Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Adenylate cyclase type 2

Gene

Adcy2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the formation of the signaling molecule cAMP in response to G-protein signaling (PubMed:22906005, PubMed:24363043, PubMed:10427002, PubMed:1719547, PubMed:7761832, PubMed:21596131, PubMed:11087399, PubMed:15591060, PubMed:19243146, PubMed:16766715). Down-stream signaling cascades mediate changes in gene expression patterns and lead to increased IL6 production (PubMed:24363043). Functions in signaling cascades downstream of the muscarinic acetylcholine receptors (PubMed:22906005).10 Publications

Catalytic activityi

ATP = 3',5'-cyclic AMP + diphosphate.10 Publications

Cofactori

Mg2+6 Publications, Mn2+3 PublicationsNote: Binds 2 magnesium ions per subunit. Is also active with manganese (in vitro).1 Publication1 Publication

Enzyme regulationi

Activated by forskolin (PubMed:1719547, PubMed:22906005, PubMed:24363043). Is not activated by calmodulin (PubMed:1719547). Inhibited by calcium ions, already at micromolar concentration. Activated by the G protein alpha subunit GNAS (PubMed:1719547, PubMed:7761832, PubMed:21596131). Activated by the G protein beta and gamma subunit complex (PubMed:7761832, PubMed:21596131, PubMed:22906005). Phosphorylation by RAF1 results in its activation (By similarity). Phosphorylation by PKC activates the enzyme (PubMed:22906005).By similarity5 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi294 – 2941Magnesium 1; catalyticPROSITE-ProRule annotationCurated
Metal bindingi294 – 2941Magnesium 2; catalyticPROSITE-ProRule annotationCurated1 Publication
Metal bindingi295 – 2951Magnesium 2; via carbonyl oxygen; catalyticPROSITE-ProRule annotationCurated1 Publication
Metal bindingi338 – 3381Magnesium 1; catalyticPROSITE-ProRule annotationCurated
Metal bindingi338 – 3381Magnesium 2; catalyticPROSITE-ProRule annotationCurated1 Publication
Binding sitei382 – 3821ATPBy similarity
Binding sitei938 – 9381ATP5 Publications
Binding sitei1065 – 10651ATP5 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi294 – 2996ATPBy similarity
Nucleotide bindingi336 – 3383ATPBy similarity
Nucleotide bindingi1018 – 10203ATP5 Publications
Nucleotide bindingi1025 – 10295ATPCombined sources1 Publication

GO - Molecular functioni

  • adenylate cyclase activity Source: UniProtKB
  • adenylate cyclase binding Source: BHF-UCL
  • ATP binding Source: UniProtKB-KW
  • G-protein beta/gamma-subunit complex binding Source: RGD
  • magnesium ion binding Source: UniProtKB
  • manganese ion binding Source: UniProtKB
  • protein heterodimerization activity Source: BHF-UCL

GO - Biological processi

  • adenylate cyclase-activating G-protein coupled receptor signaling pathway Source: UniProtKB
  • adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway Source: GO_Central
  • adenylate cyclase-modulating G-protein coupled receptor signaling pathway Source: BHF-UCL
  • cAMP biosynthetic process Source: UniProtKB
  • cAMP-mediated signaling Source: UniProtKB
  • cellular response to forskolin Source: UniProtKB
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

BRENDAi4.6.1.1. 5301.

Names & Taxonomyi

Protein namesi
Recommended name:
Adenylate cyclase type 2 (EC:4.6.1.17 Publications)
Alternative name(s):
ATP pyrophosphate-lyase 2
Adenylate cyclase type II
Adenylyl cyclase 2
Short name:
AC21 Publication
Gene namesi
Name:Adcy2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Unplaced

