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P26769 (ADCY2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Adenylate cyclase type 2

EC=4.6.1.1
Alternative name(s):
ATP pyrophosphate-lyase 2
Adenylate cyclase type II
Adenylyl cyclase 2
Gene names
Name:Adcy2
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length1090 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This is a membrane-bound, calmodulin-insensitive adenylyl cyclase.

Catalytic activity

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

Cofactor

Binds 2 magnesium ions per subunit By similarity.

Enzyme regulation

Insensitive to calcium/calmodulin. Stimulated by the G protein beta and gamma subunit complex. Phosphorylation by RAF1 results in its activation By similarity.

Subunit structure

Interacts with RAF1 By similarity.

Subcellular location

Membrane; Multi-pass membrane protein.

Tissue specificity

Expressed in brain and, at lower levels, in olfactory epithelium and lung.

Post-translational modification

Phosphorylated by RAF1 By similarity.

Sequence similarities

Belongs to the adenylyl cyclase class-4/guanylyl cyclase family.

Contains 2 guanylate cyclase domains.

Ontologies

Keywords
   Biological processcAMP biosynthesis
   Cellular componentMembrane
   DomainRepeat
Transmembrane
Transmembrane helix
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionLyase
   PTMGlycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processadenylate cyclase-modulating G-protein coupled receptor signaling pathway

Inferred from direct assay PubMed 18164588. Source: BHF-UCL

cAMP biosynthetic process

Inferred from direct assay PubMed 18164588. Source: BHF-UCL

intracellular signal transduction

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: Ensembl

dendrite

Inferred from sequence or structural similarity. Source: UniProtKB

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

intracellular

Inferred from direct assay PubMed 18164588. Source: BHF-UCL

membrane

Inferred from sequence or structural similarity. Source: UniProtKB

membrane raft

Inferred from direct assay PubMed 18164588. Source: BHF-UCL

plasma membrane

Inferred from direct assay PubMed 18164588. Source: BHF-UCL

protein complex

Inferred from direct assay PubMed 16967511. Source: RGD

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

G-protein beta/gamma-subunit complex binding

Inferred from physical interaction PubMed 16967511. Source: RGD

adenylate cyclase activity

Inferred from direct assay PubMed 18164588. Source: BHF-UCL

adenylate cyclase binding

Inferred from direct assay PubMed 18164588. Source: BHF-UCL

calcium- and calmodulin-responsive adenylate cyclase activity

Inferred from direct assay PubMed 11350817. Source: RGD

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein heterodimerization activity

Inferred from direct assay PubMed 18164588. Source: BHF-UCL

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PDE4DQ08499-23EBI-1027877,EBI-8095525From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10901090Adenylate cyclase type 2
PRO_0000195686

Regions

Topological domain1 – 4444Cytoplasmic Potential
Transmembrane45 – 6521Helical; Potential
Transmembrane75 – 9521Helical; Potential
Transmembrane107 – 12721Helical; Potential
Transmembrane132 – 15221Helical; Potential
Transmembrane157 – 17721Helical; Potential
Transmembrane186 – 20621Helical; Potential
Topological domain207 – 600394Cytoplasmic Potential
Transmembrane601 – 62121Helical; Potential
Transmembrane626 – 64621Helical; Potential
Transmembrane679 – 69921Helical; Potential
Transmembrane734 – 75421Helical; Potential
Transmembrane763 – 78321Helical; Potential
Transmembrane800 – 82021Helical; Potential
Topological domain821 – 1090270Cytoplasmic Potential

Sites

Metal binding2941Magnesium 1 By similarity
Metal binding2941Magnesium 2 By similarity
Metal binding2951Magnesium 2; via carbonyl oxygen By similarity
Metal binding3381Magnesium 1 By similarity
Metal binding3381Magnesium 2 By similarity

Amino acid modifications

Glycosylation7121N-linked (GlcNAc...) Potential
Glycosylation7171N-linked (GlcNAc...) Potential

Secondary structure

................................. 1090
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P26769 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: 935CE44DF73199B3

FASTA1,090123,316
        10         20         30         40         50         60 
MRRRRYLRDR AEAAAAAAAG GGEGLQRSRD WLYESYYCMS QQHPLIVFLL LIVMGACLAL 

        70         80         90        100        110        120 
LAVFFALGLE VEDHVAFLIT VPTALAIFFA IFILVCIESV FKKLLRVFSL VIWICLVAMG 

       130        140        150        160        170        180 
YLFMCFGGTV SAWDQVSFFL FIIFVVYTML PFNMRDAIIA SILTSSSHTI VLSVYLSATP 

       190        200        210        220        230        240 
GAKEHLFWQI LANVIIFICG NLAGAYHKHL MELALQQTYR DTCNCIKSRI KLEFEKRQQE 

       250        260        270        280        290        300 
RLLLSLLPAH IAMEMKAEII QRLQGPKAGQ MENTNNFHNL YVKRHTNVSI LYADIVGFTR 

