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Protein

cGMP-specific 3',5'-cyclic phosphodiesterase

Gene

PDE5A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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:9714779, PubMed:15489334). Specifically regulates nitric-oxide-generated cGMP (PubMed:15489334).2 Publications

Catalytic activityi

Guanosine 3',5'-cyclic phosphate + H2O = guanosine 5'-phosphate.1 Publication

Cofactori

Protein has several cofactor binding sites:

Enzyme regulationi

Sildenafil (Viagra) is a highly selective and potent inhibitor of PDE5A and is effective in the treatment of penile erectile dysfunction. Also inhibited by zaprinast.1 Publication

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), High affinity cGMP-specific 3',5'-cyclic phosphodiesterase 9A (PDE9A), cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A (PDE10A)
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 sitei613Proton donorBy similarity1
Metal bindingi617Zinc; via tele nitrogen1 Publication1
Metal bindingi653Zinc; via tele nitrogen1 Publication1
Metal bindingi654Magnesium1 Publication1
Metal bindingi654Zinc1 Publication1
Metal bindingi764Zinc1 Publication1
Binding sitei817cGMP1 Publication1

GO - Molecular functioni

  • 3',5'-cyclic-GMP phosphodiesterase activity Source: Reactome
  • 3',5'-cyclic-nucleotide phosphodiesterase activity Source: UniProtKB
  • cGMP binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

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

Enzyme and pathway databases

BioCyciZFISH:HS06542-MONOMER.
BRENDAi3.1.4.35. 2681.
ReactomeiR-HSA-418457. cGMP effects.
SIGNORiO76074.
UniPathwayiUPA00763; UER00748.

Names & Taxonomyi

Protein namesi
Recommended name:
cGMP-specific 3',5'-cyclic phosphodiesterase (EC:3.1.4.351 Publication)
Alternative name(s):
cGMP-binding cGMP-specific phosphodiesterase
Short name:
CGB-PDE
Gene namesi
Name:PDE5A
Synonyms:PDE5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:8784. PDE5A.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

DisGeNETi8654.
OpenTargetsiENSG00000138735.
PharmGKBiPA33132.

Chemistry databases

ChEMBLiCHEMBL1827.
DrugBankiDB06237. Avanafil.
DB00201. Caffeine.
DB00975. Dipyridamole.
DB00806. