ID   PDE1B_RAT               Reviewed;         535 AA.
AC   Q01066; Q548L3;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   27-MAR-2024, entry version 159.
DE   RecName: Full=Dual specificity calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B {ECO:0000305|PubMed:1326532};
DE            Short=Cam-PDE 1B;
DE            EC=3.1.4.17 {ECO:0000269|PubMed:1326532};
DE   AltName: Full=63 kDa Cam-PDE {ECO:0000303|PubMed:1326532};
GN   Name=Pde1b {ECO:0000312|RGD:3278}; Synonyms=Pde1b1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP   REGULATION, AND TISSUE SPECIFICITY.
RX   PubMed=1326532; DOI=10.1016/s0021-9258(19)37015-2;
RA   Repaske D.R., Swinnen J.V., Jin S.-L.C., van Wyk J.J., Conti M.;
RT   "A polymerase chain reaction strategy to identify and clone cyclic
RT   nucleotide phosphodiesterase cDNAs. Molecular cloning of the cDNA encoding
RT   the 63-kDa calmodulin-dependent phosphodiesterase.";
RL   J. Biol. Chem. 267:18683-18688(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Wistar;
RA   Prime G.R., Sutor B.;
RT   "Phosphodiesterase 1B (PDE1B) in rat brain.";
RL   Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-465, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Cyclic nucleotide phosphodiesterase with a dual specificity
CC       for the second messengers cAMP and cGMP, which are key regulators of
CC       many important physiological processes. Has a preference for cGMP as a
CC       substrate. {ECO:0000269|PubMed:1326532}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a nucleoside 3',5'-cyclic phosphate + H2O = a nucleoside 5'-
CC         phosphate + H(+); Xref=Rhea:RHEA:14653, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57867, ChEBI:CHEBI:58464; EC=3.1.4.17;
CC         Evidence={ECO:0000269|PubMed:1326532};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14654;
CC         Evidence={ECO:0000305|PubMed:1326532};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3',5'-cyclic GMP + H2O = GMP + H(+); Xref=Rhea:RHEA:16957,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57746,
CC         ChEBI:CHEBI:58115; Evidence={ECO:0000269|PubMed:1326532};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16958;
CC         Evidence={ECO:0000305|PubMed:1326532};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3',5'-cyclic AMP + H2O = AMP + H(+); Xref=Rhea:RHEA:25277,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58165,
CC         ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q01064};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25278;
CC         Evidence={ECO:0000250|UniProtKB:Q01064};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:Q01064};
CC       Note=Binds 2 divalent metal cations per subunit. Site 1 may
CC       preferentially bind zinc ions. {ECO:0000250|UniProtKB:Q01064};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q01064};
CC       Note=Binds 2 divalent metal cations per subunit. Site 2 has a
CC       preference for magnesium ions. {ECO:0000250|UniProtKB:Q01064};
CC   -!- ACTIVITY REGULATION: Type I PDE are activated by the binding of
CC       calmodulin in the presence of Ca(2+). {ECO:0000269|PubMed:1326532}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P14100}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:Q01064}.
CC   -!- TISSUE SPECIFICITY: Expressed in brain. {ECO:0000269|PubMed:1326532}.
CC   -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family.
CC       PDE1 subfamily. {ECO:0000305}.
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DR   EMBL; M94537; AAA16530.1; -; mRNA.
DR   EMBL; AF327906; AAK15740.1; -; mRNA.
DR   PIR; A44161; A44161.
DR   RefSeq; NP_073201.1; NM_022710.1.
DR   AlphaFoldDB; Q01066; -.
DR   SMR; Q01066; -.
DR   BioGRID; 248311; 1.
DR   STRING; 10116.ENSRNOP00000052147; -.
DR   BindingDB; Q01066; -.
DR   ChEMBL; CHEMBL2111322; -.
DR   DrugCentral; Q01066; -.
DR   iPTMnet; Q01066; -.
DR   PhosphoSitePlus; Q01066; -.
DR   PaxDb; 10116-ENSRNOP00000052147; -.
DR   Ensembl; ENSRNOT00000055272.4; ENSRNOP00000052147.1; ENSRNOG00000036828.4.
DR   Ensembl; ENSRNOT00055049675; ENSRNOP00055040875; ENSRNOG00055028699.
DR   Ensembl; ENSRNOT00060023860; ENSRNOP00060018987; ENSRNOG00060013949.
DR   Ensembl; ENSRNOT00065041426; ENSRNOP00065033840; ENSRNOG00065024115.
DR   GeneID; 29691; -.
DR   KEGG; rno:29691; -.
DR   UCSC; RGD:3278; rat.
DR   AGR; RGD:3278; -.
