ID   PDE1B_MOUSE             Reviewed;         535 AA.
AC   Q01065; O35384;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   27-MAR-2024, entry version 177.
DE   RecName: Full=Dual specificity calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B {ECO:0000250|UniProtKB:Q01064};
DE            Short=Cam-PDE 1B;
DE            EC=3.1.4.17 {ECO:0000250|UniProtKB:Q01064};
DE   AltName: Full=63 kDa Cam-PDE;
GN   Name=Pde1b {ECO:0000312|MGI:MGI:97523}; Synonyms=Pde1b1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1332068; DOI=10.1073/pnas.89.22.11079;
RA   Polli J.W., Kincaid R.L.;
RT   "Molecular cloning of DNA encoding a calmodulin-dependent phosphodiesterase
RT   enriched in striatum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:11079-11083(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 38-535.
RC   STRAIN=129/SvJ;
RX   PubMed=9657856; DOI=10.1007/s003359900820;
RA   Reed T.M., Browning J.E., Blough R.I., Vorhees C.V., Repaske D.R.;
RT   "Genomic structure and chromosome location of the murine PDE1B
RT   phosphodiesterase gene.";
RL   Mamm. Genome 9:571-576(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 221-336.
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   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-465, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7; SER-14; SER-465 AND
RP   SER-513, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, and Liver;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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:0000250|UniProtKB:Q01064}.
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:0000250|UniProtKB:Q01064};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14654;
CC         Evidence={ECO:0000250|UniProtKB:Q01064};
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:0000250|UniProtKB:Q01064};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16958;
CC         Evidence={ECO:0000250|UniProtKB:Q01064};
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:0000250|UniProtKB:Q01064}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P14100}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:Q01064}.
CC   -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family.
CC       PDE1 subfamily. {ECO:0000305}.
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DR   EMBL; L01695; AAA39902.1; -; mRNA.
DR   EMBL; AH007066; AAC96022.1; -; Genomic_DNA.
DR   EMBL; M94538; AAA37367.1; -; mRNA.
DR   CCDS; CCDS27904.1; -.
DR   PIR; A46378; A46378.
DR   RefSeq; NP_032826.1; NM_008800.2.
DR   AlphaFoldDB; Q01065; -.
DR   SMR; Q01065; -.
DR   BioGRID; 202075; 10.
DR   IntAct; Q01065; 1.
DR   STRING; 10090.ENSMUSP00000023132; -.
DR   GlyGen; Q01065; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q01065; -.
DR   PhosphoSitePlus; Q01065; -.
DR   MaxQB; Q01065; -.
DR   PaxDb; 10090-ENSMUSP00000023132; -.
DR   PeptideAtlas; Q01065; -.
DR   ProteomicsDB; 287804; -.
DR   Antibodypedia; 15408; 425 antibodies from 31 providers.
DR   DNASU; 18574; -.
DR   Ensembl; ENSMUST00000023132.5; ENSMUSP00000023132.4; ENSMUSG00000022489.7.
DR   GeneID; 18574; -.
DR   KEGG; mmu:18574; -.
DR   UCSC; uc007xyh.2; mouse.
DR   AGR; MGI:97523; -.
DR   CTD; 5153; -.
DR   MGI; MGI:97523; Pde1b.
DR   VEuPathDB; HostDB:ENSMUSG00000022489; -.
DR   eggNOG; KOG3688; Eukaryota.
DR   GeneTree; ENSGT00940000160712; -.
DR   HOGENOM; CLU_005940_1_0_1; -.
DR   InParanoid; Q01065; -.
DR   OMA; KIQWKDS; -.
DR   OrthoDB; 240889at2759; -.
DR   PhylomeDB; Q01065; -.
DR   TreeFam; TF314638; -.
DR   BRENDA; 3.1.4.17; 3474.
DR   Reactome; R-MMU-111957; Cam-PDE 1 activation.
DR   Reactome; R-MMU-418457; cGMP effects.
DR   Reactome; R-MMU-418555; G alpha (s) signalling events.
DR   BioGRID-ORCS; 18574; 5 hits in 76 CRISPR screens.
DR   PRO; PR:Q01065; -.
DR   Proteomes; UP000000589; Chromosome 15.
DR   RNAct; Q01065; Protein.
DR   Bgee; ENSMUSG00000022489; Expressed in caudate-putamen and 212 other cell types or tissues.
DR   ExpressionAtlas; Q01065; baseline and differential.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR   GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; ISO:MGI.
DR   GO; GO:0047555; F:3',5'-cyclic-GMP phosphodiesterase activity; ISO:MGI.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0048101; F:calmodulin-activated 3',5'-cyclic-GMP phosphodiesterase activity; ISO:MGI.
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; ISO:MGI.
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:MGI.
DR   GO; GO:0036006; P:cellular response to macrophage colony-stimulating factor stimulus; ISO:MGI.
DR   GO; GO:0042420; P:dopamine catabolic process; IMP:MGI.
DR   GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR   GO; GO:0030224; P:monocyte differentiation; IEA:Ensembl.
DR   GO; GO:0001975; P:response to amphetamine; IMP:MGI.
DR   GO; GO:0042428; P:serotonin metabolic process; IMP:MGI.
DR   GO; GO:0007165; P:signal transduction; IMP:MGI.
DR   GO; GO:0008542; P:visual learning; IMP:MGI.
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; Q01065; MM.
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_0000198790"
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          444..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:0007744|PubMed:21183079"
FT   MOD_RES         14
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         465
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:15345747,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         513
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CONFLICT        38
FT                   /note="L -> M (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        224
FT                   /note="Q -> R (in Ref. 3; AAA37367)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   535 AA;  61226 MW;  F87A585537C8D1CD CRC64;
     MELSPRSPPE MLESDCPSPL ELKSAPSKKM WIKLRSLLRY MVKQLENGEV NIEELKKNLE
     YTASLLEAVY IDETRQILDT EDELRELRSD AVPSEVRDWL ASTFTQQTRA KGRRAEEKPK
     FRSIVHAVQA GIFVERMFRR TYTSVGPTYS TAVHNCLKNL DLWCFDVFSL NRAADDHALR
     TIVFELLTRH SLISRFKIPT VFLMSFLEAL ETGYGKYKNP YHNQIHAADV TQTVHCFLLR
     TGMVHCLSEI EVLAIIFAAA IHDYEHTGTT NSFHIQTKSE CAILYNDRSV LENHHISSVF
     RMMQDDEMNI FINLTKDEFA ELRALVIEMV LATDMSCHFQ QVKTMKTALQ QLERIDKSKA
     LSLLLHAADI SHPTKQWSVH SRWTKALMEE FFRQGDKEAE LGLPFSPLCD RTSTLVAQSQ
     IGFIDFIVEP TFSVLTDVAE KSVQPLADDD SKPKSQPSFQ WRQPSLDVDV GDPNPDVVSF
     RATWTKYIQE NKQKWKERAA SGITNQMSID ELSPCEEEAP SSPAEDEHNQ NGNLD
//