ID A0A0D9QZB3_CHLSB Unreviewed; 536 AA. AC A0A0D9QZB3; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 02-OCT-2024, entry version 54. DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067}; DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067}; GN Name=PDE1B {ECO:0000313|Ensembl:ENSCSAP00000001702.1}; OS Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; OC Cercopithecidae; Cercopithecinae; Chlorocebus. OX NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000001702.1, ECO:0000313|Proteomes:UP000029965}; RN [1] {ECO:0000313|Ensembl:ENSCSAP00000001702.1, ECO:0000313|Proteomes:UP000029965} RP NUCLEOTIDE SEQUENCE. RA Warren W., Wilson R.K.; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSCSAP00000001702.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUN-2024) to UniProtKB. 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:0000256|ARBA:ARBA00033675}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25278; CC Evidence={ECO:0000256|ARBA:ARBA00033675}; 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:0000256|ARBA:ARBA00033684}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16958; CC Evidence={ECO:0000256|ARBA:ARBA00033684}; 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:0000256|ARBA:ARBA00033709}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14654; CC Evidence={ECO:0000256|ARBA:ARBA00033709}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|ARBA:ARBA00001947}; CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000256|RuleBase:RU363067}; CC Note=Binds 2 divalent metal cations per subunit. Site 1 may CC preferentially bind zinc ions, while site 2 has a preference for CC magnesium and/or manganese ions. {ECO:0000256|RuleBase:RU363067}; CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol CC {ECO:0000256|ARBA:ARBA00004514}. CC -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family. CC PDE1 subfamily. {ECO:0000256|ARBA:ARBA00010664}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AQIB01022982; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_008001716.1; XM_008003525.1. DR AlphaFoldDB; A0A0D9QZB3; -. DR STRING; 60711.ENSCSAP00000001702; -. DR Ensembl; ENSCSAT00000003423.1; ENSCSAP00000001702.1; ENSCSAG00000005388.1. DR GeneID; 103238444; -. DR KEGG; csab:103238444; -. DR CTD; 5153; -. DR eggNOG; KOG3688; Eukaryota. DR GeneTree; ENSGT00940000160712; -. DR OMA; VTQTIHC; -. DR OrthoDB; 240889at2759; -. DR BioGRID-ORCS; 103238444; 0 hits in 9 CRISPR screens. DR Proteomes; UP000029965; Chromosome 11. DR Bgee; ENSCSAG00000005388; Expressed in caudate nucleus and 5 other cell types or tissues. DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell. DR GO; GO:0004117; F:calmodulin-activated dual specificity 3',5'-cyclic-GMP, 3',5'-cyclic-AMP phosphodiesterase activity; IEA:Ensembl. 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; IEA:Ensembl. DR GO; GO:0036006; P:cellular response to macrophage colony-stimulating factor stimulus; IEA:Ensembl. DR GO; GO:0042420; P:dopamine catabolic process; IEA:Ensembl. DR GO; GO:0007626; P:locomotory behavior; IEA:Ensembl. DR GO; GO:0030224; P:monocyte differentiation; IEA:Ensembl. DR GO; GO:0001975; P:response to amphetamine; IEA:Ensembl. DR GO; GO:0042428; P:serotonin metabolic process; IEA:Ensembl. DR GO; GO:0007165; P:signal transduction; IEA:Ensembl. DR GO; GO:0008542; P:visual learning; IEA:Ensembl. 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 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363067}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR623088-3}; KW Reference proteome {ECO:0000313|Proteomes:UP000029965}. FT DOMAIN 146..503 FT /note="PDEase" FT /evidence="ECO:0000259|PROSITE:PS51845" FT REGION 1..20 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 447..473 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 494..536 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 39..91 FT /evidence="ECO:0000256|SAM:Coils" FT COMPBIAS 450..464 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 223 FT /note="Proton donor" FT /evidence="ECO:0000256|PIRSR:PIRSR623088-1" FT BINDING 223..227 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2" FT BINDING 227 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3" FT BINDING 263 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3" FT BINDING 264 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2" FT BINDING 264 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3" FT BINDING 264 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3" FT BINDING 370 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2" FT BINDING 370 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3" FT BINDING 421 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2" SQ SEQUENCE 536 AA; 61365 MW; 5B0F82829574B9C6 CRC64; MELSPRSPPE MLEESDCPSP LELKSAPSKK MWIKLRSLLR YMVKQLENGE VNIEELKKNL EYTASLLEAV YIDETRQILD TEDELQELRS DAVPSEVRDW LASTFTQQAR AKGRRAEEKP KFRSIVHAVQ AGIFVERMFR RTYTSVGPTY STAVLNCFKN LDLWCFDVFS LNRAADDHAL RTIVFELLTR HNLISRFKIP TVFLMSFLDA LETGYGKYKN PYHNQIHAAD VTQTVHCFLL RTGMVHCLSE IEVLAIIFAA AIHDYEHTGT TNSFHIQTKS ECAILYNDRS VLENHHISSV FRLMQDDELN IFINLTKDEF VELRALVIEM VLATDMSCHF QQVKTMKTAL QQLERIDKPK ALSLLLHAAD ISHPTKQWSV HSRWTKALME EFFRQGDKEA ELGLPFSPLC DRTSTLVAQS QIGFIDFIVE PTFSVLTDVA EKSVQPLADE DSKSKNQPSF QWRQPSLDVE VGDPNPDVVS FRSTWIKHIQ ENKQKWKERA ASGITNQMSI DELSPCDEEA PPSPAEDEHN QNGNLD //