DR   CTD; 5153; -.
DR   RGD; 3278; Pde1b.
DR   eggNOG; KOG3688; Eukaryota.
DR   GeneTree; ENSGT00940000160712; -.
DR   HOGENOM; CLU_005940_1_3_1; -.
DR   InParanoid; Q01066; -.
DR   OMA; VTQTIHC; -.
DR   OrthoDB; 240889at2759; -.
DR   PhylomeDB; Q01066; -.
DR   TreeFam; TF314638; -.
DR   Reactome; R-RNO-111957; Cam-PDE 1 activation.
DR   Reactome; R-RNO-418457; cGMP effects.
DR   Reactome; R-RNO-418555; G alpha (s) signalling events.
DR   PRO; PR:Q01066; -.
DR   Proteomes; UP000002494; Chromosome 7.
DR   Bgee; ENSRNOG00000036828; Expressed in frontal cortex and 18 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR   GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IDA:UniProtKB.
DR   GO; GO:0047555; F:3',5'-cyclic-GMP phosphodiesterase activity; ISO:RGD.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0048101; F:calmodulin-activated 3',5'-cyclic-GMP phosphodiesterase activity; IBA:GO_Central.
DR   GO; GO:0004117; F:calmodulin-activated dual specificity 3',5'-cyclic-GMP, 3',5'-cyclic-AMP phosphodiesterase activity; ISS:UniProtKB.
DR   GO; GO:0004112; F:cyclic-nucleotide phosphodiesterase activity; IDA:RGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0097011; P:cellular response to granulocyte macrophage colony-stimulating factor stimulus; ISO:RGD.
DR   GO; GO:0036006; P:cellular response to macrophage colony-stimulating factor stimulus; ISO:RGD.
DR   GO; GO:0042420; P:dopamine catabolic process; ISO:RGD.
DR   GO; GO:0007626; P:locomotory behavior; ISO:RGD.
DR   GO; GO:0030224; P:monocyte differentiation; ISO:RGD.
DR   GO; GO:0001975; P:response to amphetamine; ISO:RGD.
DR   GO; GO:0042428; P:serotonin metabolic process; ISO:RGD.
DR   GO; GO:0007165; P:signal transduction; ISO:RGD.
DR   GO; GO:0008542; P:visual learning; ISO:RGD.
DR   CDD; cd00077; HDc; 1.
DR   Gene3D; 1.10.1300.10; 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain; 1.
DR   InterPro; IPR003607; HD/PDEase_dom.
DR   InterPro; IPR023088; PDEase.
DR   InterPro; IPR002073; PDEase_catalytic_dom.
DR   InterPro; IPR036971; PDEase_catalytic_dom_sf.
DR   InterPro; IPR023174; PDEase_CS.
DR   InterPro; IPR013706; PDEase_N.
DR   PANTHER; PTHR11347; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; 1.
DR   PANTHER; PTHR11347:SF194; DUAL SPECIFICITY CALCIUM_CALMODULIN-DEPENDENT 3',5'-CYCLIC NUCLEOTIDE PHOSPHODIESTERASE 1B; 1.
DR   Pfam; PF00233; PDEase_I; 1.
DR   Pfam; PF08499; PDEase_I_N; 1.
DR   PRINTS; PR00387; PDIESTERASE1.
DR   SMART; SM00471; HDc; 1.
DR   SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR   PROSITE; PS00126; PDEASE_I_1; 1.
DR   PROSITE; PS51845; PDEASE_I_2; 1.
DR   Genevisible; Q01066; RN.
PE   1: Evidence at protein level;
KW   Calmodulin-binding; cAMP; cGMP; Cytoplasm; Hydrolase; Magnesium;
KW   Metal-binding; Phosphoprotein; Reference proteome; Zinc.
FT   CHAIN           1..535
FT                   /note="Dual specificity calcium/calmodulin-dependent 3',5'-
FT                   cyclic nucleotide phosphodiesterase 1B"
FT                   /id="PRO_0000198791"
FT   DOMAIN          145..502
FT                   /note="PDEase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01192"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          27..47
FT                   /note="Calmodulin-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P14100"
FT   REGION          117..140
FT                   /note="Calmodulin-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P14100"
FT   REGION          445..474
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          495..535
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        449..463
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        222
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:O76083"
FT   BINDING         226
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q01064"
FT   BINDING         262
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q01064"
FT   BINDING         263
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q01064"
FT   BINDING         263
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q01064"
FT   BINDING         369
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q01064"
FT   MOD_RES         7
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01065"
FT   MOD_RES         14
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01065"
FT   MOD_RES         465
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         513
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01065"
SQ   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
//