PDE4C_HUMAN
ID PDE4C_HUMAN Reviewed; 712 AA.
AC Q08493; B3KTC4; Q9UN44; Q9UN45; Q9UN46; Q9UPJ6;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-MAR-2002, sequence version 2.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=cAMP-specific 3',5'-cyclic phosphodiesterase 4C {ECO:0000305};
DE EC=3.1.4.53 {ECO:0000269|PubMed:7843419};
DE AltName: Full=DPDE1;
DE AltName: Full=PDE21;
GN Name=PDE4C {ECO:0000312|HGNC:HGNC:8782}; Synonyms=DPDE1;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PDE4C1), TISSUE SPECIFICITY, FUNCTION,
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Substantia nigra;
RX PubMed=7843419; DOI=10.1016/0014-5793(94)01460-i;
RA Engels P., Sullivan M., Mueller T., Luebbert H.;
RT "Molecular cloning and functional expression in yeast of a human cAMP-
RT specific phosphodiesterase subtype (PDE IV-C).";
RL FEBS Lett. 358:305-310(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS PDE4C1; PDE4C2 AND PDE4C3).
RX PubMed=10574328; DOI=10.1016/s0898-6568(99)00037-6;
RA Sullivan M., Olsen A.S., Houslay M.D.;
RT "Genomic organisation of the human cyclic AMP-specific phosphodiesterase
RT PDE4C gene and its chromosomal localisation to 19p13.1, between RAB3A and
RT JUND.";
RL Cell. Signal. 11:735-742(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM PDE4C1).
RC TISSUE=Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 462-712.
RX PubMed=8413254; DOI=10.1128/mcb.13.10.6558-6571.1993;
RA Bolger G., Michaeli T., Martins T., St John T., Steiner B., Rodgers L.,
RA Riggs M., Wigler M., Ferguson K.;
RT "A family of human phosphodiesterases homologous to the dunce learning and
RT memory gene product of Drosophila melanogaster are potential targets for
RT antidepressant drugs.";
RL Mol. Cell. Biol. 13:6558-6571(1993).
RN [7] {ECO:0007744|PDB:2QYM}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 306-663 IN COMPLEX WITH ZINC AND
RP MAGNESIUM, FUNCTION, AND COFACTOR.
RX PubMed=17727341; DOI=10.1042/bj20070970;
RA Wang H., Peng M.-S., Chen Y., Geng J., Robinson H., Houslay M.D., Cai J.,
RA Ke H.;
RT "Structures of the four subfamilies of phosphodiesterase-4 provide insight
RT into the selectivity of their inhibitors.";
RL Biochem. J. 408:193-201(2007).
CC -!- FUNCTION: Hydrolyzes the second messenger cAMP, which is a key
CC regulator of many important physiological processes.
CC {ECO:0000269|PubMed:17727341, ECO:0000269|PubMed:7843419}.
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:0000269|PubMed:7843419};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25278;
CC Evidence={ECO:0000305|PubMed:7843419};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:17727341};
CC Note=Binds 2 divalent metal cations per subunit. Site 1 may
CC preferentially bind zinc ions. {ECO:0000269|PubMed:17727341};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:17727341};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q07343};
CC Note=Binds 2 divalent metal cations per subunit (PubMed:17727341). Site
CC 2 has a preference for magnesium and/or manganese ions (By similarity).
CC {ECO:0000250|UniProtKB:Q07343, ECO:0000269|PubMed:17727341};
CC -!- ACTIVITY REGULATION: Inhibited by rolipram.
CC {ECO:0000269|PubMed:7843419}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.5 uM for 3',5'-cyclic AMP {ECO:0000269|PubMed:7843419};
CC Vmax=37 nmol/min/mg enzyme {ECO:0000269|PubMed:7843419};
CC -!- PATHWAY: Purine metabolism; 3',5'-cyclic AMP degradation; AMP from
CC 3',5'-cyclic AMP: step 1/1. {ECO:0000305|PubMed:7843419}.
CC -!- SUBUNIT: Part of a complex containing AKAP5, ADCY5, ADCY6 and PKD2.
