curated1
Sequence conflicti1183T → TSRSFA in AAM50201 (PubMed:12537569).Curated1

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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9VW60. 1 interactor.
STRINGi7227.FBpp0293288.

Proteomic databases

PaxDbiQ9VW60.
PRIDEiQ9VW60.

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.
OrthoDBiEOG091G05JR.
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-432040. Vasopressin regulates renal water homeostasis via Aquaporins.

Miscellaneous databases

GenomeRNAii40180.
PROiQ9VW60.

Gene expression databases

BgeeiFBgn0004852.
ExpressionAtlasiQ9VW60. baseline.
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...

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: November 30, 2016
This is version 118 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.