Organism-specific databases

RGDi619965. Adcy2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 4444CytoplasmicSequence analysisAdd
BLAST
Transmembranei45 – 6521HelicalSequence analysisAdd
BLAST
Transmembranei75 – 9521HelicalSequence analysisAdd
BLAST
Transmembranei107 – 12721HelicalSequence analysisAdd
BLAST
Transmembranei132 – 15221HelicalSequence analysisAdd
BLAST
Transmembranei157 – 17721HelicalSequence analysisAdd
BLAST
Transmembranei186 – 20621HelicalSequence analysisAdd
BLAST
Topological domaini207 – 600394CytoplasmicSequence analysisAdd
BLAST
Transmembranei601 – 62121HelicalSequence analysisAdd
BLAST
Transmembranei626 – 64621HelicalSequence analysisAdd
BLAST
Transmembranei679 – 69921HelicalSequence analysisAdd
BLAST
Transmembranei734 – 75421HelicalSequence analysisAdd
BLAST
Transmembranei763 – 78321HelicalSequence analysisAdd
BLAST
Transmembranei800 – 82021HelicalSequence analysisAdd
BLAST
Topological domaini821 – 1090270CytoplasmicSequence analysisCuratedAdd
BLAST

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • dendrite Source: UniProtKB
  • integral component of plasma membrane Source: UniProtKB
  • intracellular Source: BHF-UCL
  • membrane Source: UniProtKB
  • membrane raft Source: BHF-UCL
  • plasma membrane Source: BHF-UCL
  • protein complex Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi490 – 4901S → A: Reduces activation by PKC. Abolishes activation by PKC; when associated with A-543. 1 Publication
Mutagenesisi490 – 4901S → D: Increases basal level of enzyme activity. Abolishes activation by PKC; when associated with D-543. 1 Publication
Mutagenesisi543 – 5431S → A: Reduces activation by PKC. Abolishes activation by PKC; when associated with A-490. 1 Publication
Mutagenesisi543 – 5431S → D: Increases basal level of enzyme activity. Abolishes activation by PKC; when associated with D-490. 1 Publication

Chemistry

ChEMBLiCHEMBL2095179.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10901090Adenylate cyclase type 2PRO_0000195686Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei490 – 4901Phosphoserine; by PKC1 Publication
Modified residuei543 – 5431Phosphoserine; by PKC1 Publication
Glycosylationi712 – 7121N-linked (GlcNAc...)Sequence analysis
Glycosylationi717 – 7171N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

Phosphorylated by RAF1 (By similarity).By similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP26769.
PRIDEiP26769.

PTM databases

iPTMnetiP26769.
PhosphoSiteiP26769.

Expressioni

Tissue specificityi

Expressed in brain, olfactory epithelium and lung.1 Publication

Interactioni

Subunit structurei

Interacts with RAF1 (By similarity). Interacts with GNAS (PubMed:9417641, PubMed:10427002, PubMed:11087399, PubMed:15591060, PubMed:16766715, PubMed:19243146). Interacts with the G protein beta and gamma subunit complex (PubMed:21596131).By similarity7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PDE4DQ08499-23EBI-1027877,EBI-8095525From a different organism.

Protein-protein interaction databases

BioGridi249536. 1 interaction.
DIPiDIP-164N.
IntActiP26769. 7 interactions.
MINTiMINT-8041796.
STRINGi10116.ENSRNOP00000038994.

Chemistry

BindingDBiP26769.

Structurei

Secondary structure

1
1090
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi879 – 89113Combined sources
Helixi895 – 8984Combined sources
Turni903 – 9086Combined sources
Helixi909 – 92315Combined sources
Helixi924 – 9274Combined sources
Helixi929 – 9313Combined sources
Beta strandi934 – 9407Combined sources
Beta strandi943 – 9486Combined sources
Helixi967 – 98721Combined sources
Turni988 – 9914Combined sources
Beta strandi997 – 101014Combined sources
Beta strandi1012 – 10143Combined sources
Beta strandi1016 – 10216Combined sources
Helixi1022 – 103211Combined sources
Beta strandi1039 – 10413Combined sources
Helixi1043 – 105210Combined sources
Beta strandi1056 – 10649Combined sources
Turni1065 – 10673Combined sources
Beta strandi1068 – 10758Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AB8X-ray2.20A/B871-1090[»]
1AZSX-ray2.30B870-1081[»]
1CJKX-ray3.00B870-1081[»]
1CJTX-ray2.80B870-1081[»]
1CJUX-ray2.80B870-1081[»]
1CJVX-ray3.00B870-1081[»]
1CS4X-ray2.50B870-1081[»]
1CULX-ray2.40B874-1081[»]
1TL7X-ray2.80B870-1081[»]
1U0HX-ray2.90B870-1081[»]
2GVDX-ray2.90B870-1081[»]
2GVZX-ray3.27B870-1081[»]
3C14X-ray2.68B870-1081[»]
3C15X-ray2.78B870-1081[»]
3C16X-ray2.87B870-1081[»]
3G82X-ray3.11B870-1081[»]
3MAAX-ray3.00B870-1081[»]
ProteinModelPortaliP26769.
SMRiP26769. Positions 277-463, 878-1077.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP26769.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni904 – 92118Interaction with GNAS1 PublicationAdd
BLAST
Regioni989 – 9924Interaction with GNAS1 Publication

