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P84309

- ADCY5_MOUSE

UniProt

P84309 - ADCY5_MOUSE

Protein

Adenylate cyclase type 5

Gene

Adcy5

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 2 (09 Jan 2007)
      Previous versions | rss
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    Functioni

    This is a membrane-bound, calcium-inhibitable adenylyl cyclase.Curated

    Catalytic activityi

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

    Cofactori

    Binds 2 magnesium ions per subunit.By similarity

    Enzyme regulationi

    Inhibition by calcium in the submicromolar concentration range. Phosphorylation by RAF1 results in its activation.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi475 – 4751Magnesium 1PROSITE-ProRule annotation
    Metal bindingi475 – 4751Magnesium 2PROSITE-ProRule annotation
    Metal bindingi476 – 4761Magnesium 2; via carbonyl oxygenPROSITE-ProRule annotation

    GO - Molecular functioni

    1. adenylate cyclase activity Source: MGI
    2. adenylate cyclase binding Source: BHF-UCL
    3. ATP binding Source: UniProtKB-KW
    4. metal ion binding Source: UniProtKB-KW
    5. protein binding Source: UniProtKB
    6. protein heterodimerization activity Source: BHF-UCL

    GO - Biological processi

    1. adenosine receptor signaling pathway Source: MGI
    2. adenylate cyclase-activating dopamine receptor signaling pathway Source: MGI
    3. adenylate cyclase-activating G-protein coupled receptor signaling pathway Source: MGI
    4. adenylate cyclase-inhibiting dopamine receptor signaling pathway Source: MGI
    5. cAMP biosynthetic process Source: MGI
    6. intracellular signal transduction Source: InterPro
    7. locomotory behavior Source: MGI
    8. neuromuscular process controlling balance Source: MGI

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    cAMP biosynthesis

    Keywords - Ligandi

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

    Enzyme and pathway databases

    ReactomeiREACT_210399. Glucagon signaling in metabolic regulation.
    REACT_213947. Regulation of water balance by renal Aquaporins.
    REACT_220108. PKA activation.
    REACT_220758. PKA activation in glucagon signalling.
    REACT_222824. Adenylate cyclase inhibitory pathway.
    REACT_224974. Adenylate cyclase activating pathway.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Adenylate cyclase type 5 (EC:4.6.1.1)
    Alternative name(s):
    ATP pyrophosphate-lyase 5
    Adenylate cyclase type V
    Adenylyl cyclase 5
    Gene namesi
    Name:Adcy5Imported
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 16

    Organism-specific databases

    MGIiMGI:99673. Adcy5.

    Subcellular locationi

    Membrane By similarity; Multi-pass membrane protein By similarity. Cell projectioncilium 1 Publication

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. membrane Source: MGI
    3. plasma membrane Source: BHF-UCL
    4. primary cilium Source: UniProtKB

    Keywords - Cellular componenti

    Cell projection, Cilium, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12621262Adenylate cyclase type 5PRO_0000195695Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi239 – 2391N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi834 – 8341N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi871 – 8711N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi888 – 8881N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi973 – 9731N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    Phosphorylated by RAF1.By similarity

    Keywords - PTMi

    Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiP84309.
    PRIDEiP84309.

    PTM databases

    PhosphoSiteiP84309.

    Expressioni

    Gene expression databases

    BgeeiP84309.
    CleanExiMM_ADCY5.
    GenevestigatoriP84309.

    Interactioni

    Subunit structurei

    Part of a complex containing AKAP5, ADCY6, PDE4C and PKD2. Interacts with RAF1 By similarity.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliP84309.
    SMRiP84309. Positions 455-644, 1065-1256.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 196196CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini396 – 763368CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini858 – 91053ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1006 – 1262257CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei197 – 21721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei243 – 26321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei269 – 28921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei300 – 32021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei326 – 34621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei375 – 39521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei764 – 78421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei790 – 81021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei837 – 85721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei911 – 93121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei936 – 95621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei985 – 100521HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini470 – 597128Guanylate cyclase 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini1072 – 1211140Guanylate cyclase 2PROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili1019 – 104527Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi64 – 674Poly-Gln
    Compositional biasi141 – 1477Poly-Ala

    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

    Coiled coil, Repeat, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG2114.
    GeneTreeiENSGT00680000099709.
    HOGENOMiHOG000006941.
    HOVERGENiHBG050458.
    KOiK08045.
    OMAiVRSKMNS.
    OrthoDBiEOG7B8S30.
    PhylomeDBiP84309.
    TreeFamiTF313845.

