PDE7A_MOUSE
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 03-AUG-2022, entry version 158.
DE RecName: Full=High affinity cAMP-specific 3',5'-cyclic phosphodiesterase 7A;
DE EC=3.1.4.53 {ECO:0000269|PubMed:11027622};
DE AltName: Full=P2A {ECO:0000303|PubMed:8943082};
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; P70453; -.
DR PRIDE; P70453; -.
DR ProteomicsDB; 288018; -. [P70453-1]
DR ProteomicsDB; 288019; -. [P70453-2]
DR Antibodypedia; 4363; 201 antibodies from 28 providers.
DR DNASU; 18583; -.
DR Ensembl; ENSMUST00000091314; ENSMUSP00000088863; ENSMUSG00000069094. [P70453-1]
DR Ensembl; ENSMUST00000099195; ENSMUSP00000096800; ENSMUSG00000069094. [P70453-2]
DR GeneID; 18583; -.
DR KEGG; mmu:18583; -.
DR UCSC; uc008ort.3; mouse. [P70453-1]
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; NENFHIA; -.
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 73 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 256 other tissues.
DR ExpressionAtlas; P70453; baseline and differential.
DR Genevisible; P70453; MM.
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:0004114; F:3',5'-cyclic-nucleotide phosphodiesterase activity; IBA:GO_Central.
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 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 1: Evidence at protein level;
KW Alternative splicing; cAMP; Cytoplasm; Hydrolase; Metal-binding;
KW Reference proteome.
FT CHAIN 1..456
FT /note="High affinity cAMP-specific 3',5'-cyclic
FT 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
