ID   PDE1B_BOVIN             Reviewed;         534 AA.
AC   Q01061;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   27-MAR-2024, entry version 148.
DE   RecName: Full=Dual specificity calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B {ECO:0000305|PubMed:1326531};
DE            Short=Cam-PDE 1B {ECO:0000303|PubMed:1651112};
DE            EC=3.1.4.17 {ECO:0000269|PubMed:1326531};
DE   AltName: Full=63 kDa Cam-PDE {ECO:0000303|PubMed:1651112};
GN   Name=PDE1B {ECO:0000250|UniProtKB:Q01064}; Synonyms=PDE1B1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP   REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   PubMed=1326531; DOI=10.1016/s0021-9258(19)37014-0;
RA   Bentley J.K., Kadlecek A., Sherbert C.H., Seger D., Sonnenburg W.K.,
RA   Charbonneau H., Novack J.P., Beavo J.A.;
RT   "Molecular cloning of cDNA encoding a '63'-kDa calmodulin-stimulated
RT   phosphodiesterase from bovine brain.";
RL   J. Biol. Chem. 267:18676-18682(1992).
RN   [2]
RP   PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Brain;
RX   PubMed=1651112; DOI=10.1021/bi00246a010;
RA   Novack J.P., Charbonneau H., Bentley J.K., Walsh K.A., Beavo J.A.;
RT   "Sequence comparison of the 63-, 61-, and 59-kDa calmodulin-dependent
RT   cyclic nucleotide phosphodiesterases.";
RL   Biochemistry 30:7940-7947(1991).
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:1326531}.
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:1326531};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14654;
CC         Evidence={ECO:0000305|PubMed:1326531};
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:1326531};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16958;
CC         Evidence={ECO:0000305|PubMed:1326531};
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:0000269|PubMed:1326531};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25278;
CC         Evidence={ECO:0000305|PubMed:1326531};
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:1326531}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         Vmax=23 nmol/min/mg enzyme with cGMP as substrate (in presence of
CC         calcium and calmodulin) {ECO:0000269|PubMed:1326531};
CC         Vmax=4.9 nmol/min/mg enzyme with cAMP as substrate (in presence of
CC         calcium and calmodulin) {ECO:0000269|PubMed:1326531};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P14100}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:Q01064}.
CC   -!- TISSUE SPECIFICITY: Expressed in central nervous system regions. Most
CC       abundant in basal ganglia. Also found in kidney papilla and adrenal
CC       medulla. {ECO:0000269|PubMed:1326531}.
CC   -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family.
CC       PDE1 subfamily. {ECO:0000305}.
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DR   EMBL; M94867; AAA74558.1; -; mRNA.
DR   PIR; A44162; A44162.
DR   RefSeq; NP_776840.1; NM_174415.2.
DR   AlphaFoldDB; Q01061; -.
DR   SMR; Q01061; -.
DR   BioGRID; 159261; 2.
DR   STRING; 9913.ENSBTAP00000005680; -.
DR   BindingDB; Q01061; -.
DR   ChEMBL; CHEMBL2650; -.
DR   DrugCentral; Q01061; -.
DR   PaxDb; 9913-ENSBTAP00000005680; -.
DR   GeneID; 281970; -.
DR   KEGG; bta:281970; -.
DR   CTD; 5153; -.
DR   eggNOG; KOG3688; Eukaryota.
DR   HOGENOM; CLU_005940_1_3_1; -.
DR   InParanoid; Q01061; -.
DR   SABIO-RK; Q01061; -.
DR   PRO; PR:Q01061; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0043025; C:neuronal cell body; IBA:GO_Central.
DR   GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IDA:UniProtKB.
DR   GO; GO:0047555; F:3',5'-cyclic-GMP phosphodiesterase activity; IDA:UniProtKB.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0048101; F:calmodulin-activated 3',5'-cyclic-GMP phosphodiesterase activity; IDA:MGI.
DR   GO; GO:0004117; F:calmodulin-activated dual specificity 3',5'-cyclic-GMP, 3',5'-cyclic-AMP phosphodiesterase activity; IDA:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
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.
PE   1: Evidence at protein level;
KW   Calmodulin-binding; cAMP; cGMP; Cytoplasm; Direct protein sequencing;
KW   Hydrolase; Magnesium; Metal-binding; Phosphoprotein; Reference proteome;
KW   Zinc.
FT   CHAIN           1..534
FT                   /note="Dual specificity calcium/calmodulin-dependent 3',5'-
FT                   cyclic nucleotide phosphodiesterase 1B"
FT                   /id="PRO_0000198787"
FT   DOMAIN          144..501
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          116..139
FT                   /note="Calmodulin-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P14100"
FT   REGION          442..473
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          494..534
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        448..462
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        221
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:O76083"
FT   BINDING         225
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q01064"
FT   BINDING         261
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q01064"
FT   BINDING         262
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
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         368
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         464
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01065"
FT   MOD_RES         512
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01065"
SQ   SEQUENCE   534 AA;  61006 MW;  C86C3F48E0AE9B69 CRC64;
     MELSPRSPPE MLESDCPSPL ELKSAPSKKM WIKLRSLLRY MVKQLENGEV NIEELKKNLE
     YTASLLEAVY IDETRQILDT EDELQELRSD AVPSEVRDWL ASTFTQQTRA KGPSEEKPKF
     RSIVHAVQAG IFVERMFRRT YTSVGPTYST AVLNCLKNVD LWCFDVFSLN RAADDHALRT
     IVFELLTRHN LISRFKIPTV FLMTFLDALE TGYGKYKNPY HNQIHAADVT QTVHCFLLRT
     GMVHCLSEIE VLAIIFAAAI HDYEHTGTTN SFHIQTKSEC AILYNDRSVL ENHHISSVFR
     MMQDDEMNIF INLTKDEFVE LRALVIEMVL ATDMSCHFQQ VKSMKTALQQ LERIDKSKAL
     SLLLHAADIS HPTKQWSVHS RWTKALMEEF FRQGDKEAEL GLPFSPLCDR TSTLVAQSQI
     GFIDFIVEPT FSVLTDVAEK SVQPTGDDDS KSKNQPSFQW RQPSLDVEVG DPNPDVVSFR
     STWTKYIQEN KQKWKERAAS GITNQMSIDE LSPCEEEAPA SPAEDEHNQN GNLD
//