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.6 Publications

Sequence similaritiesi

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

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3619. Eukaryota.
COG2114. LUCA.
HOGENOMiHOG000006941.
HOVERGENiHBG050458.
InParanoidiP26769.
KOiK08042.
PhylomeDBiP26769.

Family and domain databases

Gene3Di3.30.70.1230. 2 hits.
InterProiIPR001054. A/G_cyclase.
IPR018297. A/G_cyclase_CS.
IPR032628. AC_N.
IPR030672. Adcy.
IPR009398. Adcy_conserved_dom.
IPR029787. Nucleotide_cyclase.
[Graphical view]
PfamiPF16214. AC_N. 1 hit.
PF06327. DUF1053. 1 hit.
PF00211. Guanylate_cyc. 2 hits.
[Graphical view]
PIRSFiPIRSF039050. Ade_cyc. 1 hit.
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.

P26769-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRRRRYLRDR AEAAAAAAAG GGEGLQRSRD WLYESYYCMS QQHPLIVFLL
60 70 80 90 100
LIVMGACLAL LAVFFALGLE VEDHVAFLIT VPTALAIFFA IFILVCIESV
110 120 130 140 150
FKKLLRVFSL VIWICLVAMG YLFMCFGGTV SAWDQVSFFL FIIFVVYTML
160 170 180 190 200
PFNMRDAIIA SILTSSSHTI VLSVYLSATP GAKEHLFWQI LANVIIFICG
210 220 230 240 250
NLAGAYHKHL MELALQQTYR DTCNCIKSRI KLEFEKRQQE RLLLSLLPAH
260 270 280 290 300
IAMEMKAEII QRLQGPKAGQ MENTNNFHNL YVKRHTNVSI LYADIVGFTR
310 320 330 340 350
LASDCSPGEL VHMLNELFGK FDQIAKENEC MRIKILGDCY YCVSGLPISL
360 370 380 390 400
PNHAKNCVKM GLDMCEAIKK VRDATGVDIN MRVGVHSGNV LCGVIGLQKW
410 420 430 440 450
QYDVWSHDVT LANHMEAGGV PGRVHISSVT LEHLNGAYKV EEGDGEIRDP
460 470 480 490 500
YLKQHLVKTY FVINPKGERR SPQHLFRPRH TLDGAKMRAS VRMTRYLESW
510 520 530 540 550
GAAKPFAHLH HRDSMTTENG KISTTDVPMG QHNFQNRTLR TKSQKKRFEE
560 570 580 590 600
ELNERMIQAI DGINAQKQWL KSEDIQRISL LFYNKNIEKE YRATALPAFK
610 620 630 640 650
YYVTCACLIF LCIFIVQILV LPKTSILGFS FGAAFLSLIF ILFVCFAGQL
660 670 680 690 700
LQCSKKASTS LMWLLKSSGI IANRPWPRIS LTIVTTAIIL TMAVFNMFFL
710 720 730 740 750
SNSEETTLPT ANTSNANVSV PDNQASILHA RNLFFLPYFI YSCILGLISC
760 770 780 790 800
SVFLRVNYEL KMLIMMVALV GYNTILLHTH AHVLDAYSQV LFQRPGIWKD
810 820 830 840 850
LKTMGSVSLS IFFITLLVLG RQSEYYCRLD FLWKNKFKKE REEIETMENL
860 870 880 890 900
NRVLLENVLP AHVAEHFLAR SLKNEELYHQ SYDCVCVMFA SIPDFKEFYT
910 920 930 940 950
ESDVNKEGLE CLRLLNEIIA DFDDLLSKPK FSGVEKIKTI GSTYMAATGL
960 970 980 990 1000
SAIPSQEHAQ EPERQYMHIG TMVEFAYALV GKLDAINKHS FNDFKLRVGI
1010 1020 1030 1040 1050
NHGPVIAGVI GAQKPQYDIW GNTVNVASRM DSTGVLDKIQ VTEETSLILQ
1060 1070 1080 1090
TLGYTCTCRG IINVKGKGDL KTYFVNTEMS RSLSQSNLAS
Length:1,090
Mass (Da):123,316
Last modified:August 1, 1992 - v1
Checksum:i935CE44DF73199B3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M80550 mRNA. Translation: AAA40682.1.
PIRiA41541.
RefSeqiNP_112269.1. NM_031007.1.
UniGeneiRn.10731.

