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P14100 (PDE1A_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1A

Short name=Cam-PDE 1A
EC=3.1.4.17
Alternative name(s):
61 kDa Cam-PDE
Gene names
Name:PDE1A
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length530 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Catalytic activity

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

Cofactor

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.

Enzyme regulation

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

Subunit structure

Homodimer.

Sequence similarities

Belongs to the cyclic nucleotide phosphodiesterase family. PDE1 subfamily.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

HpcaP840762EBI-907809,EBI-908193From a different organism.
NCALDP616022EBI-907809,EBI-908133
Ncs1P621682EBI-907809,EBI-907774From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 2 (identifier: P14100-1)

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.
Isoform 1 (identifier: P14100-2)

Also known as: PDE1A1;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 530529Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1A
PRO_0000198784

Regions

Region24 – 4421Calmodulin-binding
Region193 – 501309Catalytic By similarity

Sites

Active site2191Proton donor By similarity
Metal binding2231Divalent metal cation 1 By similarity
Metal binding2591Divalent metal cation 1 By similarity
Metal binding2601Divalent metal cation 1 By similarity
Metal binding2601Divalent metal cation 2 By similarity
Metal binding3661Divalent metal cation 1 By similarity

Natural variations

Alternative sequence1 – 3434MGSTA…RLKGI → MDDHVTIRRKHLQRPIFR in isoform 1.
VSP_004546

Experimental info

Sequence conflict2371H → G AA sequence Ref.5
Sequence conflict3211N → W AA sequence Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 2 (PDE1A2) [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 24CF83E5211AE06F

FASTA53060,843
        10         20         30         40         50         60 
MGSTATETEE LENTTFKYLI GEQTEKMWQR LKGILRCLVK QLEKGDVNVI DLKKNIEYAA 

        70         80         90        100        110        120 
SVLEAVYIDE TRRLLDTDDE LSDIQSDSVP SEVRDWLAST FTRKMGMMKK KSEEKPRFRS 

       130        140        150        160        170        180 
IVHVVQAGIF VERMYRKSYH MVGLAYPEAV IVTLKDVDKW SFDVFALNEA SGEHSLKFMI 

       190        200        210        220        230        240 
YELFTRYDLI NRFKIPVSCL IAFAEALEVG YSKYKNPYHN LIHAADVTQT VHYIMLHTGI 

       250        260        270        280        290        300 
MHWLTELEIL AMVFAAAIHD YEHTGTTNNF HIQTRSDVAI LYNDRSVLEN HHVSAAYRLM 

       310        320        330        340        350        360 
QEEEMNVLIN LSKDDWRDLR NLVIEMVLST DMSGHFQQIK NIRNSLQQPE GLDKAKTMSL 

       370        380        390        400        410        420 
ILHAADISHP AKSWKLHHRW TMALMEEFFL QGDKEAELGL PFSPLCDRKS TMVAQSQIGF 

       430        440        450        460        470        480 
IDFIVEPTFS LLTDSTEKII IPLIEEDSKT KTPSYGASRR SNMKGTTNDG TYSPDYSLAS 

       490        500        510        520        530 
VDLKSFKNSL VDIIQQNKER WKELAAQGEP DPHKNSDLVN AEEKHAETHS 

« Hide

Isoform 1 (PDE1A1) [UniParc].

Checksum: 7CE7D8A1C366CCE5
Show »

FASTA51459,198

References

« Hide 'large scale' references
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M90358 mRNA. Translation: AAA74560.1.
L34069 mRNA. Translation: AAA92555.1.
BC123449 mRNA. Translation: AAI23450.1.
PIRA45334.
RefSeqNP_776839.1. NM_174414.3.
XP_005202315.1. XM_005202258.1.
UniGeneBt.512.

3D structure databases

ProteinModelPortalP14100.
SMRP14100. Positions 142-506.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid159260. 2 interactions.
IntActP14100. 3 interactions.
MINTMINT-1339090.

Chemistry

BindingDBP14100.
ChEMBLCHEMBL2111408.

Proteomic databases

PRIDEP14100.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000016060; ENSBTAP00000016060; ENSBTAG00000012100. [P14100-2]
ENSBTAT00000052318; ENSBTAP00000051204; ENSBTAG00000012100. [P14100-1]
GeneID281969.
KEGGbta:281969.

Organism-specific databases

CTD5136.

Phylogenomic databases

eggNOGNOG139098.
GeneTreeENSGT00660000095451.
HOGENOMHOG000231888.
HOVERGENHBG056120.
InParanoidP14100.
KOK13755.
OMAQEEEMNV.
OrthoDBEOG7X9G6J.
TreeFamTF314638.

Family and domain databases

Gene3D1.10.1300.10. 2 hits.
InterProIPR003607. HD/PDEase_dom.
IPR023088. PDEase.
IPR002073. PDEase_catalytic_dom.
IPR023174. PDEase_CS.
IPR013706. PDEase_N.
[Graphical view]
PfamPF00233. PDEase_I. 1 hit.
PF08499. PDEase_I_N. 1 hit.
[Graphical view]
PRINTSPR00387. PDIESTERASE1.
SMARTSM00471. HDc. 1 hit.
[Graphical view]
PROSITEPS00126. PDEASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20805840.

Entry information

Entry namePDE1A_BOVIN
AccessionPrimary (citable) accession number: P14100
Secondary accession number(s): Q08E30, Q28063
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 114 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families