CC {ECO:0000250|UniProtKB:Q3UEI1}.
CC -!- INTERACTION:
CC Q08493-2; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-12169289, EBI-742054;
CC Q08493-2; O15499: GSC2; NbExp=3; IntAct=EBI-12169289, EBI-19954058;
CC Q08493-2; P26718: KLRK1; NbExp=3; IntAct=EBI-12169289, EBI-458344;
CC Q08493-2; P50221: MEOX1; NbExp=3; IntAct=EBI-12169289, EBI-2864512;
CC Q08493-2; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-12169289, EBI-16439278;
CC Q08493-2; Q9UJX0: OSGIN1; NbExp=3; IntAct=EBI-12169289, EBI-9057006;
CC Q08493-2; P26367: PAX6; NbExp=3; IntAct=EBI-12169289, EBI-747278;
CC Q08493-2; P30626: SRI; NbExp=3; IntAct=EBI-12169289, EBI-750459;
CC Q08493-2; P59817: ZNF280A; NbExp=3; IntAct=EBI-12169289, EBI-8489342;
CC Q08493-3; P30626: SRI; NbExp=3; IntAct=EBI-10225541, EBI-750459;
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium
CC {ECO:0000250|UniProtKB:Q3UEI1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=PDE4C1;
CC IsoId=Q08493-1; Sequence=Displayed;
CC Name=PDE4C2;
CC IsoId=Q08493-2; Sequence=VSP_004575;
CC Name=PDE4C3;
CC IsoId=Q08493-3; Sequence=VSP_004574;
CC Name=PDE4C4;
CC IsoId=Q08493-4; Sequence=Not described;
CC Name=PDE4C5;
CC IsoId=Q08493-5; Sequence=Not described;
CC Name=PDE4C6;
CC IsoId=Q08493-6; Sequence=Not described;
CC Name=PDE4C7;
CC IsoId=Q08493-7; Sequence=Not described;
CC -!- TISSUE SPECIFICITY: Expressed in various tissues but not in cells of
CC the immune system. {ECO:0000269|PubMed:7843419}.
CC -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family.
CC PDE4 subfamily. {ECO:0000305}.
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DR EMBL; Z46632; CAA86601.1; -; mRNA.
DR EMBL; AF157816; AAD47053.1; -; Genomic_DNA.
DR EMBL; AF157811; AAD47053.1; JOINED; Genomic_DNA.
DR EMBL; AF157814; AAD47053.1; JOINED; Genomic_DNA.
DR EMBL; AF157815; AAD47053.1; JOINED; Genomic_DNA.
DR EMBL; AF157816; AAD47054.1; -; Genomic_DNA.
DR EMBL; AF157812; AAD47054.1; JOINED; Genomic_DNA.
DR EMBL; AF157814; AAD47054.1; JOINED; Genomic_DNA.
DR EMBL; AF157815; AAD47054.1; JOINED; Genomic_DNA.
DR EMBL; AF157816; AAD47055.1; -; Genomic_DNA.
DR EMBL; AF157814; AAD47055.1; JOINED; Genomic_DNA.
DR EMBL; AF157815; AAD47055.1; JOINED; Genomic_DNA.
DR EMBL; AK095384; BAG53036.1; -; mRNA.
DR EMBL; AC005759; AAC83047.1; -; Genomic_DNA.
DR EMBL; CH471106; EAW84677.1; -; Genomic_DNA.
DR EMBL; L20968; AAA03591.1; -; mRNA.
DR CCDS; CCDS12373.1; -. [Q08493-1]
DR CCDS; CCDS42523.1; -. [Q08493-3]
DR CCDS; CCDS46016.1; -. [Q08493-2]
DR PIR; S71626; S71626.
DR RefSeq; NP_000914.2; NM_000923.5. [Q08493-1]
DR RefSeq; NP_001092288.1; NM_001098818.3. [Q08493-3]
DR RefSeq; NP_001092289.1; NM_001098819.3. [Q08493-2]
DR RefSeq; NP_001317101.1; NM_001330172.1. [Q08493-1]
DR RefSeq; XP_011526358.1; XM_011528056.2. [Q08493-2]
DR PDB; 2QYM; X-ray; 1.90 A; A=306-663.
