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Protein

cGMP-specific 3',5'-cyclic phosphodiesterase

Gene

PDE5A

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: -Experimental evidence at protein 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 (PubMed:8530505). Specifically regulates nitric-oxide-generated cGMP (By similarity).By similarity1 Publication

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:
  • Zn2+By similarityNote: Binds 1 Zn2+ ion per subunit. Binds 2 divalent metal cations per subunit: site 1 preferentially binds zinc, while site 2 has a preference for magnesium. Tightly binds zinc.By similarity
  • Mg2+By similarityNote: Binds 1 Mg2+ ions per subunit. Binds 2 divalent metal cations per subunit: site 1 preferentially binds zinc, while site 2 has a preference for magnesium. Binds magnesium less tightly than zinc.By similarity

Enzyme regulationi

Most potently inhibited by zaprinast and dipyridamole.

Pathwayi: 3',5'-cyclic GMP degradation

This protein is involved in step 1 of the subpathway that synthesizes GMP from 3',5'-cyclic GMP.
Proteins known to be involved in this subpathway in this organism are:
  1. cGMP-specific 3',5'-cyclic phosphodiesterase (PDE5A)
This subpathway is part of the pathway 3',5'-cyclic GMP 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 GMP from 3',5'-cyclic GMP, the pathway 3',5'-cyclic GMP degradation and in Purine metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei603Proton donorBy similarity1
Metal bindingi607Zinc; via tele nitrogenBy similarity1
Metal bindingi643Zinc; via tele nitrogenBy similarity1
Metal bindingi644MagnesiumBy similarity1
Metal bindingi644ZincBy similarity1
Metal bindingi754ZincBy similarity1
Binding sitei807cGMPBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionAllosteric enzyme, Hydrolase
LigandcGMP, cGMP-binding, Magnesium, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

ReactomeiR-BTA-418457 cGMP effects
UniPathwayiUPA00763; UER00748

Names & Taxonomyi

Protein namesi
Recommended name:
cGMP-specific 3',5'-cyclic phosphodiesterase (EC:3.1.4.35By similarity)
Alternative name(s):
cGMP-binding cGMP-specific phosphodiesterase
Short name:
CGB-PDE
Gene namesi
Name:PDE5A
Synonyms:PDE5
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 6

Organism-specific databases

VGNCiVGNC:32678 PDE5A

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi276N → A: Decreased cGMP-binding; no change in catalytic activity. 1 Publication1
Mutagenesisi277K → A: Decreased cGMP-binding; no change in catalytic activity. 1 Publication1
Mutagenesisi277K → R: Slight increase in cGMP-binding. 1 Publication1
Mutagenesisi289D → A: Decreased cGMP-binding; no change in catalytic activity. 3 Publications1
Mutagenesisi289D → N: Increased cGMP-binding; no change in catalytic activity. 3 Publications1
Mutagenesisi290E → A: No change in cGMP-binding. 1 Publication1
Mutagenesisi478D → A: Increased cGMP-binding; no change in catalytic activity. Phosphorylated at lower concentrations of cGMP. 2 Publications1

Chemistry databases

ChEMBLiCHEMBL3478

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001988211 – 865cGMP-specific 3',5'-cyclic phosphodiesteraseAdd BLAST865

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei92PhosphoserineSequence analysis1

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ28156
PRIDEiQ28156

PTM databases

iPTMnetiQ28156

Expressioni

Gene expression databases

BgeeiENSBTAG00000024888

Interactioni

Protein-protein interaction databases

BioGridi159263, 1 interactor
STRINGi9913.ENSBTAP00000014479

Chemistry databases

BindingDBiQ28156

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FL4model-A118-309[»]
3JABelectron microscopy11.00C/O525-850[»]
3JBQelectron microscopy11.00B/F525-850[»]
ProteinModelPortaliQ28156
SMRiQ28156
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini154 – 304GAF 1Add BLAST151
Domaini336 – 493GAF 2Add BLAST158
Domaini526 – 850PDEasePROSITE-ProRule annotationAdd BLAST325

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG3689 Eukaryota
ENOG410XRI7 LUCA
GeneTreeiENSGT00760000119066
HOGENOMiHOG000007068
HOVERGENiHBG101207
InParanoidiQ28156
KOiK13762
OMAiVDEDCSD
OrthoDBiEOG091G04JU
TreeFamiTF316499

