ID   PDE7A_MOUSE             Reviewed;         456 AA.
AC   P70453; Q3TFY5; Q9ERB3;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   27-MAR-2024, entry version 167.
DE   RecName: Full=High affinity 3',5'-cyclic-AMP phosphodiesterase 7A {ECO:0000305};
DE            EC=3.1.4.53 {ECO:0000269|PubMed:11027622};
DE   AltName: Full=P2A {ECO:0000303|PubMed:8943082};
DE   AltName: Full=cAMP-specific phosphodiesterase 7A {ECO:0000305};
GN   Name=Pde7a {ECO:0000303|PubMed:11027622, ECO:0000312|MGI:MGI:1202402};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC   TISSUE=Skeletal muscle;
RX   PubMed=8943082; DOI=10.1073/pnas.93.24.14188;
RA   Bloom T.J., Beavo J.A.;
RT   "Identification and tissue-specific expression of PDE7 phosphodiesterase
RT   splice variants.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:14188-14192(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RC   TISSUE=Brain, and Testis;
RX   PubMed=11027622; DOI=10.1006/bbrc.2000.3613;
RA   Wang P., Wu P., Egan R.W., Billah M.M.;
RT   "Cloning, characterization, and tissue distribution of mouse
RT   phosphodiesterase 7A1.";
RL   Biochem. Biophys. Res. Commun. 276:1271-1277(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Amnion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: Hydrolyzes the second messenger cAMP, which is a key
CC       regulator of many important physiological processes (PubMed:11027622).
CC       May have a role in muscle signal transduction (By similarity).
CC       {ECO:0000250|UniProtKB:Q13946, ECO:0000269|PubMed:11027622}.
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:11027622};
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.2 uM for 3',5'-cyclic AMP {ECO:0000269|PubMed:11027622};
CC   -!- PATHWAY: Purine metabolism; 3',5'-cyclic AMP degradation; AMP from
CC       3',5'-cyclic AMP: step 1/1. {ECO:0000269|PubMed:11027622}.
CC   -!- SUBUNIT: Interacts with CBFA2T3. {ECO:0000250|UniProtKB:Q13946}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:Q13946}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC         Comment=Additional isoforms seem to exist.;
CC       Name=1; Synonyms=PDE7A2 {ECO:0000303|PubMed:8943082};
CC         IsoId=P70453-1; Sequence=Displayed;
CC       Name=2; Synonyms=PDE7A1 {ECO:0000303|PubMed:8943082};
CC         IsoId=P70453-2; Sequence=VSP_004594;
CC   -!- TISSUE SPECIFICITY: Widely expressed with highest levels in the
CC       skeletal muscle. {ECO:0000269|PubMed:8943082}.
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}.
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DR   EMBL; U68171; AAB08479.1; -; mRNA.
DR   EMBL; AY007702; AAG16295.1; -; mRNA.
DR   EMBL; AK168957; BAE40763.1; -; mRNA.
DR   CCDS; CCDS38398.1; -. [P70453-1]
DR   CCDS; CCDS50871.1; -. [P70453-2]
DR   RefSeq; NP_001116231.1; NM_001122759.2. [P70453-2]
DR   RefSeq; NP_032828.2; NM_008802.3. [P70453-1]
DR   AlphaFoldDB; P70453; -.
DR   SMR; P70453; -.
DR   BioGRID; 202081; 5.
DR   IntAct; P70453; 1.
DR   STRING; 10090.ENSMUSP00000096800; -.
DR   BindingDB; P70453; -.
DR   ChEMBL; CHEMBL2040702; -.
DR   iPTMnet; P70453; -.
DR   PhosphoSitePlus; P70453; -.
DR   EPD; P70453; -.
DR   MaxQB; P70453; -.
DR   PaxDb; 10090-ENSMUSP00000096800; -.
DR   ProteomicsDB; 288018; -. [P70453-1]
DR   ProteomicsDB; 288019; -. [P70453-2]
DR   Pumba; P70453; -.
DR   Antibodypedia; 4363; 254 antibodies from 28 providers.
DR   DNASU; 18583; -.
DR   Ensembl; ENSMUST00000091314.11; ENSMUSP00000088863.5; ENSMUSG00000069094.13. [P70453-1]
DR   Ensembl; ENSMUST00000099195.10; ENSMUSP00000096800.4; ENSMUSG00000069094.13. [P70453-2]
DR   GeneID; 18583; -.
