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Reviewed, UniProtKB/Swiss-Prot P26769 (ADCY2_RAT)

Last modified June 16, 2009. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Adenylate cyclase type 2
    EC=4.6.1.1
Alternative name(s):
    Adenylate cyclase type II
    ATP pyrophosphate-lyase 2
    Adenylyl cyclase 2
Gene names
Name: Adcy2
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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Protein attributes

Sequence length1090 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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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.

Subcellular location

Membrane; Multi-pass membrane protein.

Tissue specificity

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

Sequence similarities

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

Contains 2 guanylate cyclase domains.

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Ontologies

Keywords
   Biological processcAMP biosynthesis
   Cellular componentMembrane
   DomainRepeat
Transmembrane
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionLyase
   PTMGlycoprotein
   Technical term3D-structure
Gene Ontology (GO)
   Biological processcAMP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

intracellular signaling cascade

Inferred from electronic annotation. Source: InterPro

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

adenylate cyclase activity Ref.1

Inferred from direct assay. Source: RGD

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10901090Adenylate cyclase type 2
PRO_0000195686

Regions

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

1 ............................. 1090
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P26769-1 [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

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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: 1719547] [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: 9069282] [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: 9417641] [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: 10427002] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 870-1081 OF COMPLEX WITH G(S)-ALPHA.
+Additional computationally mapped references.

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Cross-references

Sequence databases

M80550 mRNA. Translation: AAA40682.1.
IPIIPI00196228.
PIRA41541.
RefSeqNP_112269.1.
UniGeneRn.10731

3D structure databases

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[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:164N.

PTM databases

PhosphoSiteP26769.

Proteomic databases

PRIDEP26769.

Genome annotation databases

EnsemblENSRNOG00000032150. Rattus norvegicus. [Contig view]
GeneID81636.
KEGGrno:81636.

Organism-specific databases

RGD619965. Adcy2.

Phylogenomic databases

HOVERGENP26769.

Enzyme and pathway databases

BRENDA4.6.1.1. 248.

Gene expression databases

ArrayExpressP26769.
GermOnlineENSRNOG00000032150. Rattus norvegicus.

Family and domain databases

InterProIPR001054. A/G_cyclase.
IPR018297. A/G_cyclase_CS.
IPR009398. Aden_cycl-like.
[Graphical view]
Gene3DG3DSA:3.30.70.1230. A/G_cyclase. 2 hits.
PfamPF06327. DUF1053. 1 hit.
PF00211. Guanylate_cyc. 2 hits.
[Graphical view]
SMARTSM00044. CYCc. 2 hits.
[Graphical view]
PROSITEPS00452. GUANYLATE_CYCLASE_1. 2 hits.
PS50125. GUANYLATE_CYCLASE_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio615124.

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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: June 16, 2009
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents