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P14100

- PDE1A_BOVIN

UniProt

P14100 - PDE1A_BOVIN

Protein

Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1A

Gene

PDE1A

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Cyclic nucleotide phosphodiesterase with a dual-specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes. Has a higher affinity for cGMP than for cAMP By similarity.By similarity

    Catalytic activityi

    Nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate.

    Cofactori

    Binds 2 divalent metal cations per subunit. Site 1 may preferentially bind zinc ions, while site 2 has a preference for magnesium and/or manganese ions By similarity.By similarity

    Enzyme regulationi

    Type I PDE are activated by the binding of calmodulin in the presence of Ca2+.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei219 – 2191Proton donorBy similarity
    Metal bindingi223 – 2231Divalent metal cation 1By similarity
    Metal bindingi259 – 2591Divalent metal cation 1By similarity
    Metal bindingi260 – 2601Divalent metal cation 1By similarity
    Metal bindingi260 – 2601Divalent metal cation 2By similarity
    Metal bindingi366 – 3661Divalent metal cation 1By similarity

    GO - Molecular functioni

    1. calcium- and calmodulin-regulated 3',5'-cyclic-GMP phosphodiesterase activity Source: MGI
    2. calmodulin-dependent cyclic-nucleotide phosphodiesterase activity Source: MGI
    3. metal ion binding Source: UniProtKB-KW
    4. protein binding Source: IntAct

    GO - Biological processi

    1. metabolic process Source: GOC
    2. signal transduction Source: InterPro

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Calmodulin-binding, cAMP, cGMP, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_205403. cGMP effects.
    REACT_206547. G alpha (s) signalling events.
    REACT_212942. Cam-PDE 1 activation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1A (EC:3.1.4.17)
    Short name:
    Cam-PDE 1A
    Alternative name(s):
    61 kDa Cam-PDE
    Gene namesi
    Name:PDE1A
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Chromosome 2

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed
    Chaini2 – 530529Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1APRO_0000198784Add
    BLAST

    Proteomic databases

    PRIDEiP14100.

    Interactioni

    Subunit structurei

    Homodimer.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HpcaP840762EBI-907809,EBI-908193From a different organism.
    NCALDP616022EBI-907809,EBI-908133
    Ncs1P621682EBI-907809,EBI-907774From a different organism.

    Protein-protein interaction databases

    BioGridi159260. 2 interactions.
    IntActiP14100. 3 interactions.
    MINTiMINT-1339090.

    Structurei

    3D structure databases

    ProteinModelPortaliP14100.
    SMRiP14100. Positions 142-506.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni24 – 4421Calmodulin-bindingAdd
    BLAST
    Regioni193 – 501309CatalyticBy similarityAdd
    BLAST

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG139098.
    GeneTreeiENSGT00660000095451.
    HOGENOMiHOG000231888.
    HOVERGENiHBG056120.
    InParanoidiP14100.
    KOiK13755.
    OMAiQEEEMNV.
    OrthoDBiEOG7X9G6J.
    TreeFamiTF314638.

    Family and domain databases

    Gene3Di1.10.1300.10. 2 hits.
    InterProiIPR003607. HD/PDEase_dom.
    IPR023088. PDEase.
    IPR002073. PDEase_catalytic_dom.
    IPR023174. PDEase_CS.
    IPR013706. PDEase_N.
    [Graphical view]
    PfamiPF00233. PDEase_I. 1 hit.
    PF08499. PDEase_I_N. 1 hit.
    [Graphical view]
    PRINTSiPR00387. PDIESTERASE1.
    SMARTiSM00471. HDc. 1 hit.
    [Graphical view]
    PROSITEiPS00126. PDEASE_I. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 2 (identifier: P14100-1) [UniParc]FASTAAdd to Basket

    Also known as: PDE1A2

    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

    MGSTATETEE LENTTFKYLI GEQTEKMWQR LKGILRCLVK QLEKGDVNVI    50
    DLKKNIEYAA SVLEAVYIDE TRRLLDTDDE LSDIQSDSVP SEVRDWLAST 100
    FTRKMGMMKK KSEEKPRFRS IVHVVQAGIF VERMYRKSYH MVGLAYPEAV 150
    IVTLKDVDKW SFDVFALNEA SGEHSLKFMI YELFTRYDLI NRFKIPVSCL 200
    IAFAEALEVG YSKYKNPYHN LIHAADVTQT VHYIMLHTGI MHWLTELEIL 250
    AMVFAAAIHD YEHTGTTNNF HIQTRSDVAI LYNDRSVLEN HHVSAAYRLM 300
    QEEEMNVLIN LSKDDWRDLR NLVIEMVLST DMSGHFQQIK NIRNSLQQPE 350
    GLDKAKTMSL ILHAADISHP AKSWKLHHRW TMALMEEFFL QGDKEAELGL 400
    PFSPLCDRKS TMVAQSQIGF IDFIVEPTFS LLTDSTEKII IPLIEEDSKT 450
    KTPSYGASRR SNMKGTTNDG TYSPDYSLAS VDLKSFKNSL VDIIQQNKER 500
    WKELAAQGEP DPHKNSDLVN AEEKHAETHS 530
    Length:530
    Mass (Da):60,843
    Last modified:January 23, 2007 - v3
    Checksum:i24CF83E5211AE06F
    GO
    Isoform 1 (identifier: P14100-2) [UniParc]FASTAAdd to Basket

