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Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1A (Cam-PDE 1A) (EC 3.1.4.17) (61 kDa Cam-PDE)

 PDE1A_BOVIN             Reviewed;         530 AA.
P14100; Q08E30; Q28063;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
12-SEP-2018, entry version 147.
RecName: Full=Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1A;
Short=Cam-PDE 1A;
EC=3.1.4.17;
AltName: Full=61 kDa Cam-PDE;
Name=PDE1A;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=7678006;
Sonnenburg W.K., Seger D., Beavo J.A.;
"Molecular cloning of a cDNA encoding the '61-kDa' calmodulin-
stimulated cyclic nucleotide phosphodiesterase. Tissue-specific
expression of structurally related isoforms.";
J. Biol. Chem. 268:645-652(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Lung;
PubMed=8537356; DOI=10.1074/jbc.270.52.30989;
Sonnenburg W.K., Seger D., Kwak K.S., Huang J., Charbonneau H.,
Beavo J.A.;
"Identification of inhibitory and calmodulin-binding domains of the
PDE1A1 and PDE1A2 calmodulin-stimulated cyclic nucleotide
phosphodiesterases.";
J. Biol. Chem. 270:30989-31000(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=Hereford; TISSUE=Hippocampus;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
[4]
PROTEIN SEQUENCE OF 2-530 (ISOFORM 2).
TISSUE=Brain;
PubMed=1651111; DOI=10.1021/bi00246a009;
Charbonneau H., Kumar S., Novack J.P., Blumenthal D.K., Griffin P.R.,
Shabanowitz J., Hunt D.F., Beavo J.A., Walsh K.A.;
"Evidence for domain organization within the 61-kDa calmodulin-
dependent cyclic nucleotide phosphodiesterase from bovine brain.";
Biochemistry 30:7931-7940(1991).
[5]
PROTEIN SEQUENCE OF 194-427.
TISSUE=Brain;
PubMed=3025833; DOI=10.1073/pnas.83.24.9308;
Charbonneau H., Beier N., Walsh K.A., Beavo J.A.;
"Identification of a conserved domain among cyclic nucleotide
phosphodiesterases from diverse species.";
Proc. Natl. Acad. Sci. U.S.A. 83:9308-9312(1986).
-!- 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). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: Nucleoside 3',5'-cyclic phosphate + H(2)O =
nucleoside 5'-phosphate.
-!- COFACTOR:
Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
Evidence={ECO:0000250};
Note=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. {ECO:0000250};
-!- ACTIVITY REGULATION: Type I PDE are activated by the binding of
calmodulin in the presence of Ca(2+).
-!- SUBUNIT: Homodimer.
-!- INTERACTION:
P84076:Hpca (xeno); NbExp=2; IntAct=EBI-907809, EBI-908193;
P61602:NCALD; NbExp=2; IntAct=EBI-907809, EBI-908133;
P62168:Ncs1 (xeno); NbExp=2; IntAct=EBI-907809, EBI-907774;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=2; Synonyms=PDE1A2;
IsoId=P14100-1; Sequence=Displayed;
Name=1; Synonyms=PDE1A1;
IsoId=P14100-2; Sequence=VSP_004546;
-!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase
family. PDE1 subfamily. {ECO:0000305}.
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EMBL; M90358; AAA74560.1; -; mRNA.
EMBL; L34069; AAA92555.1; -; mRNA.
EMBL; BC123449; AAI23450.1; -; mRNA.
PIR; A45334; A45334.
RefSeq; NP_776839.1; NM_174414.3. [P14100-2]
RefSeq; XP_010800147.1; XM_010801845.1. [P14100-1]
UniGene; Bt.512; -.
ProteinModelPortal; P14100; -.
SMR; P14100; -.
BioGrid; 159260; 2.
IntAct; P14100; 3.
STRING; 9913.ENSBTAP00000051204; -.
BindingDB; P14100; -.
ChEMBL; CHEMBL3774; -.
iPTMnet; P14100; -.
PaxDb; P14100; -.
PRIDE; P14100; -.
Ensembl; ENSBTAT00000016060; ENSBTAP00000016060; ENSBTAG00000012100. [P14100-2]
Ensembl; ENSBTAT00000052318; ENSBTAP00000051204; ENSBTAG00000012100. [P14100-1]
GeneID; 281969; -.
KEGG; bta:281969; -.
CTD; 5136; -.
VGNC; VGNC:32671; PDE1A.
eggNOG; KOG3688; Eukaryota.
eggNOG; ENOG410XQDD; LUCA.
GeneTree; ENSGT00760000118889; -.
HOGENOM; HOG000231888; -.
HOVERGEN; HBG056120; -.
InParanoid; P14100; -.
