PDE1B_BOVIN
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 03-AUG-2022, entry version 142.
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; Q01061; -.
DR PRIDE; Q01061; -.
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: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; 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; -; 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; 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