Genome annotation databases

GeneIDi81636.
KEGGirno:81636.
UCSCiRGD:619965. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M80550 mRNA. Translation: AAA40682.1.
PIRiA41541.
RefSeqiNP_112269.1. NM_031007.1.
UniGeneiRn.10731.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AB8X-ray2.20A/B871-1090[»]
1AZSX-ray2.30B870-1081[»]
1CJKX-ray3.00B870-1081[»]
1CJTX-ray2.80B870-1081[»]
1CJUX-ray2.80B870-1081[»]
1CJVX-ray3.00B870-1081[»]
1CS4X-ray2.50B870-1081[»]
1CULX-ray2.40B874-1081[»]
1TL7X-ray2.80B870-1081[»]
1U0HX-ray2.90B870-1081[»]
2GVDX-ray2.90B870-1081[»]
2GVZX-ray3.27B870-1081[»]
3C14X-ray2.68B870-1081[»]
3C15X-ray2.78B870-1081[»]
3C16X-ray2.87B870-1081[»]
3G82X-ray3.11B870-1081[»]
3MAAX-ray3.00B870-1081[»]
ProteinModelPortaliP26769.
SMRiP26769. Positions 277-463, 878-1077.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi249536. 1 interaction.
DIPiDIP-164N.
IntActiP26769. 7 interactions.
MINTiMINT-8041796.
STRINGi10116.ENSRNOP00000038994.

Chemistry

BindingDBiP26769.
ChEMBLiCHEMBL2095179.

PTM databases

iPTMnetiP26769.
PhosphoSiteiP26769.

Proteomic databases

PaxDbiP26769.
PRIDEiP26769.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi81636.
KEGGirno:81636.
UCSCiRGD:619965. rat.

Organism-specific databases

CTDi108.
RGDi619965. Adcy2.

Phylogenomic databases

eggNOGiKOG3619. Eukaryota.
COG2114. LUCA.
HOGENOMiHOG000006941.
HOVERGENiHBG050458.
InParanoidiP26769.
KOiK08042.
PhylomeDBiP26769.

Enzyme and pathway databases

BRENDAi4.6.1.1. 5301.

Miscellaneous databases

EvolutionaryTraceiP26769.
NextBioi615124.
PROiP26769.

