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O54735

- PDE5A_RAT

UniProt

O54735 - PDE5A_RAT

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Protein

cGMP-specific 3',5'-cyclic phosphodiesterase

Gene
Pde5a, Pde5
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript leveli

Functioni

Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides. This phosphodiesterase catalyzes the specific hydrolysis of cGMP to 5'-GMP.

Catalytic activityi

Guanosine 3',5'-cyclic phosphate + H2O = guanosine 5'-phosphate.

Cofactori

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.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei571 – 5711Proton donor By similarity
Metal bindingi575 – 5751Divalent metal cation 1 By similarity
Metal bindingi611 – 6111Divalent metal cation 1 By similarity
Metal bindingi612 – 6121Divalent metal cation 1 By similarity
Metal bindingi612 – 6121Divalent metal cation 2 By similarity
Metal bindingi722 – 7221Divalent metal cation 1 By similarity
Binding sitei775 – 7751cGMP By similarity

GO - Molecular functioni

  1. 3',5'-cyclic-GMP phosphodiesterase activity Source: RGD
  2. cGMP binding Source: UniProtKB-KW
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. cGMP catabolic process Source: UniProtKB-UniPathway
  2. nervous system development Source: RGD
  3. positive regulation of apoptotic process Source: RGD
  4. positive regulation of chronic inflammatory response Source: RGD
  5. positive regulation of vasoconstriction Source: RGD
  6. regulation of the force of heart contraction Source: RGD
  7. response to hypoxia Source: RGD
  8. response to lipopolysaccharide Source: RGD
  9. response to testosterone Source: RGD
  10. short-term memory Source: RGD
  11. signal transduction Source: InterPro
  12. vasodilation Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

cGMP, cGMP-binding, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00763; UER00748.

Names & Taxonomyi

Protein namesi
Recommended name:
cGMP-specific 3',5'-cyclic phosphodiesterase (EC:3.1.4.35)
Alternative name(s):
cGMP-binding cGMP-specific phosphodiesterase
Short name:
CGB-PDE
Gene namesi
Name:Pde5a
Synonyms:Pde5
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi620995. Pde5a.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: RGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 833833cGMP-specific 3',5'-cyclic phosphodiesterasePRO_0000198825Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei60 – 601Phosphoserine Reviewed prediction

Post-translational modificationi

Phosphorylation is regulated by binding of cGMP to the two allosteric sites By similarity. Phosphorylation by PRKG1 leads to its activation By similarity.

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO54735.
PRIDEiO54735.

PTM databases

PhosphoSiteiO54735.

Expressioni

Gene expression databases

GenevestigatoriO54735.

Interactioni

Structurei

3D structure databases

ProteinModelPortaliO54735.
SMRiO54735. Positions 122-269, 493-818.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini122 – 272151GAF 1Add
BLAST
Domaini304 – 461158GAF 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni546 – 811266Catalytic By similarityAdd
BLAST

Domaini

Composed of a C-terminal catalytic domain containing two putative divalent metal sites and an N-terminal regulatory domain which contains two homologous allosteric cGMP-binding regions, A and B.

Sequence similaritiesi

Contains 2 GAF domains.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG270709.
HOGENOMiHOG000007068.
HOVERGENiHBG101207.
InParanoidiO54735.
KOiK13762.
PhylomeDBiO54735.

