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P70453 (PDE7A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
High affinity cAMP-specific 3',5'-cyclic phosphodiesterase 7A

EC=3.1.4.53
Alternative name(s):
P2A
Gene names
Name:Pde7a
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length456 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. May have a role in muscle signal transduction By similarity.

Catalytic activity

Adenosine 3',5'-cyclic phosphate + H2O = adenosine 5'-phosphate.

Cofactor

Binds 2 divalent metal cations per subunit. Site 1 may preferentially bind zinc ions, while site 2 has a preference for magnesium and/or manganese ions By similarity.

Enzyme regulation

Insensitive to all selective PDE inhibitors.

Pathway

Purine metabolism; 3',5'-cyclic AMP degradation; AMP from 3',5'-cyclic AMP: step 1/1.

Subunit structure

Interacts with CBFA2T3 By similarity.

Tissue specificity

Widely expressed with highest levels in the skeletal muscle.

Domain

Composed of a C-terminal catalytic domain containing two putative divalent metal sites and an N-terminal regulatory domain.

Sequence similarities

Belongs to the cyclic nucleotide phosphodiesterase family. PDE7 subfamily.

Ontologies

Keywords
   Coding sequence diversityAlternative splicing
   LigandcAMP
Metal-binding
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcAMP catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

signal transduction

Inferred from electronic annotation. Source: InterPro

   Molecular_function3',5'-cyclic-AMP phosphodiesterase activity

Inferred from sequence orthology Ref.1. Source: MGI

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: P70453-1)

Also known as: PDE7A2;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P70453-2)

Also known as: PDE7A1;

The sequence of this isoform differs from the canonical sequence as follows:
     1-20: MGITLIWCLALVLIKWITSK → MEVCYQLPVLPLDRPVPQHVLSRRGAISFSSSSALFGCPHPRQLSQ

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 456456High affinity cAMP-specific 3',5'-cyclic phosphodiesterase 7A
PRO_0000198834

Regions

Region161 – 425265Catalytic By similarity

Sites

Active site1861Proton donor By similarity
Metal binding1901Divalent metal cation 1 By similarity
Metal binding2261Divalent metal cation 1 By similarity
Metal binding2271Divalent metal cation 1 By similarity
Metal binding2271Divalent metal cation 2 By similarity
Metal binding3361Divalent metal cation 1 By similarity

Natural variations

Alternative sequence1 – 2020MGITL…WITSK → MEVCYQLPVLPLDRPVPQHV LSRRGAISFSSSSALFGCPH PRQLSQ in isoform 2.
VSP_004594

Experimental info

Sequence conflict4071D → A in AAB08479. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (PDE7A2) [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 0B84B62094BD9F6E

FASTA45652,486
        10         20         30         40         50         60 
MGITLIWCLA LVLIKWITSK RRGAISYDSS DQTALYIRML GDVRVRSRAG FETERRGSHP 

        70         80         90        100        110        120 
YIDFRIFHSQ SDIEASVSAR NIRRLLSFQR YLRSSRVFRG ATVCSSLDIL DEDYNGQAKC 

       130        140        150        160        170        180 
MLEKVGNWNF DIFLFDRLTN GNSLVSLTFH LFSLHGLIEY FHLDMVKLRR FLVMIQEDYH 

       190        200        210        220        230        240 
SQNPYHNAVH AADVTQAMHC YLKEPKLASS VTPWDILLSL IAAATHDLDH PGVNQPFLIK 

       250        260        270        280        290        300 
TNHYLATLYK NSSVLENHHW RSAVGLLRES GLFSHLPLES RQEMEAQIGA LILATDISRQ 

       310        320        330        340        350        360 
NEYLSLFRSH LDKGDLHLDD GRHRHLVLQM ALKCADICNP CRNWELSKQW SEKVTEEFFH 

       370        380        390        400        410        420 
QGDIEKKYHL GVSPLCDRQT ESIANIQIGF MTYLVEPLFT EWARFSDTRL SQTMLGHVGL 

       430        440        450 
NKASWKGLQR QQPSSEDANA AFELNSQLLT QENRLS 

« Hide

Isoform 2 (PDE7A1) [UniParc].

Checksum: E8470DD85BFF7714
Show »

FASTA48255,289

References

« Hide 'large scale' references
[1]"Identification and tissue-specific expression of PDE7 phosphodiesterase splice variants."
Bloom T.J., Beavo J.A.
Proc. Natl. Acad. Sci. U.S.A. 93:14188-14192(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Skeletal muscle.
[2]"Cloning, characterization, and tissue distribution of mouse phosphodiesterase 7A1."
Wang P., Wu P., Egan R.W., Billah M.M.
Biochem. Biophys. Res. Commun. 276:1271-1277(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Brain and Testis.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Amnion.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U68171 mRNA. Translation: AAB08479.1.
AY007702 mRNA. Translation: AAG16295.1.
AK168957 mRNA. Translation: BAE40763.1.
CCDSCCDS38398.1. [P70453-1]
CCDS50871.1. [P70453-2]
RefSeqNP_001116231.1. NM_001122759.2. [P70453-2]
NP_032828.2. NM_008802.3. [P70453-1]
UniGeneMm.355614.

3D structure databases

ProteinModelPortalP70453.
SMRP70453. Positions 113-430.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202081. 1 interaction.
IntActP70453. 1 interaction.

Chemistry

ChEMBLCHEMBL2040702.

PTM databases

PhosphoSiteP70453.

Proteomic databases

PRIDEP70453.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000091314; ENSMUSP00000088863; ENSMUSG00000069094. [P70453-1]
ENSMUST00000099195; ENSMUSP00000096800; ENSMUSG00000069094. [P70453-2]
GeneID18583.
KEGGmmu:18583.
UCSCuc008ort.2. mouse. [P70453-1]

Organism-specific databases

CTD5150.
MGIMGI:1202402. Pde7a.

Phylogenomic databases

eggNOGNOG300643.
GeneTreeENSGT00730000110321.
HOGENOMHOG000220881.
HOVERGENHBG053543.
KOK01120.
OMALCDRQTE.
OrthoDBEOG7M98G3.
TreeFamTF314638.

Enzyme and pathway databases

UniPathwayUPA00762; UER00747.

Gene expression databases

ArrayExpressP70453.
BgeeP70453.
CleanExMM_PDE7A.
GenevestigatorP70453.

Family and domain databases

Gene3D1.10.1300.10. 1 hit.
InterProIPR003607. HD/PDEase_dom.
IPR023088. PDEase.
IPR002073. PDEase_catalytic_dom.
IPR023174. PDEase_CS.
[Graphical view]
PfamPF00233. PDEase_I. 1 hit.
[Graphical view]
PRINTSPR00387. PDIESTERASE1.
SMARTSM00471. HDc. 1 hit.
[Graphical view]
PROSITEPS00126. PDEASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio294452.
PROP70453.
SOURCESearch...

Entry information

Entry namePDE7A_MOUSE
AccessionPrimary (citable) accession number: P70453
Secondary accession number(s): Q3TFY5, Q9ERB3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot