ID Q7KYS4_HUMAN Unreviewed; 606 AA. AC Q7KYS4; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 10-FEB-2021, entry version 104. DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067}; DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|EMBL:AAC51915.1}; RN [1] {ECO:0000313|EMBL:AAC51915.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Glioblastoma {ECO:0000313|EMBL:AAC51915.1}; RX PubMed=9429761; DOI=10.1016/S0898-6568(97)00072-7; RA Owens R.J., Lumb S., Rees-Milton K., Russell A., Baldock D., Lang V., RA Crabbe T., Ballesteros M., Perry M.J.; RT "Molecular cloning and expression of a human phosphodiesterase 4C."; RL Cell. Signal. 9:575-585(1997). 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; EC=3.1.4.53; CC Evidence={ECO:0000256|ARBA:ARBA00000621}; 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 -!- PATHWAY: Purine metabolism; 3',5'-cyclic AMP degradation; AMP from CC 3',5'-cyclic AMP: step 1/1. {ECO:0000256|ARBA:ARBA00004703}. 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; U88712; AAC51915.1; -; mRNA. DR RefSeq; NP_001092289.1; NM_001098819.3. DR PeptideAtlas; Q7KYS4; -. DR GeneID; 5143; -. DR CTD; 5143; -. DR PharmGKB; PA264; -. DR UniPathway; UPA00762; UER00747. DR BioGRID-ORCS; 5143; 16 hits in 872 CRISPR screens. DR GenomeRNAi; 5143; -. DR Genevisible; Q7KYS4; HS. DR GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006198; P:cAMP catabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0007165; P:signal transduction; IEA:InterPro. DR CDD; cd00077; HDc; 1. DR Gene3D; 1.10.1300.10; -; 1. DR InterPro; IPR003607; HD/PDEase_dom. DR InterPro; IPR040844; PDE4_UCR. DR InterPro; IPR023088; PDEase. DR InterPro; IPR002073; PDEase_catalytic_dom. DR InterPro; IPR036971; PDEase_catalytic_dom_sf. DR InterPro; IPR023174; PDEase_CS. DR Pfam; PF18100; PDE4_UCR; 1. DR Pfam; PF00233; PDEase_I; 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 2: Evidence at transcript level; KW cAMP {ECO:0000256|ARBA:ARBA00023149}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363067}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR623088-3, ECO:0000256|RuleBase:RU363067}. FT DOMAIN 206..535 FT /note="PDEase" FT /evidence="ECO:0000259|PROSITE:PS51845" FT NP_BIND 282..286 FT /note="cNMP" FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2" FT REGION 75..94 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 530..549 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 557..606 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 79..93 FT /note="Polar" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 557..574 FT /note="Acidic" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 282 FT /note="Proton donor" FT /evidence="ECO:0000256|PIRSR:PIRSR623088-1" FT METAL 286 FT /note="Divalent metal cation 1" FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3" FT METAL 322 FT /note="Divalent metal cation 1" FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3" FT METAL 323 FT /note="Divalent metal cation 1" FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3" FT METAL 323 FT /note="Divalent metal cation 2" FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3" FT METAL 440 FT /note="Divalent metal cation 1" FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3" FT BINDING 323 FT /note="cNMP" FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2" FT BINDING 440 FT /note="cNMP" FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2" FT BINDING 491 FT /note="cNMP" FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2" SQ SEQUENCE 606 AA; 67719 MW; AC14D9401F5CCDCE CRC64; MQAPVPHSQR RESFLYRSDS DYELSPKAMS RNSSVASDLH GEDMIVTPFA QVLASLRTVR SNVAALARQQ CLGAAKQGPV GNPSSSNQLP PAEDTGQKLA LETLDELDWC LDQLETLQTR HSVGEMASNK FKRILNRELT HLSETSRSGN QVSEYISRTF LDQQTEVELP KVTAEEAPQP MSRISGLHGL CHSASLSSAT VPRFGVQTDQ EEQLAKELED TNKWGLDVFK VAELSGNQPL TAIIFSIFQE RDLLKTFQIP ADTLATYLLM LEGHYHANVA YHNSLHAADV AQSTHVLLAT PALEAVFTDL EILAALFASA IHDVDHPGVS NQFLINTNSE LALMYNDASV LENHHLAVGF KLLQAENCDI FQNLSAKQRL SLRRMVIDMV LATDMSKHMN LLADLKTMVE TKKVTSLGVL LLDNYSDRIQ VLQNLVHCAD LSNPTKPLPL YRQWTDRIMA EFFQQGDRER ESGLDISPMC DKHTASVEKS QVGFIDYIAH PLWETWADLV HPDAQDLLDT LEDNREWYQS KIPRSPSDLT NPERDGPDRF QFELTLEEAE EEDEEEEEEG EETALAKEAL ELPDTELLSP EAGPAPGDLP LDNQRT //