ID Q7KYS4_HUMAN Unreviewed; 606 AA. AC Q7KYS4; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 11-JAN-2011, entry version 46. DE SubName: Full=Phosphodiesterase 4C; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE. RC TISSUE=Glioblastoma; RX MEDLINE=98091596; 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). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 200-557. RX PubMed=17727341; DOI=10.1042/BJ20070970; RA Wang H., Peng M.-S., Chen Y., Geng J., Robinson H., Houslay M.D., RA Cai J., Ke H.; RT "Structures of the four subfamilies of phosphodiesterase-4 provide RT insight into the selectivity of their inhibitors."; RL Biochem. J. 408:193-201(2007). 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 IPI; IPI00328206; -. DR RefSeq; NP_001092289.1; NM_001098819.1. DR UniGene; Hs.132584; -. DR ProteinModelPortal; Q7KYS4; -. DR SMR; Q7KYS4; 201-534. DR STRING; Q7KYS4; -. DR Ensembl; ENST00000262805; ENSP00000262805; ENSG00000105650. DR Ensembl; ENST00000355502; ENSP00000347689; ENSG00000105650. DR Ensembl; ENST00000447275; ENSP00000402091; ENSG00000105650. DR GeneID; 5143; -. DR KEGG; hsa:5143; -. DR CTD; 5143; -. DR HGNC; HGNC:8782; PDE4C. DR HOVERGEN; HBG108239; -. DR NextBio; 19838; -. DR ArrayExpress; Q7KYS4; -. DR Bgee; Q7KYS4; -. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0007165; P:signal transduction; IEA:InterPro. DR InterPro; IPR003607; Metal-dep_PHydrolase_HD_dom. DR InterPro; IPR023088; PDEase. DR InterPro; IPR002073; PDEase_catalytic_dom. DR InterPro; IPR023174; PDEase_CS. DR Gene3D; G3DSA:1.10.1300.10; PDEase_catalytic_dom; 1. DR Pfam; PF00233; PDEase_I; 1. DR PRINTS; PR00387; PDIESTERASE1. DR SMART; SM00471; HDc; 1. DR PROSITE; PS00126; PDEASE_I; 1. PE 1: Evidence at protein level; KW 3D-structure; Hydrolase; Metal-binding. 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 //