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Protein

High affinity cAMP-specific 3',5'-cyclic phosphodiesterase 7A

Gene

Pde7a

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -Experimental evidence at transcript leveli

Functioni

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).By similarity

Catalytic activityi

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

Cofactori

a divalent metal cationBy similarityNote: 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 regulationi

Insensitive to all selective PDE inhibitors.By similarity

Pathwayi: 3',5'-cyclic AMP degradation

This protein is involved in step 1 of the subpathway that synthesizes AMP from 3',5'-cyclic AMP.
Proteins known to be involved in this subpathway in this organism are:
  1. High affinity cAMP-specific 3',5'-cyclic phosphodiesterase 7A (Pde7a), cAMP-specific 3',5'-cyclic phosphodiesterase 4D (Pde4d), cAMP-specific 3',5'-cyclic phosphodiesterase 4A (Pde4a), cAMP-specific 3',5'-cyclic phosphodiesterase 4B (Pde4b), cAMP-specific 3',5'-cyclic phosphodiesterase 4C (Pde4c), cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A (Pde10a)
This subpathway is part of the pathway 3',5'-cyclic AMP degradation, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes AMP from 3',5'-cyclic AMP, the pathway 3',5'-cyclic AMP degradation and in Purine metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei156Proton donorBy similarity1
Metal bindingi160Divalent metal cation 1By similarity1
Metal bindingi196Divalent metal cation 1By similarity1
Metal bindingi197Divalent metal cation 1By similarity1
Metal bindingi197Divalent metal cation 2By similarity1
Metal bindingi306Divalent metal cation 1By similarity1

GO - Molecular functioni

  • 3',5'-cyclic-AMP phosphodiesterase activity Source: RGD
  • cyclic-nucleotide phosphodiesterase activity Source: RGD
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • cAMP catabolic process Source: UniProtKB-UniPathway
  • cAMP-mediated signaling Source: RGD

Keywordsi

Molecular functionHydrolase
LigandcAMP, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00762; UER00747

Names & Taxonomyi

Protein namesi
Recommended name:
High affinity cAMP-specific 3',5'-cyclic phosphodiesterase 7A (EC:3.1.4.53)
Alternative name(s):
Rolipram-insensitive phosphodiesterase type 7
Gene namesi
Name:Pde7a
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi68391 Pde7a

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000198835‹1 – 426High affinity cAMP-specific 3',5'-cyclic phosphodiesterase 7AAdd BLAST›426

Proteomic databases

PaxDbiO08593

Interactioni

Subunit structurei

Interacts with CBFA2T3.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000060777

Structurei

3D structure databases

ProteinModelPortaliO08593
SMRiO08593
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini80 – 402PDEasePROSITE-ProRule annotationAdd BLAST323

Domaini

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG3689 Eukaryota
ENOG410XRI7 LUCA
HOGENOMiHOG000220881
HOVERGENiHBG053543
InParanoidiO08593

Family and domain databases

CDDicd00077 HDc, 1 hit
Gene3Di1.10.1300.10, 1 hit
InterProiView protein in InterPro
IPR003607 HD/PDEase_dom
IPR023088 PDEase
IPR002073 PDEase_catalytic_dom
IPR036971 PDEase_catalytic_dom_sf
IPR023174 PDEase_CS
PfamiView protein in Pfam
PF00233 PDEase_I, 1 hit
PRINTSiPR00387 PDIESTERASE1
SMARTiView protein in SMART
SM00471 HDc, 1 hit
PROSITEiView protein in PROSITE
PS00126 PDEASE_I_1, 1 hit
PS51845 PDEASE_I_2, 1 hit

Sequencei

Sequence statusi: Fragment.

O08593-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
DQTALYIRML GDVRVRSRAG FETERRGSHP YIDFRIFHAQ SEIEASVSAR
60 70 80 90 100
NIRRLLSFQR YLRSSRFFRG ATVCRSLNIL DEDYNGQAKC MLEKVGNWNF
110 120 130 140 150
DIFLFDRLTN GNSLVSLTFH LFSLHGLIEY FHLDMVKLRR FLVMIQEDYH
160 170 180 190 200
SQNPYHNAVH AADVTQAMHC YLKEPKLANS VTPWDILLSL IAAATHDLDH
210 220 230 240 250
PGVNQPFLIK TNHYLATLYK NTSVLENHHW RSAVGLLRES GLFSHLPLES
260 270 280 290 300
RHEMEAQIGA LILATDISRQ NEYLSLFRSH LDKGDLHLDD GRHRHLVLQM
310 320 330 340 350
ALKCADICNP CRNWELSKQW SEKVTEEFFH QGDIEKKYHL GVSPLCDRQT
360 370 380 390 400
ESIANIQIGF MTYLQEPLFT EWARFSDTRL SQTMLGHVGL NKASWKGLQR
410 420
QQPSSEDASA AFELNSQLLT QENRLS
Length:426
Mass (Da):49,274
Last modified:July 1, 1997 - v1
Checksum:i129BDC01C9351D26
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U77880 mRNA Translation: AAB51234.1
UniGeneiRn.39142

Genome annotation databases

UCSCiRGD:68391 rat

Similar proteinsi

Entry informationi

Entry nameiPDE7A_RAT
AccessioniPrimary (citable) accession number: O08593
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 1, 1997
Last modified: May 23, 2018
This is version 112 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

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