Family and domain databases

Gene3Di3.30.70.1230. 2 hits.
InterProiIPR001054. A/G_cyclase.
IPR018297. A/G_cyclase_CS.
IPR032628. AC_N.
IPR030672. Adcy.
IPR009398. Adcy_conserved_dom.
IPR029787. Nucleotide_cyclase.
[Graphical view]
PfamiPF16214. AC_N. 1 hit.
PF06327. DUF1053. 1 hit.
PF00211. Guanylate_cyc. 2 hits.
[Graphical view]
PIRSFiPIRSF039050. Ade_cyc. 1 hit.
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. "Molecular cloning and characterization of a Ca2+/calmodulin-insensitive adenylyl cyclase from rat brain."
    Feinstein P.G., Schrader K.A., Bakalyar H.A., Tang W.J., Krupinski J., Gilman A.G., Reed R.R.
    Proc. Natl. Acad. Sci. U.S.A. 88:10173-10177(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Brain.
  2. "A region of adenylyl cyclase 2 critical for regulation by G protein beta gamma subunits."
    Chen J., DeVivo M., Dingus J., Harry A., Li J., Sui J., Carty D.J., Blank J.L., Exton J.H., Stoffel R.H.
    Science 268:1166-1169(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, SUBCELLULAR LOCATION.
  3. "Identification of new Gbetagamma interaction sites in adenylyl cyclase 2."
    Boran A.D., Chen Y., Iyengar R.
    Cell. Signal. 23:1489-1495(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, SUBCELLULAR LOCATION, INTERACTION WITH THE G PROTEIN BETA AND GAMMA SUBUNIT COMPLEX.
  4. "Muscarinic receptors stimulate AC2 by novel phosphorylation sites, whereas Gbetagamma subunits exert opposing effects depending on the G-protein source."
    Shen J.X., Wachten S., Halls M.L., Everett K.L., Cooper D.M.
    Biochem. J. 447:393-405(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-490 AND SER-543, MUTAGENESIS OF SER-490 AND SER-543, CATALYTIC ACTIVITY, FUNCTION, SUBCELLULAR LOCATION, ENZYME REGULATION.
  5. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "Non-raft adenylyl cyclase 2 defines a cAMP signaling compartment that selectively regulates IL-6 expression in airway smooth muscle cells: differential regulation of gene expression by AC isoforms."
    Bogard A.S., Birg A.V., Ostrom R.S.
    Naunyn Schmiedebergs Arch. Pharmacol. 387:329-339(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION.
  7. "Structure of the adenylyl cyclase catalytic core."
    Zhang G., Liu Y., Ruoho A.E., Hurley J.H.
    Nature 386:247-253(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 871-1090 IN COMPLEX WITH FORSKOLIN.
  8. Erratum
    Zhang G., Liu Y., Ruoho A.E., Hurley J.H.
    Nature 388:204-204(1997)
  9. "Crystal structure of the catalytic domains of adenylyl cyclase in a complex with Gsalpha.GTPgammaS."
    Tesmer J.J.G., Sunahara R.K., Gilman A.G., Sprang S.R.
    Science 278:1907-1916(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 870-1081 OF CHIMERA WITH ADCY5 IN COMPLEX WITH GNAS, INTERACTION WITH GNAS, DOMAIN.
  10. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 870-1081 OF CHIMERA WITH ADCY5 IN COMPLEX WITH GNAS AND ATP ANALOGS, INTERACTION WITH GNAS, DOMAIN, CATALYTIC ACTIVITY, FUNCTION, COFACTOR.
  11. Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 874-1081 OF CHIMERA WITH ADCY5 IN COMPLEX WITH GNAS; MAGNESIUM AND ATP ANALOGS, INTERACTION WITH GNAS, DOMAIN, FUNCTION, CATALYTIC ACTIVITY, COFACTOR.
  12. "Structural basis for the inhibition of mammalian membrane adenylyl cyclase by 2 '(3')-O-(N-Methylanthraniloyl)-guanosine 5 '-triphosphate."
    Mou T.C., Gille A., Fancy D.A., Seifert R., Sprang S.R.
    J. Biol. Chem. 280:7253-7261(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 870-1081 OF CHIMERA WITH ADCY5 IN COMPLEX WITH GNAS AND ATP ANALOG, FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH GNAS, DOMAIN.
  13. "Broad specificity of mammalian adenylyl cyclase for interaction with 2',3'-substituted purine- and pyrimidine nucleotide inhibitors."
    Mou T.C., Gille A., Suryanarayana S., Richter M., Seifert R., Sprang S.R.
    Mol. Pharmacol. 70:878-886(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 870-1081 OF CHIMERA WITH ADCY5 IN COMPLEX WITH GNAS AND ATP ANALOG, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, INTERACTION WITH GNAS, DOMAIN.
  14. "Structural basis for inhibition of mammalian adenylyl cyclase by calcium."
    Mou T.C., Masada N., Cooper D.M., Sprang S.R.
    Biochemistry 48:3387-3397(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.68 ANGSTROMS) OF 870-1081 OF CHIMERA WITH ADCY5 IN COMPLEX WITH GNAS; FORSKOLIN; MAGNESIUM IONS AND ATP ANALOG, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, INTERACTION WITH GNAS, DOMAIN.

Entry informationi

Entry nameiADCY2_RAT
AccessioniPrimary (citable) accession number: P26769
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: January 20, 2016
This is version 142 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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.