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P26769

- ADCY2_RAT

UniProt

P26769 - ADCY2_RAT

Protein

Adenylate cyclase type 2

Gene

Adcy2

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 1 (01 Aug 1992)
      Previous versions | rss
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    Functioni

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

    Catalytic activityi

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

    Cofactori

    Binds 2 magnesium ions per subunit.By similarity

    Enzyme regulationi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi294 – 2941Magnesium 1PROSITE-ProRule annotation
    Metal bindingi294 – 2941Magnesium 2PROSITE-ProRule annotation
    Metal bindingi295 – 2951Magnesium 2; via carbonyl oxygenPROSITE-ProRule annotation
    Metal bindingi338 – 3381Magnesium 1PROSITE-ProRule annotation
    Metal bindingi338 – 3381Magnesium 2PROSITE-ProRule annotation

    GO - Molecular functioni

    1. adenylate cyclase activity Source: BHF-UCL
    2. adenylate cyclase binding Source: BHF-UCL
    3. ATP binding Source: UniProtKB-KW
    4. calcium- and calmodulin-responsive adenylate cyclase activity Source: RGD
    5. G-protein beta/gamma-subunit complex binding Source: RGD
    6. metal ion binding Source: UniProtKB-KW
    7. protein binding Source: IntAct
    8. protein heterodimerization activity Source: BHF-UCL

    GO - Biological processi

    1. adenylate cyclase-modulating G-protein coupled receptor signaling pathway Source: BHF-UCL
    2. cAMP biosynthetic process Source: BHF-UCL
    3. intracellular signal transduction Source: InterPro

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    cAMP biosynthesis

    Keywords - Ligandi

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

    Enzyme and pathway databases

    BRENDAi4.6.1.1. 5301.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Adenylate cyclase type 2 (EC:4.6.1.1)
    Alternative name(s):
    ATP pyrophosphate-lyase 2
    Adenylate cyclase type II
    Adenylyl cyclase 2
    Gene namesi
    Name:Adcy2
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi619965. Adcy2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: Ensembl
    2. dendrite Source: UniProtKB
    3. integral component of membrane Source: UniProtKB-KW
    4. intracellular Source: BHF-UCL
    5. membrane Source: UniProtKB
    6. membrane raft Source: BHF-UCL
    7. plasma membrane Source: BHF-UCL
    8. protein complex Source: RGD

    Keywords - Cellular componenti

    Membrane

    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
    Glycosylationi712 – 7121N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi717 – 7171N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    Phosphorylated by RAF1.By similarity

    Keywords - PTMi

    Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiP26769.
    PRIDEiP26769.

    PTM databases

    PhosphoSiteiP26769.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    ArrayExpressiP26769.
    GenevestigatoriP26769.

    Interactioni

    Subunit structurei

    Interacts with RAF1.By similarity

    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.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 4444CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini207 – 600394CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini821 – 1090270CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei45 – 6521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei75 – 9521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei107 – 12721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei132 – 15221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei157 – 17721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei186 – 20621HelicalSequence 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

    Family & Domainsi

    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

    eggNOGiCOG2114.
    HOGENOMiHOG000006941.
    HOVERGENiHBG050458.
    InParanoidiP26769.
    KOiK08042.
    PhylomeDBiP26769.

    Family and domain databases

    Gene3Di3.30.70.1230. 2 hits.
    InterProiIPR001054. A/G_cyclase.
    IPR018297. A/G_cyclase_CS.
    IPR009398. Adenylate_cyclase-like.
    [Graphical view]
    PfamiPF06327. DUF1053. 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.

