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O88444

- ADCY1_MOUSE

UniProt

O88444 - ADCY1_MOUSE

Protein

Adenylate cyclase type 1

Gene

Adcy1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 2 (12 Apr 2005)
      Previous versions | rss
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    Functioni

    This is a calmodulin-sensitive adenylyl cyclase. May be involved in regulatory processes in the central nervous system. It may play a role in memory acquisition and learning. Plays a role in the regulation of the circadian rhythm of daytime contrast sensitivity probably by modulating the rhythmic synthesis of cyclic AMP in the retina.1 Publication

    Catalytic activityi

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

    Cofactori

    Binds 2 magnesium ions per subunit.By similarity

    Enzyme regulationi

    Activated by calcium/calmodulin. Inhibited by the G protein beta and gamma subunit complex By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi307 – 3071Magnesium 1PROSITE-ProRule annotation
    Metal bindingi307 – 3071Magnesium 2PROSITE-ProRule annotation
    Metal bindingi308 – 3081Magnesium 2; via carbonyl oxygenPROSITE-ProRule annotation
    Metal bindingi351 – 3511Magnesium 1PROSITE-ProRule annotation
    Metal bindingi351 – 3511Magnesium 2PROSITE-ProRule annotation

    GO - Molecular functioni

    1. adenylate cyclase activity Source: MGI
    2. ATP binding Source: UniProtKB-KW
    3. calcium- and calmodulin-responsive adenylate cyclase activity Source: Ensembl
    4. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. activation of adenylate cyclase activity Source: MGI
    2. axonogenesis Source: MGI
    3. cAMP biosynthetic process Source: MGI
    4. circadian rhythm Source: Ensembl
    5. intracellular signal transduction Source: InterPro
    6. long-term memory Source: MGI
    7. regulation of circadian rhythm Source: UniProtKB
    8. response to drug Source: Ensembl
    9. response to lithium ion Source: Ensembl

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Biological rhythms, cAMP biosynthesis

    Keywords - Ligandi

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

    Enzyme and pathway databases

    ReactomeiREACT_198242. CREB phosphorylation through the activation of Adenylate Cyclase.
    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.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Adenylate cyclase type 1 (EC:4.6.1.1)
    Alternative name(s):
    ATP pyrophosphate-lyase 1
    Adenylate cyclase type I
    Adenylyl cyclase 1
    Ca(2+)/calmodulin-activated adenylyl cyclase
    Gene namesi
    Name:Adcy1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:99677. Adcy1.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. nucleus Source: Ensembl
    3. plasma membrane Source: MGI

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Mice show a significant reduction in daytime contrast sensitivity.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11181118Adenylate cyclase type 1PRO_0000195683Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi703 – 7031N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PaxDbiO88444.
    PRIDEiO88444.

    PTM databases

    PhosphoSiteiO88444.

    Expressioni

    Inductioni

    Expression in the retina oscillates in a circadian manner.1 Publication

    Gene expression databases

    BgeeiO88444.
    CleanExiMM_ADCY1.
    GenevestigatoriO88444.

    Interactioni

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000020706.

    Structurei

    3D structure databases

    ProteinModelPortaliO88444.
    SMRiO88444. Positions 289-476, 859-1053.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 6262CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini234 – 609376CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini794 – 1118325CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei63 – 8321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei87 – 10721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei124 – 14421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei157 – 17721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei182 – 20221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei213 – 23321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei610 – 63021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei634 – 65421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei673 – 69321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei724 – 74421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei752 – 77221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei774 – 79320HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni492 – 51928Interaction with calmodulinBy similarityAdd
    BLAST
    Regioni1023 – 104624Interaction with calmodulinBy similarityAdd
    BLAST

    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.
    GeneTreeiENSGT00680000099709.
    HOGENOMiHOG000006941.
    HOVERGENiHBG050458.
    InParanoidiO88444.
    KOiK08041.
    OMAiCLPWAWS.
    OrthoDBiEOG7B8S30.
    PhylomeDBiO88444.
    TreeFamiTF313845.

    Family and domain databases

    Gene3Di3.30.70.1230. 2 hits.
    InterProiIPR001054. A/G_cyclase.
    IPR018297. A/G_cyclase_CS.
    [Graphical view]
    PfamiPF00211. 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.