    Also known as: PDE1A1

    The sequence of this isoform differs from the canonical sequence as follows:
         1-34: MGSTATETEELENTTFKYLIGEQTEKMWQRLKGI → MDDHVTIRRKHLQRPIFR

    Show »
    Length:514
    Mass (Da):59,198
    Checksum:i7CE7D8A1C366CCE5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti237 – 2371H → G AA sequence (PubMed:3025833)Curated
    Sequence conflicti321 – 3211N → W AA sequence (PubMed:3025833)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 3434MGSTA…RLKGI → MDDHVTIRRKHLQRPIFR in isoform 1. 2 PublicationsVSP_004546Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M90358 mRNA. Translation: AAA74560.1.
    L34069 mRNA. Translation: AAA92555.1.
    BC123449 mRNA. Translation: AAI23450.1.
    PIRiA45334.
    RefSeqiNP_776839.1. NM_174414.3. [P14100-2]
    XP_005202315.1. XM_005202258.1. [P14100-1]
    UniGeneiBt.512.

    Genome annotation databases

    EnsembliENSBTAT00000016060; ENSBTAP00000016060; ENSBTAG00000012100. [P14100-2]
    ENSBTAT00000052318; ENSBTAP00000051204; ENSBTAG00000012100. [P14100-1]
    GeneIDi281969.
    KEGGibta:281969.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M90358 mRNA. Translation: AAA74560.1 .
    L34069 mRNA. Translation: AAA92555.1 .
    BC123449 mRNA. Translation: AAI23450.1 .
    PIRi A45334.
    RefSeqi NP_776839.1. NM_174414.3. [P14100-2 ]
    XP_005202315.1. XM_005202258.1. [P14100-1 ]
    UniGenei Bt.512.

    3D structure databases

    ProteinModelPortali P14100.
    SMRi P14100. Positions 142-506.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 159260. 2 interactions.
    IntActi P14100. 3 interactions.
    MINTi MINT-1339090.

    Chemistry

    BindingDBi P14100.
    ChEMBLi CHEMBL3774.

    Proteomic databases

    PRIDEi P14100.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSBTAT00000016060 ; ENSBTAP00000016060 ; ENSBTAG00000012100 . [P14100-2 ]
    ENSBTAT00000052318 ; ENSBTAP00000051204 ; ENSBTAG00000012100 . [P14100-1 ]
    GeneIDi 281969.
    KEGGi bta:281969.

    Organism-specific databases

    CTDi 5136.

    Phylogenomic databases

    eggNOGi NOG139098.
    GeneTreei ENSGT00660000095451.
    HOGENOMi HOG000231888.
    HOVERGENi HBG056120.
    InParanoidi P14100.
    KOi K13755.
    OMAi QEEEMNV.
    OrthoDBi EOG7X9G6J.
    TreeFami TF314638.

    Enzyme and pathway databases

    Reactomei REACT_205403. cGMP effects.
    REACT_206547. G alpha (s) signalling events.
    REACT_212942. Cam-PDE 1 activation.

    Miscellaneous databases

    NextBioi 20805840.

    Family and domain databases

    Gene3Di 1.10.1300.10. 2 hits.
    InterProi IPR003607. HD/PDEase_dom.
    IPR023088. PDEase.
    IPR002073. PDEase_catalytic_dom.
    IPR023174. PDEase_CS.
    IPR013706. PDEase_N.
    [Graphical view ]
    Pfami PF00233. PDEase_I. 1 hit.
    PF08499. PDEase_I_N. 1 hit.
    [Graphical view ]
    PRINTSi PR00387. PDIESTERASE1.
    SMARTi SM00471. HDc. 1 hit.
    [Graphical view ]
    PROSITEi PS00126. PDEASE_I. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of a cDNA encoding the '61-kDa' calmodulin-stimulated cyclic nucleotide phosphodiesterase. Tissue-specific expression of structurally related isoforms."
      Sonnenburg W.K., Seger D., Beavo J.A.
      J. Biol. Chem. 268:645-652(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    2. "Identification of inhibitory and calmodulin-binding domains of the PDE1A1 and PDE1A2 calmodulin-stimulated cyclic nucleotide phosphodiesterases."
      Sonnenburg W.K., Seger D., Kwak K.S., Huang J., Charbonneau H., Beavo J.A.
      J. Biol. Chem. 270:30989-31000(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Lung.
    3. NIH - Mammalian Gene Collection (MGC) project
      Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Strain: Hereford.
      Tissue: Hippocampus.
    4. "Evidence for domain organization within the 61-kDa calmodulin-dependent cyclic nucleotide phosphodiesterase from bovine brain."
      Charbonneau H., Kumar S., Novack J.P., Blumenthal D.K., Griffin P.R., Shabanowitz J., Hunt D.F., Beavo J.A., Walsh K.A.
      Biochemistry 30:7931-7940(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-530 (ISOFORM 2).
      Tissue: Brain.
    5. "Identification of a conserved domain among cyclic nucleotide phosphodiesterases from diverse species."
      Charbonneau H., Beier N., Walsh K.A., Beavo J.A.
      Proc. Natl. Acad. Sci. U.S.A. 83:9308-9312(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 194-427.
      Tissue: Brain.

    Entry informationi

    Entry nameiPDE1A_BOVIN
    AccessioniPrimary (citable) accession number: P14100
    Secondary accession number(s): Q08E30, Q28063
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 118 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3