ID   PDE4A_CAVPO             Reviewed;         117 AA.
AC   O89085;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=cAMP-specific 3',5'-cyclic phosphodiesterase 4A;
DE            EC=3.1.4.53 {ECO:0000250|UniProtKB:P27815};
DE   Flags: Fragment;
GN   Name=PDE4A;
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=9677330; DOI=10.1042/bj3330693;
RA   Sullivan M., Rena G., Begg F., Gordon L., Olsen A.S., Houslay M.D.;
RT   "Identification and characterization of the human homologue of the short
RT   PDE4A cAMP-specific phosphodiesterase 4A variant RD1 (PDE4A1) by analysis
RT   of the human HSPDE4A gene locus located at chromosome 19p13.2.";
RL   Biochem. J. 333:693-703(1998).
CC   -!- FUNCTION: Hydrolyzes the second messenger 3',5'-cyclic AMP (cAMP),
CC       which is a key regulator of many important physiological processes.
CC       {ECO:0000250|UniProtKB:P27815}.
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:0000250|UniProtKB:P27815};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25278;
CC         Evidence={ECO:0000250|UniProtKB:P27815};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P27815};
CC       Note=Binds 2 divalent metal cations per subunit. Site 1 may
CC       preferentially bind zinc ions. {ECO:0000250|UniProtKB:P27815};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P27815};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:Q07343};
CC       Note=Binds 2 divalent metal cations per subunit (By similarity). Site 2
CC       has a preference for magnesium and/or manganese ions (By similarity).
CC       {ECO:0000250|UniProtKB:P27815, ECO:0000250|UniProtKB:Q07343};
CC   -!- PATHWAY: Purine metabolism; 3',5'-cyclic AMP degradation; AMP from
CC       3',5'-cyclic AMP: step 1/1. {ECO:0000250|UniProtKB:P27815}.
CC   -!- SUBUNIT: Interacts with LYN (via SH3 domain). Interacts with ARRB2.
CC       {ECO:0000250|UniProtKB:P27815}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:P27815}. Membrane; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P27815}.
CC   -!- PTM: Proteolytically cleaved by CASP3. {ECO:0000250|UniProtKB:P27815}.
CC   -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family.
CC       PDE4 subfamily. {ECO:0000305}.
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DR   EMBL; U97588; AAC25683.1; -; mRNA.
DR   AlphaFoldDB; O89085; -.
DR   SMR; O89085; -.
DR   STRING; 10141.ENSCPOP00000014250; -.
DR   BindingDB; O89085; -.
DR   ChEMBL; CHEMBL2366459; -.
DR   DrugCentral; O89085; -.
DR   eggNOG; KOG3689; Eukaryota.
DR   InParanoid; O89085; -.
DR   UniPathway; UPA00762; UER00747.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006198; P:cAMP catabolic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR040844; PDE4_UCR.
DR   Pfam; PF18100; PDE4_UCR; 1.
DR   PROSITE; PS00014; ER_TARGET; 1.
PE   2: Evidence at transcript level;
KW   cAMP; Cytoplasm; Hydrolase; Membrane; Phosphoprotein; Reference proteome;
KW   Zinc.
FT   CHAIN           <1..>117
FT                   /note="cAMP-specific 3',5'-cyclic phosphodiesterase 4A"
FT                   /id="PRO_0000198805"
FT   REGION          42..79
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          78..>117
FT                   /note="Catalytic"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        48..62
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT   NON_TER         117
SQ   SEQUENCE   117 AA;  13503 MW;  87288E127BA6D008 CRC64;
     PWLVGWWDQF KRMLNRELTH LSEMSRSGNQ VSEYISTTFL DKQNEVEIPS PTMKDREPQE
     APRQRPCQQL PPPVPHLQPM SQITGVKRLS HNSGLNNASI PRFGVKTDQE ELLAQEL