PDE7A_RAT
ID PDE7A_RAT Reviewed; 426 AA.
AC O08593;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=High affinity cAMP-specific 3',5'-cyclic phosphodiesterase 7A;
DE EC=3.1.4.53 {ECO:0000250|UniProtKB:Q13946};
DE AltName: Full=Rolipram-insensitive phosphodiesterase type 7;
DE Flags: Fragment;
GN Name=Pde7a;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=9515162; DOI=10.1007/bf02737807;
RA Hoffmann R., Abdel'Al S., Engels P.;
RT "Differential distribution of rat PDE-7 mRNA in embryonic and adult rat
RT brain.";
RL Cell Biochem. Biophys. 28:103-113(1998).
CC -!- FUNCTION: Hydrolyzes the second messenger cAMP, which is a key
CC regulator of many important physiological processes. May have a role in
CC muscle signal transduction. {ECO:0000250|UniProtKB:Q13946}.
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:Q13946};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250|UniProtKB:Q13946};
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:0000250|UniProtKB:Q13946};
CC -!- PATHWAY: Purine metabolism; 3',5'-cyclic AMP degradation; AMP from
CC 3',5'-cyclic AMP: step 1/1. {ECO:0000250|UniProtKB:Q13946}.
CC -!- SUBUNIT: Interacts with CBFA2T3. {ECO:0000250|UniProtKB:Q13946}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q13946}.
CC -!- DOMAIN: Composed of a C-terminal catalytic domain containing two
CC putative divalent metal sites and an N-terminal regulatory domain.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family.
CC PDE7 subfamily. {ECO:0000305}.
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; U77880; AAB51234.1; -; mRNA.
DR AlphaFoldDB; O08593; -.
DR SMR; O08593; -.
DR STRING; 10116.ENSRNOP00000060777; -.
DR PaxDb; O08593; -.
DR UCSC; RGD:68391; rat.
DR RGD; 68391; Pde7a.
DR eggNOG; KOG3689; Eukaryota.
DR InParanoid; O08593; -.
DR Reactome; R-RNO-418555; G alpha (s) signalling events.
DR UniPathway; UPA00762; UER00747.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; ISO:RGD.
DR GO; GO:0004114; F:3',5'-cyclic-nucleotide phosphodiesterase activity; IBA:GO_Central.
DR GO; GO:0004112; F:cyclic-nucleotide phosphodiesterase activity; IMP:RGD.
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:0019933; P:cAMP-mediated signaling; IEP:RGD.
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; IPR023088; PDEase.
DR InterPro; IPR002073; PDEase_catalytic_dom.
DR InterPro; IPR036971; PDEase_catalytic_dom_sf.
DR InterPro; IPR023174; PDEase_CS.
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; Cytoplasm; Hydrolase; Metal-binding; Reference proteome.
FT CHAIN <1..426
FT /note="High affinity cAMP-specific 3',5'-cyclic
FT phosphodiesterase 7A"
FT /id="PRO_0000198835"
FT DOMAIN 80..402
FT /note="PDEase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01192"
FT ACT_SITE 156
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O76083"
FT BINDING 160
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q13946"
FT BINDING 196
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q13946"
FT BINDING 197
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q13946"
FT BINDING 197
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q13946"
FT BINDING 306
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q13946"
FT NON_TER 1
SQ SEQUENCE 426 AA; 49274 MW; 129BDC01C9351D26 CRC64;
DQTALYIRML GDVRVRSRAG FETERRGSHP YIDFRIFHAQ SEIEASVSAR NIRRLLSFQR
YLRSSRFFRG ATVCRSLNIL DEDYNGQAKC MLEKVGNWNF DIFLFDRLTN GNSLVSLTFH
LFSLHGLIEY FHLDMVKLRR FLVMIQEDYH SQNPYHNAVH AADVTQAMHC YLKEPKLANS
VTPWDILLSL IAAATHDLDH PGVNQPFLIK TNHYLATLYK NTSVLENHHW RSAVGLLRES
GLFSHLPLES RHEMEAQIGA LILATDISRQ NEYLSLFRSH LDKGDLHLDD GRHRHLVLQM
ALKCADICNP CRNWELSKQW SEKVTEEFFH QGDIEKKYHL GVSPLCDRQT ESIANIQIGF
MTYLQEPLFT EWARFSDTRL SQTMLGHVGL NKASWKGLQR QQPSSEDASA AFELNSQLLT
QENRLS