    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P84309-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MSGSKSVSPP GYAAQTAASP APRGGPEHRA AWGEADSRAN GYPHAPGGST     50
    RGSTKRSGGA VTPQQQQRLA SRWRGGDDDE DPPLSGDDPL AGGFGFSFRS 100
    KSAWQERGGD DGGRGSRRQR RGAAGGGSTR APPAGGSGSS AAAAAAAGGT 150
    EVRPRSVELG LEERRGKGRA AEELEPGTGI VEDGDGSEDG GSSVASGSGT 200
    GAVLSLGACC LALLQIFRSK KFPSDKLERL YQRYFFRLNQ SSLTMLMAVL 250
    VLVCLVMLAF HAARPPLQIA YLAVLAAAVG VILIMAVLCN RAAFHQDHMG 300
    LACYALIAVV LAVQVVGLLL PQPRSASEGI WWTVFFIYTI YTLLPVRMRA 350
    AVLSGVLLSA LHLAISLHTN SQDQFLLKQL VSNVLIFSCT NIVGVCTHYP 400
    AEVSQRQAFQ ETRECIQARL HSQRENQQQE RLLLSVLPRH VAMEMKADIN 450
    AKQEDMMFHK IYIQKHDNVS ILFADIEGFT SLASQCTAQE LVMTLNELFA 500
    RFDKLAAENH CLRIKILGDC YYCVSGLPEA RADHAHCCVE MGMDMIEAIS 550
    LVREVTGVNV NMRVGIHSGR VHCGVLGLRK WQFDVWSNDV TLANHMEAGG 600
    KAGRIHITKA TLNYLNGDYE VEPGCGGDRN AYLKEHSIET FLILSCTQKR 650
    KEEKAMIAKM NRQRTNSIGH NPPHWGAERP FYNHLGGNQV SKEMKRMGFE 700
    DPKDKNAQES ANPEDEVDEF LGRAIDARSI DRLRSEHVRK FLLTFREPDL 750
    EKKYSKQVDD RFGAYVACAS LVFLFICFVQ ITIVPHSLFM LSFYLSCFLL 800
    LALVVFVSVI YACVKLFPTP LQTLSRKIVR SKKNSTLVGV FTITLVFLSA 850
    FVNMFMCNSK NLVGCLAEEH NITVNQVNAC HVMESAFNYS LGDEQGFCGS 900
    PQPNCNFPEY FTYSVLLSLL ACSVFLQISC IGKLVLMLAI EFIYVLIVEV 950
    PGVTLFDNAD LLVTANAIDF SNNGTSQCPE HATKVALKVV TPIIISVFVL 1000
    ALYLHAQQVE STARLDFLWK LQATEEKEEM EELQAYNRRL LHNILPKDVA 1050
    AHFLARERRN DELYYQSCEC VAVMFASIAN FSEFYVELEA NNEGVECLRL 1100
    LNEIIADFDE IISEDRFRQL EKIKTIGSTY MAASGLNDST YDKAGKTHIK 1150
    AIADFAMKLM DQMKYINEHS FNNFQMKIGL NIGPVVAGVI GARKPQYDIW 1200
    GNTVNVASRM DSTGVPDRIQ VTTDMYQVLA ANTYQLECRG VVKVKGKGEM 1250
    MTYFLNGGPP LS 1262
    Length:1,262
    Mass (Da):139,122
    Last modified:January 9, 2007 - v2
    Checksum:i342966E7CA67E28D
    GO
    Isoform 2 (identifier: P84309-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1259-1262: PPLS → LGHDGVVGKL...GSEQKKIFIK

    Note: No experimental confirmation available.