    O88444-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAGAPRGQGG GGGAGEPGGA ERAAGPGGRR GFRACGEEFA CPELEALFRG     50
    YTLRLEQAAT LKALAVLSLL AGALALAELL GAPGPAPGLA KGSHPVHCIL 100
    FLALFVVTNV RSLQVSQLQQ VGQLALFFSL TFALLCCPFA LGGPARSSAG 150
    GAMGSTVAEQ GVWQLLLVTF VSYALLPVRS LLAIGFGLVV AASHLLVTAA 200
    LVPAKRPRLW RTLGANALLF FGVNMYGVFV RILTERSQRK AFLQARNCIE 250
    DRLRLEDENE KQERLLMSLL PRNVAMEMKE DFLKPPERIF HKIYIQRHDN 300
    VSILFADIVG FTGLASQCTA QELVKLLNEL FGKFDELATE NHCRRIKILG 350
    DCYYCVSGLT QPKTDHAHCC VEMGLDMIDT ITSVAEATEV DLNMRVGLHT 400
    GRVLCGVLGL RKWQYDVWSN DVTLANVMEA AGLPGKVHIT KTTLACLNGD 450
    YEVEPGHGHE RNTFLRTHNI ETFFIVPSHR RKIFPGLILS DIKPAKRMKF 500
    KTVCYLLVQL MHCRKMFKAE IPFSNVMTCE DDDKRRALRT ASEKLRNRSS 550
    FSTNVVYTTP GTRVNRYISR LLEARQTELE MADLNFFTLK YKHVEREQKY 600
    HQLQDEYFTS AVVLALILAA LFGLIYLLVI PQSVAVLLLL VFSICFLVAC 650
    TLYLHITRVQ CFPGCLTIQI RTALCVFIVV LIYSVAQGCV VGCLPWAWSS 700
    QSNSSLVVLA AGGRRTVLPA LPCESAHHAL LCCLVGTLPL AIFLRVSSLP 750
    KMILLSGLTT SYILVLELSG YTKVGGGALS GRSYEPIMAI LLFSCTLALH 800
    ARQVDVRLRL DYLWAAQAEE ERDDMERVKL DNKRILFNLL PAHVAQHFLM 850
    SNPRNMDLYY QSYSQVGVMF ASIPNFNDFY IELDGNNMGV ECLRLLNEII 900
    ADFDELMDKD FYKDLEKIKT IGSTYMAAVG LAPTAGTRAK KSISSHLCTL 950
    ADFAIDMFDV LDEINYQSYN DFVLRVGINV GPVVAGVIGA RRPQYDIWGN 1000
    TVNVASRMDS TGVQGRIQVT EEVHRLLKRC SYQFVCRGKV SVKGKGEMLT 1050
    YFLEGRTDGN SSHGRTFRLE RRMCPYGRGG GQARRPPLCP AAGPPVRPGL 1100
    PPAPTSQYLS STAAGKEA 1118
    Length:1,118
    Mass (Da):123,373
    Last modified:April 12, 2005 - v2
    Checksum:iCEFAFF3940B22277
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti147 – 1559SSAGGAMGS → ALQEAQWAR in AAC29478. (PubMed:9662407)Curated
    Sequence conflicti234 – 2341T → A in AAC29478. (PubMed:9662407)Curated
    Sequence conflicti270 – 2701L → M in AAC29478. (PubMed:9662407)Curated
    Sequence conflicti319 – 3191T → K in AAC29478. (PubMed:9662407)Curated
    Sequence conflicti466 – 4661R → K in AAC29478. (PubMed:9662407)Curated
    Sequence conflicti523 – 5231F → I in AAC29478. (PubMed:9662407)Curated
    Sequence conflicti542 – 5421S → T in AAC29478. (PubMed:9662407)Curated
    Sequence conflicti549 – 5491S → T in AAC29478. (PubMed:9662407)Curated
    Sequence conflicti570 – 5701R → L in AAC29478. (PubMed:9662407)Curated
    Sequence conflicti598 – 5981Q → R in AAC29478. (PubMed:9662407)Curated
    Sequence conflicti692 – 6921G → V in AAC29478. (PubMed:9662407)Curated
    Sequence conflicti697 – 6971A → S in AAC29478. (PubMed:9662407)Curated
    Sequence conflicti707 – 7071V → L in AAC29478. (PubMed:9662407)Curated
    Sequence conflicti713 – 7131G → C in AAC29478. (PubMed:9662407)Curated
    Sequence conflicti720 – 7212AL → GP in AAC29478. (PubMed:9662407)Curated
    Sequence conflicti774 – 7763VGG → AMGA in AAC29478. (PubMed:9662407)Curated
    Sequence conflicti867 – 8693GVM → AVL in AAC29478. (PubMed:9662407)Curated
    Sequence conflicti938 – 9381R → K in AAC29478. (PubMed:9662407)Curated
    Sequence conflicti991 – 9911R → C in AAC29478. (PubMed:9662407)Curated
    Sequence conflicti1020 – 10201T → I in AAC29478. (PubMed:9662407)Curated
    Sequence conflicti1030 – 10301C → S in AAC29478. (PubMed:9662407)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL669838 Genomic DNA. Translation: CAI25155.1.
    AF053980 mRNA. Translation: AAC29478.1.
    CCDSiCCDS24426.1.
    RefSeqiNP_033752.1. NM_009622.1.
    UniGeneiMm.259733.