DR PDBsum; 2QYM; -.
DR AlphaFoldDB; Q08493; -.
DR SMR; Q08493; -.
DR BioGRID; 111169; 9.
DR IntAct; Q08493; 9.
DR STRING; 9606.ENSP00000347689; -.
DR BindingDB; Q08493; -.
DR ChEMBL; CHEMBL291; -.
DR DrugBank; DB01427; Amrinone.
DR DrugBank; DB00201; Caffeine.
DR DrugBank; DB05219; Crisaborole.
DR DrugBank; DB00651; Dyphylline.
DR DrugBank; DB06246; Exisulind.
DR DrugBank; DB05266; Ibudilast.
DR DrugBank; DB01088; Iloprost.
DR DrugBank; DB01791; Piclamilast.
DR DrugBank; DB01656; Roflumilast.
DR DrugBank; DB09283; Trapidil.
DR DrugCentral; Q08493; -.
DR GuidetoPHARMACOLOGY; 1302; -.
DR GlyGen; Q08493; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q08493; -.
DR PhosphoSitePlus; Q08493; -.
DR BioMuta; PDE4C; -.
DR DMDM; 20141263; -.
DR EPD; Q08493; -.
DR jPOST; Q08493; -.
DR MassIVE; Q08493; -.
DR MaxQB; Q08493; -.
DR PaxDb; Q08493; -.
DR PeptideAtlas; Q08493; -.
DR PRIDE; Q08493; -.
DR ProteomicsDB; 58615; -. [Q08493-1]
DR ProteomicsDB; 58616; -. [Q08493-2]
DR ProteomicsDB; 58617; -. [Q08493-3]
DR Antibodypedia; 27961; 226 antibodies from 31 providers.
DR DNASU; 5143; -.
DR Ensembl; ENST00000262805.16; ENSP00000262805.10; ENSG00000105650.22. [Q08493-3]
DR Ensembl; ENST00000447275.7; ENSP00000402091.1; ENSG00000105650.22. [Q08493-2]
DR Ensembl; ENST00000594465.7; ENSP00000470210.1; ENSG00000105650.22. [Q08493-1]
DR Ensembl; ENST00000594617.7; ENSP00000469696.1; ENSG00000105650.22. [Q08493-1]
DR GeneID; 5143; -.
DR KEGG; hsa:5143; -.
DR MANE-Select; ENST00000262805.17; ENSP00000262805.10; NM_001098818.4; NP_001092288.1. [Q08493-3]
DR UCSC; uc002nii.5; human. [Q08493-1]
DR CTD; 5143; -.
DR DisGeNET; 5143; -.
DR GeneCards; PDE4C; -.
DR HGNC; HGNC:8782; PDE4C.
DR HPA; ENSG00000105650; Tissue enhanced (tongue).
DR MIM; 600128; gene.
DR neXtProt; NX_Q08493; -.
DR OpenTargets; ENSG00000105650; -.
DR PharmGKB; PA264; -.
DR VEuPathDB; HostDB:ENSG00000105650; -.
DR eggNOG; KOG3689; Eukaryota.
DR GeneTree; ENSGT00940000162285; -.
DR HOGENOM; CLU_005940_5_3_1; -.
DR OMA; HMNYLAD; -.
DR OrthoDB; 904682at2759; -.
DR PhylomeDB; Q08493; -.
DR TreeFam; TF314638; -.
DR BRENDA; 3.1.4.53; 2681.
DR PathwayCommons; Q08493; -.
DR Reactome; R-HSA-180024; DARPP-32 events.
DR Reactome; R-HSA-418555; G alpha (s) signalling events.
DR SignaLink; Q08493; -.
DR SIGNOR; Q08493; -.
DR UniPathway; UPA00762; UER00747.
DR BioGRID-ORCS; 5143; 25 hits in 1067 CRISPR screens.
DR ChiTaRS; PDE4C; human.
DR EvolutionaryTrace; Q08493; -.
DR GeneWiki; PDE4C; -.