Family and domain databases

Gene3Di1.10.1300.10. 1 hit.
3.30.450.40. 2 hits.
InterProiIPR003018. GAF.
IPR029016. GAF_dom_like.
IPR003607. HD/PDEase_dom.
IPR023088. PDEase.
IPR002073. PDEase_catalytic_dom.
IPR023174. PDEase_CS.
[Graphical view]
PfamiPF01590. GAF. 2 hits.
PF00233. PDEase_I. 1 hit.
[Graphical view]
PRINTSiPR00387. PDIESTERASE1.
SMARTiSM00065. GAF. 2 hits.
SM00471. HDc. 1 hit.
[Graphical view]
SUPFAMiSSF55781. SSF55781. 2 hits.
PROSITEiPS00126. PDEASE_I. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform PDE5A2 (identifier: O54735-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MLPFGDKTRD MVNAWFSERV HNIPVCKEGI RAHTESCSCS LPQSPHADNT    50
TPGAPARKIS ASEFDRPLRP IVVKDSEGTV SFLSDSGKKE QMPLTSPRFD 100
SDEGDQCSRL LELVKDISSH LDVTALCHKI FLHIHGLISA DRYSLFLVCE 150
DSSKDKFLVS RLFDVAEGST LEEASNNCIR LEWNKGIVGH VAAFGEPLNI 200
KDAYEDPRFN AEVDQITGYK TQSILCMPIK NHREEVVGVA QAINKKSGNG 250
GTFTEKDEKD FAAYLAFCGI VLHNAQLYET SLLENKRNQV LLDLASLIFE 300
EQQSLEVILK KIAATIISFM QVQKCTIFIV DEDCPDSFSR VFQMEWEEVG 350
KSSEPLTREH DANKINYMYA QYVKNTMEPL NIPDVTKDNR FPWTNENMGH 400
INTHCIRSLL CTPIKNGKKN KVIGVCQLVN KMEEKTGKIK AFNQNDEQFL 450
EAFVIFCGLG IQNTQMYEAV ERAMAKQMVT LEVLSYHASA AEEETRELQA 500
LAAAVVPSAQ TLKITDFSFS DFELSDLETA LCTIRMFTDL NLVQNFQMKH 550
EVLCRWILSV KKNYRKNVAY HNWRHAFNTA QCMFAALKAG KIQNKLTDLE 600
TLALLIAALS HDLDHRGVNN SYIQRSEHPL AQLYCHSTME HHHFDQCLMV 650
LNSPGNQILS GLSIEEYKTT LKIIKQAILA TDLALYIKRR GEFFELIRKN 700
EFSFEDPLQK ELFLAMLMTA CDLSAITKPW PIQQRIAELV AAEFFDQGDR 750
ERKELNMEPA DLMNREKKNK IPSMQVGFID AICLQLYEAL THVSEDCLPL 800
LDGCRKNRQK WQALADQQEK TLLNGESGQA KRD 833
Length:833
Mass (Da):94,556
Last modified:June 1, 1998 - v1
Checksum:i712DC159C80CB09D
GO
Isoform PDE5A1 (identifier: O54735-2)

Sequence is not available
Length:
Mass (Da):

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D89093 mRNA. Translation: BAA23672.1.
RefSeqiNP_598268.1. NM_133584.1. [O54735-1]
UniGeneiRn.10861.
Rn.133138.

Genome annotation databases

GeneIDi171115.
KEGGirno:171115.
UCSCiRGD:620995. rat. [O54735-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D89093 mRNA. Translation: BAA23672.1 .
RefSeqi NP_598268.1. NM_133584.1. [O54735-1 ]
UniGenei Rn.10861.
Rn.133138.

3D structure databases

ProteinModelPortali O54735.
SMRi O54735. Positions 122-269, 493-818.
ModBasei Search...
MobiDBi Search...

Chemistry

BindingDBi O54735.
ChEMBLi CHEMBL4567.

PTM databases

PhosphoSitei O54735.

Proteomic databases

PaxDbi O54735.
PRIDEi O54735.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 171115.
KEGGi rno:171115.
UCSCi RGD:620995. rat. [O54735-1 ]

Organism-specific databases

CTDi 8654.
RGDi 620995. Pde5a.

Phylogenomic databases

eggNOGi NOG270709.
HOGENOMi HOG000007068.
HOVERGENi HBG101207.
InParanoidi O54735.
KOi K13762.
PhylomeDBi O54735.

Enzyme and pathway databases

UniPathwayi UPA00763 ; UER00748 .

Miscellaneous databases

NextBioi 621836.
PROi O54735.

Gene expression databases

Genevestigatori O54735.

Family and domain databases

Gene3Di 1.10.1300.10. 1 hit.
3.30.450.40. 2 hits.
InterProi IPR003018. GAF.
IPR029016. GAF_dom_like.
IPR003607. HD/PDEase_dom.
IPR023088. PDEase.
IPR002073. PDEase_catalytic_dom.
IPR023174. PDEase_CS.
[Graphical view ]
Pfami PF01590. GAF. 2 hits.
PF00233. PDEase_I. 1 hit.
[Graphical view ]
PRINTSi PR00387. PDIESTERASE1.
SMARTi SM00065. GAF. 2 hits.
SM00471. HDc. 1 hit.
[Graphical view ]
SUPFAMi SSF55781. SSF55781. 2 hits.
PROSITEi PS00126. PDEASE_I. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Expression of rat cGMP-binding cGMP-specific phosphodiesterase mRNA in Purkinje cell layers during postnatal neuronal development."
    Kotera J., Yanaka N., Fujishige K., Imai Y., Akatsuka H., Ishizuka T., Kawashima K., Omori K.
    Eur. J. Biochem. 249:434-442(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Lung.

Entry informationi

Entry nameiPDE5A_RAT
AccessioniPrimary (citable) accession number: O54735
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: June 1, 1998
Last modified: June 11, 2014
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

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