    Show »
    Length:1,348
    Mass (Da):148,383
    Checksum:iB4997E3A2BC14305
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti25 – 251G → S in AAH90846. (PubMed:15489334)Curated
    Sequence conflicti686 – 6861G → D in BAE28048. (PubMed:16141072)Curated
    Sequence conflicti924 – 9241V → M in AAH90846. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1259 – 12624PPLS → LGHDGVVGKLKAGLGVSMEL KGLLFHCGEVTPPHNVWGTG TGRRVACAILSPHLHAQRQC PVRETGLLTREARGHQARSS GSEQKKIFIK in isoform 2. 1 PublicationVSP_022224

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK147649 mRNA. Translation: BAE28048.1.
    AK160942 mRNA. Translation: BAE36104.1.
    BC035550 mRNA. No translation available.
    BC090846 mRNA. Translation: AAH90846.1.
    CCDSiCCDS37322.1. [P84309-1]
    RefSeqiNP_001012783.3. NM_001012765.4. [P84309-1]
    UniGeneiMm.41137.

    Genome annotation databases

    EnsembliENSMUST00000114913; ENSMUSP00000110563; ENSMUSG00000022840. [P84309-1]
    GeneIDi224129.
    KEGGimmu:224129.
    UCSCiuc007zbj.1. mouse. [P84309-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK147649 mRNA. Translation: BAE28048.1 .
    AK160942 mRNA. Translation: BAE36104.1 .
    BC035550 mRNA. No translation available.
    BC090846 mRNA. Translation: AAH90846.1 .
    CCDSi CCDS37322.1. [P84309-1 ]
    RefSeqi NP_001012783.3. NM_001012765.4. [P84309-1 ]
    UniGenei Mm.41137.

    3D structure databases

    ProteinModelPortali P84309.
    SMRi P84309. Positions 455-644, 1065-1256.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    BindingDBi P84309.

    PTM databases

    PhosphoSitei P84309.

    Proteomic databases

    PaxDbi P84309.
    PRIDEi P84309.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000114913 ; ENSMUSP00000110563 ; ENSMUSG00000022840 . [P84309-1 ]
    GeneIDi 224129.
    KEGGi mmu:224129.
    UCSCi uc007zbj.1. mouse. [P84309-1 ]

    Organism-specific databases

    CTDi 111.
    MGIi MGI:99673. Adcy5.

    Phylogenomic databases

    eggNOGi COG2114.
    GeneTreei ENSGT00680000099709.
    HOGENOMi HOG000006941.
    HOVERGENi HBG050458.
    KOi K08045.
    OMAi VRSKMNS.
    OrthoDBi EOG7B8S30.
    PhylomeDBi P84309.
    TreeFami TF313845.

    Enzyme and pathway databases

    Reactomei REACT_210399. Glucagon signaling in metabolic regulation.
    REACT_213947. Regulation of water balance by renal Aquaporins.
    REACT_220108. PKA activation.
    REACT_220758. PKA activation in glucagon signalling.
    REACT_222824. Adenylate cyclase inhibitory pathway.
    REACT_224974. Adenylate cyclase activating pathway.

    Miscellaneous databases

    NextBioi 377103.
    PROi P84309.
    SOURCEi Search...

    Gene expression databases

    Bgeei P84309.
    CleanExi MM_ADCY5.
    Genevestigatori P84309.

    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. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Strain: C57BL/6J.
      Tissue: Head.
    2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Strain: C57BL/61 Publication.
      Tissue: Brain and Retina1 Publication.
    3. "Polycystin-2 and phosphodiesterase 4C are components of a ciliary A-kinase anchoring protein complex that is disrupted in cystic kidney diseases."
      Choi Y.H., Suzuki A., Hajarnis S., Ma Z., Chapin H.C., Caplan M.J., Pontoglio M., Somlo S., Igarashi P.
      Proc. Natl. Acad. Sci. U.S.A. 108:10679-10684(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH AKAP5; ADCY6; PDE4C AND PKD2.

    Entry informationi

    Entry nameiADCY5_MOUSE
    AccessioniPrimary (citable) accession number: P84309
    Secondary accession number(s): Q3TU67, Q3UH09, Q5BL06
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 21, 2004
    Last sequence update: January 9, 2007
    Last modified: October 1, 2014
    This is version 102 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3