PDE1B_MOUSE
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 03-AUG-2022, entry version 168.
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 iPTMnet; Q01065; -.
DR PhosphoSitePlus; Q01065; -.
DR MaxQB; Q01065; -.
DR PaxDb; Q01065; -.
DR PeptideAtlas; Q01065; -.
DR PRIDE; Q01065; -.
DR ProteomicsDB; 287804; -.
DR Antibodypedia; 15408; 394 antibodies from 31 providers.
DR DNASU; 18574; -.
DR Ensembl; ENSMUST00000023132; ENSMUSP00000023132; ENSMUSG00000022489.
DR GeneID; 18574; -.
DR KEGG; mmu:18574; -.
DR UCSC; uc007xyh.2; mouse.
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; 904682at2759; -.
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 71 CRISPR screens.
DR PRO; PR:Q01065; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q01065; protein.
DR Bgee; ENSMUSG00000022489; Expressed in caudate-putamen and 210 other tissues.
DR ExpressionAtlas; Q01065; baseline and differential.
DR Genevisible; Q01065; MM.
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:0004114; F:3',5'-cyclic-nucleotide phosphodiesterase activity; IBA:GO_Central.
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:0007626; P:locomotory behavior; IMP:MGI.
DR GO; GO:0030224; P:monocyte differentiation; IEA:Ensembl.
DR GO; GO:0042053; P:regulation of dopamine metabolic process; IMP:MGI.
DR GO; GO:0001505; P:regulation of neurotransmitter levels; IMP:MGI.
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; -; 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 Pfam; PF00233; PDEase_I; 1.
DR Pfam; PF08499; PDEase_I_N; 1.
DR PRINTS; PR00387; PDIESTERASE1.
DR SMART; SM00471; HDc; 1.
DR PROSITE; PS00126; PDEASE_I_1; 1.
DR PROSITE; PS51845; PDEASE_I_2; 1.
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
