ID O43850_HUMAN Unreviewed; 518 AA.
AC O43850;
DT 01-JUN-1998, integrated into UniProtKB/TrEMBL.
DT 01-JUN-1998, sequence version 1.
DT 22-FEB-2023, entry version 122.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
DE Flags: Fragment;
GN Name=PDE4C {ECO:0000313|EMBL:AAC83051.1};
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:AAB96877.1};
RN [1] {ECO:0000313|EMBL:AAB96877.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Testis {ECO:0000313|EMBL:AAB96877.1};
RX PubMed=9349724; DOI=10.1016/S0167-4781(97)00080-8;
RA Obernolte R., Ratzliff J., Baecker P.A., Daniels D.V., Zuppan P.,
RA Jarnagin K., Shelton E.R.;
RT "Multiple splice variants of phosphodiesterase PDE4C cloned from human lung
RT and testis.";
RL Biochim. Biophys. Acta 1353:287-297(1997).
RN [2] {ECO:0000313|EMBL:AAC83051.1}
RP NUCLEOTIDE SEQUENCE.
RA Lamerdin J.E., McCready P.M., Skowronski E., Viswanathan V.,
RA Burkhart-Schultz K., Gordon L., Dias J., Ramirez M., Stilwagen S., Phan H.,
RA Velasco N., Do L., Regala W., Terry A., Garnes J., Danganan L.,
RA Poundstone P., Christensen M., Georgescu A., Avila J., Liu S., Attix C.,
RA Andreise T., Trankheim M., Amico-Keller G., Coefield J., Duarte S.,
RA Lucas S., Bruce R., Thomas P., Quan G., Kronmiller B., Arellano A.,
RA Saunders C., Ow D., Nolan M., Trong S., Kobayashi A., Olsen A.S.,
RA Carrano A.V.;
RT "Sequence analysis of an ~600 kb region in 19p13.1 between JAK3 and
RT PDE4C.";
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
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:ARBA00033681};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25278;
CC Evidence={ECO:0000256|ARBA:ARBA00033681};
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 PDE4 subfamily. {ECO:0000256|ARBA:ARBA00009517}.
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DR EMBL; U66348; AAB96877.1; -; mRNA.
DR EMBL; AC005759; AAC83051.1; -; Genomic_DNA.
DR AlphaFoldDB; O43850; -.
DR MaxQB; O43850; -.
DR PeptideAtlas; O43850; -.
DR ProteomicsDB; 49202; -.
DR UniPathway; UPA00762; UER00747.
DR ChiTaRS; PDE4C; human.
DR GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0004114; F:3',5'-cyclic-nucleotide phosphodiesterase activity; NAS:UniProtKB.
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; 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain; 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 PANTHER; PTHR11347:SF135; CAMP-SPECIFIC 3',5'-CYCLIC PHOSPHODIESTERASE 4C; 1.
DR PANTHER; PTHR11347; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; 1.
DR Pfam; PF18100; PDE4_UCR; 1.
DR Pfam; PF00233; PDEase_I; 1.
DR PRINTS; PR00387; PDIESTERASE1.
DR SMART; SM00471; HDc; 1.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 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}.
FT DOMAIN 118..447
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT REGION 8..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 470..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..486
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 194
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT BINDING 194..198
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 198
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 234
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 235
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 235
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 235
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 352
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 352
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 403
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAB96877.1"
SQ SEQUENCE 518 AA; 58116 MW; DDDC5BE289C1192C CRC64;
PLRIRPLLPT AYHLLPTGPG QSADRSEQRG GPCPPAMPRS SQFKRILNRE LTHLSETSRS
GNQVSEYISR TFLDQQTEVE LPKVTAEEAP QPMSRISGLH GLCHSASLSS ATVPRFGVQT
DQEEQLAKEL EDTNKWGLDV FKVAELSGNR PLTAIIFSIF QERDLLKTFQ IPADTLATYL
LMLEGHYHAN VAYHNSLHAA DVAQSTHVLL ATPALEAVFT DLEILAALFA SAIHDVDHPG
VSNQFLINTN SELALMYNDA SVLENHHLAV GFKLLQAENC DIFQNLSAKQ RLSLRRMVID
MVLATDMSKH MNLLADLKTM VETKKVTSLG VLLLDNYSDR IQVLQNLVHC ADLSNPTKPL
PLYRQWTDRI MAEFFQQGDR ERESGLDISP MCDKHTASVE KSQVGFIDYI AHPLWETWAD
LVHPDAQDLL DTLEDNREWY QSKIPRSPSD LTNPERDGPD RFQFELTLEE AEEEDEEEEE
EGEETALAKE ALELPDTELL SPEAGPDPGD LPLDNQRT
//