    P26769-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRRRRYLRDR AEAAAAAAAG GGEGLQRSRD WLYESYYCMS QQHPLIVFLL     50
    LIVMGACLAL LAVFFALGLE VEDHVAFLIT VPTALAIFFA IFILVCIESV 100
    FKKLLRVFSL VIWICLVAMG YLFMCFGGTV SAWDQVSFFL FIIFVVYTML 150
    PFNMRDAIIA SILTSSSHTI VLSVYLSATP GAKEHLFWQI LANVIIFICG 200
    NLAGAYHKHL MELALQQTYR DTCNCIKSRI KLEFEKRQQE RLLLSLLPAH 250
    IAMEMKAEII QRLQGPKAGQ MENTNNFHNL YVKRHTNVSI LYADIVGFTR 300
    LASDCSPGEL VHMLNELFGK FDQIAKENEC MRIKILGDCY YCVSGLPISL 350
    PNHAKNCVKM GLDMCEAIKK VRDATGVDIN MRVGVHSGNV LCGVIGLQKW 400
    QYDVWSHDVT LANHMEAGGV PGRVHISSVT LEHLNGAYKV EEGDGEIRDP 450
    YLKQHLVKTY FVINPKGERR SPQHLFRPRH TLDGAKMRAS VRMTRYLESW 500
    GAAKPFAHLH HRDSMTTENG KISTTDVPMG QHNFQNRTLR TKSQKKRFEE 550
    ELNERMIQAI DGINAQKQWL KSEDIQRISL LFYNKNIEKE YRATALPAFK 600
    YYVTCACLIF LCIFIVQILV LPKTSILGFS FGAAFLSLIF ILFVCFAGQL 650
    LQCSKKASTS LMWLLKSSGI IANRPWPRIS LTIVTTAIIL TMAVFNMFFL 700
    SNSEETTLPT ANTSNANVSV PDNQASILHA RNLFFLPYFI YSCILGLISC 750
    SVFLRVNYEL KMLIMMVALV GYNTILLHTH AHVLDAYSQV LFQRPGIWKD 800
    LKTMGSVSLS IFFITLLVLG RQSEYYCRLD FLWKNKFKKE REEIETMENL 850
    NRVLLENVLP AHVAEHFLAR SLKNEELYHQ SYDCVCVMFA SIPDFKEFYT 900
    ESDVNKEGLE CLRLLNEIIA DFDDLLSKPK FSGVEKIKTI GSTYMAATGL 950
    SAIPSQEHAQ EPERQYMHIG TMVEFAYALV GKLDAINKHS FNDFKLRVGI 1000
    NHGPVIAGVI GAQKPQYDIW GNTVNVASRM DSTGVLDKIQ VTEETSLILQ 1050
    TLGYTCTCRG IINVKGKGDL KTYFVNTEMS RSLSQSNLAS 1090
    Length:1,090
    Mass (Da):123,316
    Last modified:August 1, 1992 - v1
    Checksum:i935CE44DF73199B3
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M80550 mRNA. Translation: AAA40682.1 .
    PIRi A41541.
    RefSeqi NP_112269.1. NM_031007.1.
    UniGenei Rn.10731.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AB8 X-ray 2.20 A/B 871-1090 [» ]
    1AZS X-ray 2.30 B 870-1081 [» ]
    1CJK X-ray 3.00 B 870-1081 [» ]
    1CJT X-ray 2.80 B 870-1081 [» ]
    1CJU X-ray 2.80 B 870-1081 [» ]
    1CJV X-ray 3.00 B 870-1081 [» ]
    1CS4 X-ray 2.50 B 870-1081 [» ]
    1CUL X-ray 2.40 B 874-1081 [» ]
    1TL7 X-ray 2.80 B 870-1081 [» ]
    1U0H X-ray 2.90 B 870-1081 [» ]
    2GVD X-ray 2.90 B 870-1081 [» ]
    2GVZ X-ray 3.27 B 870-1081 [» ]
    3C14 X-ray 2.68 B 870-1081 [» ]
    3C15 X-ray 2.78 B 870-1081 [» ]
    3C16 X-ray 2.87 B 870-1081 [» ]
    3G82 X-ray 3.11 B 870-1081 [» ]
    3MAA X-ray 3.00 B 870-1081 [» ]
    ProteinModelPortali P26769.
    SMRi P26769. Positions 277-463, 878-1077.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 249536. 1 interaction.
    DIPi DIP-164N.
    IntActi P26769. 7 interactions.
    MINTi MINT-8041796.
    STRINGi 10116.ENSRNOP00000038994.

    Chemistry

    BindingDBi P26769.
    ChEMBLi CHEMBL2958.

    PTM databases

    PhosphoSitei P26769.

    Proteomic databases

    PaxDbi P26769.
    PRIDEi P26769.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 81636.
    KEGGi rno:81636.
    UCSCi RGD:619965. rat.

    Organism-specific databases

    CTDi 108.
    RGDi 619965. Adcy2.

    Phylogenomic databases

    eggNOGi COG2114.
    HOGENOMi HOG000006941.
    HOVERGENi HBG050458.
    InParanoidi P26769.
    KOi K08042.
    PhylomeDBi P26769.

    Enzyme and pathway databases

    BRENDAi 4.6.1.1. 5301.

    Miscellaneous databases

    EvolutionaryTracei P26769.
    NextBioi 615124.

    Gene expression databases

    ArrayExpressi P26769.
    Genevestigatori P26769.

    Family and domain databases

    Gene3Di 3.30.70.1230. 2 hits.
    InterProi IPR001054. A/G_cyclase.
    IPR018297. A/G_cyclase_CS.
    IPR009398. Adenylate_cyclase-like.
    [Graphical view ]
    Pfami PF06327. DUF1053. 1 hit.
    PF00211. Guanylate_cyc. 2 hits.
    [Graphical view ]
    SMARTi SM00044. CYCc. 2 hits.
    [Graphical view ]
    SUPFAMi SSF55073. SSF55073. 2 hits.
    PROSITEi PS00452. GUANYLATE_CYCLASE_1. 2 hits.
    PS50125. GUANYLATE_CYCLASE_2. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 870-1081 OF COMPLEX WITH G(S)-ALPHA.

    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: October 1, 2014
    This is version 130 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