ID A0A0D9QZB3_CHLSB Unreviewed; 536 AA. AC A0A0D9QZB3; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 29-SEP-2021, entry version 39. 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}. 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 eggNOG; KOG3688; Eukaryota. DR GeneTree; ENSGT00940000160712; -. DR OMA; PCEEEPR; -. DR OrthoDB; 904682at2759; -. DR BioGRID-ORCS; 103238444; 0 hits in 5 CRISPR screens. DR Proteomes; UP000029965; Chromosome 11. DR GO; GO:0004114; F:3',5'-cyclic-nucleotide phosphodiesterase activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0007626; P:locomotory behavior; IEA:Ensembl. DR GO; GO:0042053; P:regulation of dopamine metabolic process; IEA:Ensembl. DR GO; GO:0001505; P:regulation of neurotransmitter levels; 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|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 NP_BIND 223..227 FT /note="cNMP" FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2" 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 residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 223 FT /note="Proton donor" FT /evidence="ECO:0000256|PIRSR:PIRSR623088-1" FT METAL 227 FT /note="Divalent metal cation 1" FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3" FT METAL 263 FT /note="Divalent metal cation 1" FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3" FT METAL 264 FT /note="Divalent metal cation 1" FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3" FT METAL 264 FT /note="Divalent metal cation 2" FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3" FT METAL 370 FT /note="Divalent metal cation 1" FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3" FT BINDING 264 FT /note="cNMP" FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2" FT BINDING 370 FT /note="cNMP" FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2" FT BINDING 421 FT /note="cNMP" 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 //