DR GenomeRNAi; 5143; -.
DR Pharos; Q08493; Tclin.
DR PRO; PR:Q08493; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q08493; protein.
DR Bgee; ENSG00000105650; Expressed in apex of heart and 95 other tissues.
DR ExpressionAtlas; Q08493; baseline and differential.
DR Genevisible; Q08493; HS.
DR GO; GO:0005929; C:cilium; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IBA:GO_Central.
DR GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IDA:UniProtKB.
DR GO; GO:0004114; F:3',5'-cyclic-nucleotide phosphodiesterase activity; IBA:GO_Central.
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; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; cAMP; Cell projection; Cilium;
KW Hydrolase; Manganese; Metal-binding; Phosphoprotein; Reference proteome;
KW Zinc.
FT CHAIN 1..712
FT /note="cAMP-specific 3',5'-cyclic phosphodiesterase 4C"
FT /id="PRO_0000198811"
FT DOMAIN 312..641
FT /note="PDEase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01192"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 45..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 636..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 664..712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..680
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 388
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q07343"
FT BINDING 388
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /evidence="ECO:0000250|UniProtKB:Q08499"
FT BINDING 388
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q07343"
FT BINDING 392
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q07343"
FT BINDING 392
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17727341,
FT ECO:0007744|PDB:2QYM"
FT BINDING 428
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17727341,
FT ECO:0007744|PDB:2QYM"
FT BINDING 429
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q07343"
FT BINDING 429
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:17727341,
FT ECO:0007744|PDB:2QYM"
FT BINDING 429
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q07343"
FT BINDING 429
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17727341,
FT ECO:0007744|PDB:2QYM"
FT BINDING 429
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q07343"
FT BINDING 546
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q07343"
FT BINDING 546
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17727341,
FT ECO:0007744|PDB:2QYM"
FT BINDING 597
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /evidence="ECO:0000250|UniProtKB:Q08499"
FT BINDING 597
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q07343"
FT BINDING 600
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /evidence="ECO:0000250|UniProtKB:Q08499"
FT BINDING 600
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q07343"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UEI1"
FT MOD_RES 641
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UEI1"
FT VAR_SEQ 1..106
FT /note="Missing (in isoform PDE4C2)"
FT /evidence="ECO:0000305"
FT /id="VSP_004575"
FT VAR_SEQ 1..81
FT /note="MENLGVGEGAEACSRLSRSRGRHSMTRAPKHLWRQPRRPIRIQQRFYSDPDK
