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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_MOUSE             Reviewed;         565 AA.
Q61481; E9Q6V1; O35388;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
20-JUN-2018, entry version 130.
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;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PDE1A2).
STRAIN=BALB/cJ; TISSUE=Brain;
Yan C., Sonnenburg W.K., Zhao A.Z., Kwak K.S., Beavo J.A.;
Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-262 (ISOFORM PDE1A1).
TISSUE=Heart;
Sonnenburg W.K., Rybalkin S.D., Bornfeldt K.E., Kwak K.S.,
Rybalkina I., Beavo J.A.;
Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
[4]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- 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};
-!- ENZYME REGULATION: Type I PDE are activated by the binding of
calmodulin in the presence of Ca(2+).
-!- SUBUNIT: Homodimer. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=PDE1A2;
IsoId=Q61481-1; Sequence=Displayed;
Name=PDE1A1;
IsoId=Q61481-2; Sequence=VSP_004551;
-!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase
family. PDE1 subfamily. {ECO:0000305}.
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EMBL; U56649; AAB03319.1; -; mRNA.
EMBL; AL844577; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL928607; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL928811; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AF023529; AAB81952.1; -; mRNA.
RefSeq; XP_006498986.1; XM_006498923.3.
UniGene; Mm.40678; -.
ProteinModelPortal; Q61481; -.
BioGrid; 202074; 2.
IntAct; Q61481; 2.
MINT; Q61481; -.
STRING; 10090.ENSMUSP00000099713; -.
iPTMnet; Q61481; -.
PhosphoSitePlus; Q61481; -.
PaxDb; Q61481; -.
PeptideAtlas; Q61481; -.
PRIDE; Q61481; -.
GeneID; 18573; -.
UCSC; uc008khd.2; mouse. [Q61481-1]
CTD; 5136; -.
MGI; MGI:1201792; Pde1a.
eggNOG; KOG3688; Eukaryota.
eggNOG; ENOG410XQDD; LUCA.
HOGENOM; HOG000231888; -.
HOVERGEN; HBG056120; -.
InParanoid; Q61481; -.
BRENDA; 3.1.4.17; 3474.
PRO; PR:Q61481; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_PDE1A; -.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0043025; C:neuronal cell body; ISO:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; ISO:MGI.
GO; GO:0048101; F:calcium- and calmodulin-regulated 3',5'-cyclic-GMP phosphodiesterase activity; ISO:MGI.
GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
GO; GO:0004117; F:calmodulin-dependent cyclic-nucleotide phosphodiesterase activity; ISO:MGI.
GO; GO:0030553; F:cGMP binding; ISO:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006198; P:cAMP catabolic process; ISO:MGI.
GO; GO:0046069; P:cGMP catabolic process; ISO:MGI.
GO; GO:0034391; P:regulation of smooth muscle cell apoptotic process; ISO:MGI.
GO; GO:0048660; P:regulation of smooth muscle cell proliferation; ISO:MGI.
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; Hydrolase; Metal-binding; Reference proteome.
CHAIN 1 565 Calcium/calmodulin-dependent 3',5'-cyclic
nucleotide phosphodiesterase 1A.
/FTId=PRO_0000198786.
DOMAIN 162 542 PDEase. {ECO:0000255|PROSITE-
ProRule:PRU01192}.
REGION 44 64 Calmodulin-binding.
ACT_SITE 239 239 Proton donor.
{ECO:0000250|UniProtKB:O76083}.
METAL 243 243 Divalent metal cation 1; via tele
nitrogen. {ECO:0000250|UniProtKB:Q01064}.
METAL 279 279 Divalent metal cation 1; via tele
nitrogen. {ECO:0000250|UniProtKB:Q01064}.
METAL 280 280 Divalent metal cation 1.
{ECO:0000250|UniProtKB:Q01064}.
METAL 280 280 Divalent metal cation 2.
{ECO:0000250|UniProtKB:Q01064}.
METAL 386 386 Divalent metal cation 1.
{ECO:0000250|UniProtKB:Q01064}.
VAR_SEQ 1 54 MCDSSPSSSHVWIAPVRNIIMGSTDTDIEELENATYKYLIG
EQTEKMWQRLKGI -> MDEYVTIRKKHLQRPIFR (in
isoform PDE1A1). {ECO:0000303|Ref.3}.
/FTId=VSP_004551.
CONFLICT 2 3 CD -> VG (in Ref. 1; AAB03319).
{ECO:0000305}.
CONFLICT 6 6 P -> T (in Ref. 1; AAB03319).
{ECO:0000305}.
SEQUENCE 565 AA; 64529 MW; 848103C73CC0FB7B CRC64;
MCDSSPSSSH VWIAPVRNII MGSTDTDIEE LENATYKYLI GEQTEKMWQR LKGILRCLVK
QLEKGDVNVV DLKKNIEYAA SVLEAVYIDE TRRLLDTEDE LSDIQTDSVP SEVRDWLAST
FTRKMGMMKK KPEEKPKFRS IVHAVQAGIF VERMYRKNYH MVGLTYPAAV IVTLKEVDKW
SFDVFALNEA SGEHSLKFMI YELFTRYDLI NRFKIPVSCL IAFAEALEVG YSKHKNPYHN
LVHAADVTQT VHYIMLHTGI MHWLTELEIL AMVFAAAIHD YEHTGTTNNF HIQTRSDVAI
LYNDRSVLEN HHVSAAYRLM QEEEMNILVN LSKDDWRDLR NLVIEMVLAT DMSGHFQQIK
NIRNSLQQPE GIDRAKTMSL ILHAADISHP AKTWKLHYRW TMALMEEFFL QGDKEAELGL
PFSPLCDRKS TMVAQSQIGF IDFIVEPTFS LLTDSTEKIV IPLIEEASKS QSSNYGASSS
STMIGFHVAD SLRRSNTKGS VCDGSYAPDY SLSAVDLKSF KNNLVDIIQQ NKERWKELAA
QGELDLHKNS EELGNTEEKH ADTRP


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