ID A0A0D9QZB3_CHLSB Unreviewed; 536 AA. AC A0A0D9QZB3; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 11-DEC-2019, entry version 32. DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067}; DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067}; GN Name=PDE1B {ECO:0000313|Ensembl:ENSCSAP00000001702}; 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, ECO:0000313|Proteomes:UP000029965}; RN [1] {ECO:0000313|Ensembl:ENSCSAP00000001702, 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} RP IDENTIFICATION. RG Ensembl; RL Submitted (APR-2015) to UniProtKB. 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 -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family. CC {ECO:0000256|RuleBase:RU363067, ECO:0000256|SAAS:SAAS01040771}. 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 STRING; 60711.ENSCSAP00000001702; -. DR Ensembl; ENSCSAT00000003423; ENSCSAP00000001702; ENSCSAG00000005388. DR GeneID; 103238444; -. DR KEGG; csab:103238444; -. DR CTD; 5153; -. DR GeneTree; ENSGT00940000160712; -. DR KO; K13755; -. DR OMA; FKIPISC; -. DR OrthoDB; 904682at2759; -. DR Proteomes; UP000029965; Chromosome 11. DR GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IEA:Ensembl. DR GO; GO:0047555; F:3',5'-cyclic-GMP 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:0007626; P:locomotory behavior; IEA:Ensembl. DR GO; GO:0030224; P:monocyte differentiation; IEA:Ensembl. DR GO; GO:0042053; P:regulation of dopamine metabolic process; 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; -; 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 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Hydrolase {ECO:0000256|RuleBase:RU363067, ECO:0000256|SAAS:SAAS01040760}; KW Metal-binding {ECO:0000256|RuleBase:RU363067, KW ECO:0000256|SAAS:SAAS01040765}; 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..59 FT /evidence="ECO:0000256|SAM:Coils" FT COILED 71..91 FT /evidence="ECO:0000256|SAM:Coils" FT COMPBIAS 450..464 FT /note="Polar" FT /evidence="ECO:0000256|SAM:MobiDB-lite" 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 //