FT SAGCRERDLSPRPELRKSRLSWPVSSCRR -> MQGPPAPAPVPGPGSPRGSPRGSPGL
FT FRKLLVNQSIRLQRRFTVAHPLC (in isoform PDE4C3)"
FT /evidence="ECO:0000305"
FT /id="VSP_004574"
FT VARIANT 131
FT /note="S -> L (in dbSNP:rs10413646)"
FT /id="VAR_050473"
FT VARIANT 289
FT /note="R -> Q (in dbSNP:rs34503849)"
FT /id="VAR_050474"
FT VARIANT 344
FT /note="R -> Q (in dbSNP:rs2229228)"
FT /id="VAR_034374"
FT VARIANT 344
FT /note="R -> W (in dbSNP:rs11879710)"
FT /id="VAR_061497"
FT CONFLICT 204
FT /note="K -> N (in Ref. 2; AAD47053/AAD47054)"
FT /evidence="ECO:0000305"
FT CONFLICT 211
FT /note="D -> Y (in Ref. 2; AAD47053/AAD47054)"
FT /evidence="ECO:0000305"
FT CONFLICT 339..340
FT /note="EL -> DV (in Ref. 1; CAA86601)"
FT /evidence="ECO:0000305"
FT CONFLICT 444..446
FT /note="NSE -> K (in Ref. 4; AAC83047)"
FT /evidence="ECO:0000305"
FT CONFLICT 446..447
FT /note="EL -> DV (in Ref. 1; CAA86601)"
FT /evidence="ECO:0000305"
FT HELIX 317..323
FT /evidence="ECO:0007829|PDB:2QYM"
FT HELIX 324..326
FT /evidence="ECO:0007829|PDB:2QYM"
FT HELIX 334..340
FT /evidence="ECO:0007829|PDB:2QYM"
FT HELIX 345..356
FT /evidence="ECO:0007829|PDB:2QYM"
FT HELIX 359..362
FT /evidence="ECO:0007829|PDB:2QYM"
FT HELIX 367..379
FT /evidence="ECO:0007829|PDB:2QYM"
FT STRAND 385..389
FT /evidence="ECO:0007829|PDB:2QYM"
FT HELIX 390..404
FT /evidence="ECO:0007829|PDB:2QYM"
FT HELIX 407..409
FT /evidence="ECO:0007829|PDB:2QYM"
FT TURN 410..412
FT /evidence="ECO:0007829|PDB:2QYM"
FT HELIX 415..427
FT /evidence="ECO:0007829|PDB:2QYM"
FT TURN 428..431
FT /evidence="ECO:0007829|PDB:2QYM"
FT HELIX 435..437
FT /evidence="ECO:0007829|PDB:2QYM"
FT HELIX 456..467
FT /evidence="ECO:0007829|PDB:2QYM"
FT HELIX 468..470
FT /evidence="ECO:0007829|PDB:2QYM"
FT TURN 476..479
FT /evidence="ECO:0007829|PDB:2QYM"
FT HELIX 482..497
FT /evidence="ECO:0007829|PDB:2QYM"
FT HELIX 501..503
FT /evidence="ECO:0007829|PDB:2QYM"
FT HELIX 504..516
FT /evidence="ECO:0007829|PDB:2QYM"
FT HELIX 531..546
FT /evidence="ECO:0007829|PDB:2QYM"
FT HELIX 549..551
FT /evidence="ECO:0007829|PDB:2QYM"
FT HELIX 554..569
FT /evidence="ECO:0007829|PDB:2QYM"
FT HELIX 600..603
FT /evidence="ECO:0007829|PDB:2QYM"
FT HELIX 605..616
FT /evidence="ECO:0007829|PDB:2QYM"
FT TURN 617..620
FT /evidence="ECO:0007829|PDB:2QYM"
FT HELIX 621..630
FT /evidence="ECO:0007829|PDB:2QYM"
SQ SEQUENCE 712 AA; 79902 MW; 1932116C9CE0322C CRC64;
MENLGVGEGA EACSRLSRSR GRHSMTRAPK HLWRQPRRPI RIQQRFYSDP DKSAGCRERD
LSPRPELRKS RLSWPVSSCR RFDLENGLSC GRRALDPQSS PGLGRIMQAP VPHSQRRESF
LYRSDSDYEL SPKAMSRNSS VASDLHGEDM IVTPFAQVLA SLRTVRSNVA ALARQQCLGA
AKQGPVGNPS SSNQLPPAED TGQKLALETL DELDWCLDQL ETLQTRHSVG EMASNKFKRI
LNRELTHLSE TSRSGNQVSE YISRTFLDQQ TEVELPKVTA EEAPQPMSRI SGLHGLCHSA
SLSSATVPRF GVQTDQEEQL AKELEDTNKW GLDVFKVAEL SGNRPLTAII FSIFQERDLL
KTFQIPADTL ATYLLMLEGH YHANVAYHNS LHAADVAQST HVLLATPALE AVFTDLEILA
ALFASAIHDV DHPGVSNQFL INTNSELALM YNDASVLENH HLAVGFKLLQ AENCDIFQNL
SAKQRLSLRR MVIDMVLATD MSKHMNLLAD LKTMVETKKV TSLGVLLLDN YSDRIQVLQN
LVHCADLSNP TKPLPLYRQW TDRIMAEFFQ QGDRERESGL DISPMCDKHT ASVEKSQVGF
IDYIAHPLWE TWADLVHPDA QDLLDTLEDN REWYQSKIPR SPSDLTNPER DGPDRFQFEL
TLEEAEEEDE EEEEEGEETA LAKEALELPD TELLSPEAGP DPGDLPLDNQ RT