Family and domain databases

CDDicd00077 HDc, 1 hit
Gene3Di1.10.1300.10, 1 hit
3.30.450.40, 3 hits
InterProiView protein in InterPro
IPR003018 GAF
IPR029016 GAF-like_dom_sf
IPR003607 HD/PDEase_dom
IPR023088 PDEase
IPR002073 PDEase_catalytic_dom
IPR036971 PDEase_catalytic_dom_sf
IPR023174 PDEase_CS
PfamiView protein in Pfam
PF01590 GAF, 2 hits
PF00233 PDEase_I, 1 hit
PRINTSiPR00387 PDIESTERASE1
SMARTiView protein in SMART
SM00065 GAF, 2 hits
SM00471 HDc, 1 hit
PROSITEiView protein in PROSITE
PS00126 PDEASE_I_1, 1 hit
PS51845 PDEASE_I_2, 1 hit

Sequencei

Sequence statusi: Complete.

Q28156-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MERAGPGSAR PQQQWDQDSV EAWLDDHWDF TFSYFVRKGT REMVNAWFAE
60 70 80 90 100
RVHTIPVCKE GIKGHTESCS CPLQPSPRAE SSVPGTPTRK ISASEFDRPL
110 120 130 140 150
RPIVIKDSEG TVSFLSDSDK KEQMPLTSPR FDNDEGDQCS RLLELVKDIS
160 170 180 190 200
SHLDVTALCH KIFLHIHGLI SADRYSLFLV CEDSSNDKFL ISRLFDVAEG
210 220 230 240 250
STLEEASNNC IRLEWNKGIV GHVAAFGEPL NIKDAYEDPR FNAEVDQITG
260 270 280 290 300
YKTQSILCMP IKNHREEVVG VAQAINKKSG NGGTFTEKDE KDFAAYLAFC
310 320 330 340 350
GIVLHNAQLY ETSLLENKRN QVLLDLASLI FEEQQSLEVI LKKIAATIIS
360 370 380 390 400
FMQVQKCTIF IVDEDCSDSF SSVFHMECEE LEKSSDTLTR ERDANRINYM
410 420 430 440 450
YAQYVKNTME PLNIPDVSKD KRFPWTNENM GNINQQCIRS LLCTPIKNGK
460 470 480 490 500
KNKVIGVCQL VNKMEETTGK VKAFNRNDEQ FLEAFVIFCG LGIQNTQMYE
510 520 530 540 550
AVERAMAKQM VTLEVLSYHA SAAEEETREL QSLAAAVVPS AQTLKITDFS
560 570 580 590 600
FSDFELSDLE TALCTIRMFT DLNLVQNFQM KHEVLCKWIL SVKKNYRKNV
610 620 630 640 650
AYHNWRHAFN TAQCMFAALK AGKIQKRLTD LEILALLIAA LSHDLDHRGV
660 670 680 690 700
NNSYIQRSEH PLAQLYCHSI MEHHHFDQCL MILNSPGNQI LSGLSIEEYK
710 720 730 740 750
TTLKIIKQAI LATDLALYIK RRGEFFELIM KNQFNLEDPH QKELFLAMLM
760 770 780 790 800
TACDLSAITK PWPIQQRIAE LVATEFFDQG DRERKELNIE PADLMNREKK
810 820 830 840 850
NKIPSMQVGF IDAICLQLYE ALTHVSEDCF PLLDGCRKNR QKWQALAEQQ
860
EKTLINGESS QTKRN
Length:865
Mass (Da):98,627
Last modified:November 1, 1996 - v1
Checksum:i2FF7144B2990B4F7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L16545 mRNA Translation: AAB00990.1
RefSeqiNP_776842.1, NM_174417.2
UniGeneiBt.540

Genome annotation databases

EnsembliENSBTAT00000014479; ENSBTAP00000014479; ENSBTAG00000024888
GeneIDi281972
KEGGibta:281972

Similar proteinsi

Entry informationi

Entry nameiPDE5A_BOVIN
AccessioniPrimary (citable) accession number: Q28156
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: May 23, 2018
This is version 137 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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