PDE1B_RAT
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 03-AUG-2022, entry version 152.
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; Q01066; -.
DR PRIDE; Q01066; -.
DR Ensembl; ENSRNOT00000055272; ENSRNOP00000052147; ENSRNOG00000036828.
DR GeneID; 29691; -.
DR KEGG; rno:29691; -.
DR UCSC; RGD:3278; rat.
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; HCADIAH; -.
DR OrthoDB; 904682at2759; -.
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 tissues.
DR Genevisible; Q01066; RN.
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: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; 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:0007626; P:locomotory behavior; ISO:RGD.
DR GO; GO:0030224; P:monocyte differentiation; ISO:RGD.
DR GO; GO:0042053; P:regulation of dopamine metabolic process; ISO:RGD.
DR GO; GO:0001505; P:regulation of neurotransmitter levels; 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; -; 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_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
