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Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B (Cam-PDE 1B) (EC 3.1.4.17) (63 kDa Cam-PDE)

 PDE1B_RAT               Reviewed;         535 AA.
Q01066; Q548L3;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
01-APR-1993, sequence version 1.
22-NOV-2017, entry version 129.
RecName: Full=Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B;
Short=Cam-PDE 1B;
EC=3.1.4.17;
AltName: Full=63 kDa Cam-PDE;
Name=Pde1b; Synonyms=Pde1b1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1326532;
Repaske D.R., Swinnen J.V., Jin S.-L.C., van Wyk J.J., Conti M.;
"A polymerase chain reaction strategy to identify and clone cyclic
nucleotide phosphodiesterase cDNAs. Molecular cloning of the cDNA
encoding the 63-kDa calmodulin-dependent phosphodiesterase.";
J. Biol. Chem. 267:18683-18688(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Wistar;
Prime G.R., Sutor B.;
"Phosphodiesterase 1B (PDE1B) in rat brain.";
Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-465, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- 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
preference for cGMP as a substrate (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.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase
family. PDE1 subfamily. {ECO:0000305}.
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EMBL; M94537; AAA16530.1; -; mRNA.
EMBL; AF327906; AAK15740.1; -; mRNA.
PIR; A44161; A44161.
RefSeq; NP_073201.1; NM_022710.1.
UniGene; Rn.53489; -.
ProteinModelPortal; Q01066; -.
SMR; Q01066; -.
STRING; 10116.ENSRNOP00000052147; -.
BindingDB; Q01066; -.
ChEMBL; CHEMBL2111322; -.
iPTMnet; Q01066; -.
PhosphoSitePlus; Q01066; -.
PaxDb; Q01066; -.
PRIDE; Q01066; -.
Ensembl; ENSRNOT00000055272; ENSRNOP00000052147; ENSRNOG00000036828.
GeneID; 29691; -.
KEGG; rno:29691; -.
UCSC; RGD:3278; rat.
CTD; 5153; -.
RGD; 3278; Pde1b.
eggNOG; KOG3688; Eukaryota.
eggNOG; ENOG410XQDD; LUCA.
GeneTree; ENSGT00760000118889; -.
HOGENOM; HOG000231888; -.
HOVERGEN; HBG056120; -.
InParanoid; Q01066; -.
KO; K13755; -.
OMA; LMQDDEM; -.
OrthoDB; EOG091G04C4; -.
PhylomeDB; Q01066; -.
TreeFam; TF314638; -.
Reactome; R-RNO-111957; Cam-PDE 1 activation.
Reactome; R-RNO-418457; cGMP effects.
Reactome; R-RNO-418555; G alpha (s) signalling events.
PRO; PR:Q01066; -.
Proteomes; UP000002494; Chromosome 7.
Bgee; ENSRNOG00000036828; -.
Genevisible; Q01066; RN.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0043025; C:neuronal cell body; IDA:RGD.
GO; GO:0005634; C:nucleus; IEA:Ensembl.
GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IDA:RGD.
GO; GO:0048101; F:calcium- and calmodulin-regulated 3',5'-cyclic-GMP phosphodiesterase activity; IDA:RGD.
GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
GO; GO:0004112; F:cyclic-nucleotide phosphodiesterase activity; IDA:RGD.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006198; P:cAMP catabolic process; IDA:RGD.
GO; GO:0097011; P:cellular response to granulocyte macrophage colony-stimulating factor stimulus; ISO:RGD.
GO; GO:0036006; P:cellular response to macrophage colony-stimulating factor stimulus; ISO:RGD.
GO; GO:0046069; P:cGMP catabolic process; IDA:RGD.
GO; GO:0007626; P:locomotory behavior; ISO:RGD.
GO; GO:0030224; P:monocyte differentiation; ISO:RGD.
GO; GO:0042053; P:regulation of dopamine metabolic process; ISO:RGD.
GO; GO:0001505; P:regulation of neurotransmitter levels; ISO:RGD.
GO; GO:0001975; P:response to amphetamine; ISO:RGD.
GO; GO:0042428; P:serotonin metabolic process; ISO:RGD.
GO; GO:0007165; P:signal transduction; ISO:RGD.
GO; GO:0008542; P:visual learning; ISO:RGD.
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: Evidence at protein level;
Calmodulin-binding; cAMP; cGMP; Complete proteome; Cytoplasm;
Hydrolase; Metal-binding; Phosphoprotein; Reference proteome.
CHAIN 1 535 Calcium/calmodulin-dependent 3',5'-cyclic
nucleotide phosphodiesterase 1B.
/FTId=PRO_0000198791.
REGION 27 47 Calmodulin-binding. {ECO:0000255}.
REGION 196 495 Catalytic. {ECO:0000250}.
ACT_SITE 222 222 Proton donor.
{ECO:0000250|UniProtKB:O76083}.
METAL 226 226 Divalent metal cation 1; via tele
nitrogen. {ECO:0000250|UniProtKB:Q01064}.
METAL 262 262 Divalent metal cation 1; via tele
nitrogen. {ECO:0000250|UniProtKB:Q01064}.
METAL 263 263 Divalent metal cation 1.
{ECO:0000250|UniProtKB:Q01064}.
METAL 263 263 Divalent metal cation 2.
{ECO:0000250|UniProtKB:Q01064}.
METAL 369 369 Divalent metal cation 1.
{ECO:0000250|UniProtKB:Q01064}.
MOD_RES 7 7 Phosphoserine.
{ECO:0000250|UniProtKB:Q01065}.
MOD_RES 14 14 Phosphoserine.
{ECO:0000250|UniProtKB:Q01065}.
MOD_RES 465 465 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 513 513 Phosphoserine.
{ECO:0000250|UniProtKB:Q01065}.
SEQUENCE 535 AA; 61260 MW; F98FFFE61F848F89 CRC64;
MELSPRSPPE MLESDCPSPL ELKSAPSKKM WIKLRSLLRY MVKQLENGEV NIEELKKNLE
YTASLLEAVY IDETRQILDT EDELRELRSD AVPSEVRDWL ASTFTQQTRA KGRRAEEKPK
FRSIVHAVQA GIFVERMFRR TYTAVGPTYS TAVHNCLKNL DVWCFDVFSL NRAADDHALR
TIVFELLTRH SLISRFKIPT VFLMSFLEAL ETGYGKYKNP YHNQIHAADV TQTVHCFLLR
TGMVHCLSEI EVLAIIFAAA IHDYEHTGTT NSFHIQTKSE CAILYNDRSV LENHHISSVF
RMMQDDEMNI FINLTKDEFV ELRALVIEMV LATDMSCHFQ QVKTMKTALQ QLERIDKSKA
LSLLLHAADI SHPTKQWSVH SRWTKALMEE FFRQGDKEAE LGLPFSPLCD RTSTLVAQSQ
IGFIDFIVEP TFSVLTDVAE KSVQPLTDDD SKSKSQPSFQ WRQPSLDVDV GDPNPDVVSF
RSTWTKYIQE NKQKWKERAA SGITNQMSID ELSPCEEEAP SSPAEDEHNQ NGNLD


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