       310        320        330        340        350        360 
LASDCSPGEL VHMLNELFGK FDQIAKENEC MRIKILGDCY YCVSGLPISL PNHAKNCVKM 

       370        380        390        400        410        420 
GLDMCEAIKK VRDATGVDIN MRVGVHSGNV LCGVIGLQKW QYDVWSHDVT LANHMEAGGV 

       430        440        450        460        470        480 
PGRVHISSVT LEHLNGAYKV EEGDGEIRDP YLKQHLVKTY FVINPKGERR SPQHLFRPRH 

       490        500        510        520        530        540 
TLDGAKMRAS VRMTRYLESW GAAKPFAHLH HRDSMTTENG KISTTDVPMG QHNFQNRTLR 

       550        560        570        580        590        600 
TKSQKKRFEE ELNERMIQAI DGINAQKQWL KSEDIQRISL LFYNKNIEKE YRATALPAFK 

       610        620        630        640        650        660 
YYVTCACLIF LCIFIVQILV LPKTSILGFS FGAAFLSLIF ILFVCFAGQL LQCSKKASTS 

       670        680        690        700        710        720 
LMWLLKSSGI IANRPWPRIS LTIVTTAIIL TMAVFNMFFL SNSEETTLPT ANTSNANVSV 

       730        740        750        760        770        780 
PDNQASILHA RNLFFLPYFI YSCILGLISC SVFLRVNYEL KMLIMMVALV GYNTILLHTH 

       790        800        810        820        830        840 
AHVLDAYSQV LFQRPGIWKD LKTMGSVSLS IFFITLLVLG RQSEYYCRLD FLWKNKFKKE 

       850        860        870        880        890        900 
REEIETMENL NRVLLENVLP AHVAEHFLAR SLKNEELYHQ SYDCVCVMFA SIPDFKEFYT 

       910        920        930        940        950        960 
ESDVNKEGLE CLRLLNEIIA DFDDLLSKPK FSGVEKIKTI GSTYMAATGL SAIPSQEHAQ 

       970        980        990       1000       1010       1020 
EPERQYMHIG TMVEFAYALV GKLDAINKHS FNDFKLRVGI NHGPVIAGVI GAQKPQYDIW 

      1030       1040       1050       1060       1070       1080 
GNTVNVASRM DSTGVLDKIQ VTEETSLILQ TLGYTCTCRG IINVKGKGDL KTYFVNTEMS 

      1090 
RSLSQSNLAS 

« Hide

References

[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].
Tissue: Brain.
[2]"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 (2.58 ANGSTROMS) OF 871-1090.
[3]Erratum
Zhang G., Liu Y., Ruoho A.E., Hurley J.H.
Nature 388:204-204(1997)
[4]"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 COMPLEX WITH G(S)-ALPHA.
[5]"Two-metal-ion catalysis in adenylyl cyclase."
Tesmer J.J.G., Sunahara R.K., Johnson R.A., Gosselin G., Gilman A.G., Sprang S.R.
Science 285:756-760(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 870-1081 OF COMPLEX WITH G(S)-ALPHA.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M80550 mRNA. Translation: AAA40682.1.
PIRA41541.
RefSeqNP_112269.1. NM_031007.1.
UniGeneRn.10731.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP26769.
SMRP26769. Positions 277-463, 878-1077.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid249536. 1 interaction.
DIPDIP-164N.
IntActP26769. 7 interactions.
MINTMINT-8041796.
STRING10116.ENSRNOP00000038994.

Chemistry

BindingDBP26769.
ChEMBLCHEMBL2958.

PTM databases

PhosphoSiteP26769.

Proteomic databases

PaxDbP26769.
PRIDEP26769.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID81636.
KEGGrno:81636.
UCSCRGD:619965. rat.

Organism-specific databases

CTD108.
RGD619965. Adcy2.

Phylogenomic databases

eggNOGCOG2114.
HOGENOMHOG000006941.
HOVERGENHBG050458.
InParanoidP26769.
KOK08042.
PhylomeDBP26769.

Enzyme and pathway databases

BRENDA4.6.1.1. 5301.

Gene expression databases

ArrayExpressP26769.
GenevestigatorP26769.

Family and domain databases

Gene3D3.30.70.1230. 2 hits.
InterProIPR001054. A/G_cyclase.
IPR018297. A/G_cyclase_CS.
IPR009398. Adenylate_cyclase-like.
[Graphical view]
PfamPF06327. DUF1053. 1 hit.
PF00211. Guanylate_cyc. 2 hits.
[Graphical view]
SMARTSM00044. CYCc. 2 hits.
[Graphical view]
SUPFAMSSF55073. SSF55073. 2 hits.
PROSITEPS00452. GUANYLATE_CYCLASE_1. 2 hits.
PS50125. GUANYLATE_CYCLASE_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP26769.
NextBio615124.

Entry information

Entry nameADCY2_RAT
AccessionPrimary (citable) accession number: P26769
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: April 16, 2014
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references