KO; K13755; -.
OMA; RMYRKSY; -.
OrthoDB; EOG091G04C4; -.
TreeFam; TF314638; -.
Reactome; R-BTA-111957; Cam-PDE 1 activation.
Reactome; R-BTA-418457; cGMP effects.
Reactome; R-BTA-418555; G alpha (s) signalling events.
SABIO-RK; P14100; -.
Proteomes; UP000009136; Chromosome 2.
Bgee; ENSBTAG00000012100; Expressed in 10 organ(s), highest expression level in brain.
GO; GO:0048101; F:calcium- and calmodulin-regulated 3',5'-cyclic-GMP phosphodiesterase activity; IDA:MGI.
GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
GO; GO:0004117; F:calmodulin-dependent cyclic-nucleotide phosphodiesterase activity; IDA:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0007165; P:signal transduction; IEA:InterPro.
CDD; cd00077; HDc; 1.
Gene3D; 1.10.1300.10; -; 1.
InterPro; IPR003607; HD/PDEase_dom.
InterPro; IPR023088; PDEase.
InterPro; IPR002073; PDEase_catalytic_dom.
InterPro; IPR036971; PDEase_catalytic_dom_sf.
InterPro; IPR023174; PDEase_CS.
InterPro; IPR013706; PDEase_N.
Pfam; PF00233; PDEase_I; 1.
Pfam; PF08499; PDEase_I_N; 1.
PRINTS; PR00387; PDIESTERASE1.
SMART; SM00471; HDc; 1.
PROSITE; PS00126; PDEASE_I_1; 1.
PROSITE; PS51845; PDEASE_I_2; 1.
1: Evidence at protein level;
Alternative splicing; Calmodulin-binding; cAMP; cGMP;
Complete proteome; Direct protein sequencing; Hydrolase;
Metal-binding; Reference proteome.
CHAIN 1 530 Calcium/calmodulin-dependent 3',5'-cyclic
nucleotide phosphodiesterase 1A.
/FTId=PRO_0000198784.
DOMAIN 142 508 PDEase. {ECO:0000255|PROSITE-
ProRule:PRU01192}.
REGION 24 44 Calmodulin-binding.
ACT_SITE 219 219 Proton donor.
{ECO:0000250|UniProtKB:O76083}.
METAL 223 223 Divalent metal cation 1; via tele
nitrogen. {ECO:0000250|UniProtKB:Q01064}.
METAL 259 259 Divalent metal cation 1; via tele
nitrogen. {ECO:0000250|UniProtKB:Q01064}.
METAL 260 260 Divalent metal cation 1.
{ECO:0000250|UniProtKB:Q01064}.
METAL 260 260 Divalent metal cation 2.
{ECO:0000250|UniProtKB:Q01064}.
METAL 366 366 Divalent metal cation 1.
{ECO:0000250|UniProtKB:Q01064}.
VAR_SEQ 1 34 MGSTATETEELENTTFKYLIGEQTEKMWQRLKGI -> MDD
HVTIRRKHLQRPIFR (in isoform 1).
{ECO:0000303|PubMed:8537356,
ECO:0000303|Ref.3}.
/FTId=VSP_004546.
CONFLICT 237 237 H -> G (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 321 321 N -> W (in Ref. 5; AA sequence).
{ECO:0000305}.
SEQUENCE 530 AA; 60843 MW; 24CF83E5211AE06F CRC64;
MGSTATETEE LENTTFKYLI GEQTEKMWQR LKGILRCLVK QLEKGDVNVI DLKKNIEYAA
SVLEAVYIDE TRRLLDTDDE LSDIQSDSVP SEVRDWLAST FTRKMGMMKK KSEEKPRFRS
IVHVVQAGIF VERMYRKSYH MVGLAYPEAV IVTLKDVDKW SFDVFALNEA SGEHSLKFMI
YELFTRYDLI NRFKIPVSCL IAFAEALEVG YSKYKNPYHN LIHAADVTQT VHYIMLHTGI
MHWLTELEIL AMVFAAAIHD YEHTGTTNNF HIQTRSDVAI LYNDRSVLEN HHVSAAYRLM
QEEEMNVLIN LSKDDWRDLR NLVIEMVLST DMSGHFQQIK NIRNSLQQPE GLDKAKTMSL
ILHAADISHP AKSWKLHHRW TMALMEEFFL QGDKEAELGL PFSPLCDRKS TMVAQSQIGF
IDFIVEPTFS LLTDSTEKII IPLIEEDSKT KTPSYGASRR SNMKGTTNDG TYSPDYSLAS
VDLKSFKNSL VDIIQQNKER WKELAAQGEP DPHKNSDLVN AEEKHAETHS


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