DR   KEGG; mmu:18583; -.
DR   UCSC; uc008ort.3; mouse. [P70453-1]
DR   AGR; MGI:1202402; -.
DR   CTD; 5150; -.
DR   MGI; MGI:1202402; Pde7a.
DR   VEuPathDB; HostDB:ENSMUSG00000069094; -.
DR   eggNOG; KOG3689; Eukaryota.
DR   GeneTree; ENSGT00940000157658; -.
DR   HOGENOM; CLU_005940_6_5_1; -.
DR   InParanoid; P70453; -.
DR   OMA; RHTIHET; -.
DR   OrthoDB; 240889at2759; -.
DR   TreeFam; TF314638; -.
DR   BRENDA; 3.1.4.53; 3474.
DR   Reactome; R-MMU-418555; G alpha (s) signalling events.
DR   UniPathway; UPA00762; UER00747.
DR   BioGRID-ORCS; 18583; 3 hits in 78 CRISPR screens.
DR   ChiTaRS; Pde7a; mouse.
DR   PRO; PR:P70453; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; P70453; Protein.
DR   Bgee; ENSMUSG00000069094; Expressed in left lung lobe and 259 other cell types or tissues.
DR   ExpressionAtlas; P70453; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IDA:UniProtKB.
DR   GO; GO:0004112; F:cyclic-nucleotide phosphodiesterase activity; ISO:MGI.
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; IDA:UniProtKB.
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; IPR023088; PDEase.
DR   InterPro; IPR002073; PDEase_catalytic_dom.
DR   InterPro; IPR036971; PDEase_catalytic_dom_sf.
DR   InterPro; IPR023174; PDEase_CS.
DR   PANTHER; PTHR11347; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; 1.
DR   PANTHER; PTHR11347:SF96; HIGH AFFINITY CAMP-SPECIFIC 3',5'-CYCLIC PHOSPHODIESTERASE 7A; 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.
DR   Genevisible; P70453; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; cAMP; Cytoplasm; Hydrolase; Metal-binding;
KW   Reference proteome.
FT   CHAIN           1..456
FT                   /note="High affinity 3',5'-cyclic-AMP phosphodiesterase 7A"
FT                   /id="PRO_0000198834"
FT   DOMAIN          110..432
FT                   /note="PDEase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01192"
FT   ACT_SITE        186
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:O76083"
FT   BINDING         190
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q13946"
FT   BINDING         226
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q13946"
FT   BINDING         227
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q13946"
FT   BINDING         227
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q13946"
FT   BINDING         336
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q13946"
FT   VAR_SEQ         1..20
FT                   /note="MGITLIWCLALVLIKWITSK -> MEVCYQLPVLPLDRPVPQHVLSRRGAIS
FT                   FSSSSALFGCPHPRQLSQ (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:11027622"
FT                   /id="VSP_004594"
FT   CONFLICT        407
FT                   /note="D -> A (in Ref. 1; AAB08479)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   456 AA;  52486 MW;  0B84B62094BD9F6E CRC64;
     MGITLIWCLA LVLIKWITSK RRGAISYDSS DQTALYIRML GDVRVRSRAG FETERRGSHP
     YIDFRIFHSQ SDIEASVSAR NIRRLLSFQR YLRSSRVFRG ATVCSSLDIL DEDYNGQAKC
     MLEKVGNWNF DIFLFDRLTN GNSLVSLTFH LFSLHGLIEY FHLDMVKLRR FLVMIQEDYH
     SQNPYHNAVH AADVTQAMHC YLKEPKLASS VTPWDILLSL IAAATHDLDH PGVNQPFLIK
     TNHYLATLYK NSSVLENHHW RSAVGLLRES GLFSHLPLES RQEMEAQIGA LILATDISRQ
     NEYLSLFRSH LDKGDLHLDD GRHRHLVLQM ALKCADICNP CRNWELSKQW SEKVTEEFFH
     QGDIEKKYHL GVSPLCDRQT ESIANIQIGF MTYLVEPLFT EWARFSDTRL SQTMLGHVGL
     NKASWKGLQR QQPSSEDANA AFELNSQLLT QENRLS
//