    Genome annotation databases

    EnsembliENSMUST00000020706; ENSMUSP00000020706; ENSMUSG00000020431.
    GeneIDi432530.
    KEGGimmu:432530.
    UCSCiuc007hzf.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL669838 Genomic DNA. Translation: CAI25155.1 .
    AF053980 mRNA. Translation: AAC29478.1 .
    CCDSi CCDS24426.1.
    RefSeqi NP_033752.1. NM_009622.1.
    UniGenei Mm.259733.

    3D structure databases

    ProteinModelPortali O88444.
    SMRi O88444. Positions 289-476, 859-1053.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000020706.

    Chemistry

    BindingDBi O88444.

    PTM databases

    PhosphoSitei O88444.

    Proteomic databases

    PaxDbi O88444.
    PRIDEi O88444.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000020706 ; ENSMUSP00000020706 ; ENSMUSG00000020431 .
    GeneIDi 432530.
    KEGGi mmu:432530.
    UCSCi uc007hzf.1. mouse.

    Organism-specific databases

    CTDi 107.
    MGIi MGI:99677. Adcy1.

    Phylogenomic databases

    eggNOGi COG2114.
    GeneTreei ENSGT00680000099709.
    HOGENOMi HOG000006941.
    HOVERGENi HBG050458.
    InParanoidi O88444.
    KOi K08041.
    OMAi CLPWAWS.
    OrthoDBi EOG7B8S30.
    PhylomeDBi O88444.
    TreeFami TF313845.

    Enzyme and pathway databases

    Reactomei REACT_198242. CREB phosphorylation through the activation of Adenylate Cyclase.
    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

    ChiTaRSi ADCY1. mouse.
    NextBioi 407738.
    PROi O88444.
    SOURCEi Search...

    Gene expression databases

    Bgeei O88444.
    CleanExi MM_ADCY1.
    Genevestigatori O88444.

    Family and domain databases

    Gene3Di 3.30.70.1230. 2 hits.
    InterProi IPR001054. A/G_cyclase.
    IPR018297. A/G_cyclase_CS.
    [Graphical view ]
    Pfami 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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    2. "Loss of adenylyl cyclase I activity disrupts patterning of mouse somatosensory cortex."
      Abdel-Majid R.M., Leong W.L., Schalkwyk L.C., Smallman D.S., Wong S.T., Storm D.R., Fine A., Dobson M.J., Guernsey D.L., Neumann P.E.
      Nat. Genet. 19:289-291(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 100-1050.
      Strain: C57BL/6J.
      Tissue: Brain.
    3. "Circadian rhythm of contrast sensitivity is regulated by a dopamine-neuronal PAS-domain protein 2-adenylyl cyclase 1 signaling pathway in retinal ganglion cells."
      Hwang C.K., Chaurasia S.S., Jackson C.R., Chan G.C., Storm D.R., Iuvone P.M.
      J. Neurosci. 33:14989-14997(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION, DISRUPTION PHENOTYPE.

    Entry informationi

    Entry nameiADCY1_MOUSE
    AccessioniPrimary (citable) accession number: O88444
    Secondary accession number(s): Q5SS89
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 21, 2004
    Last sequence update: April 12, 2005
    Last modified: October 1, 2014
    This is version 112 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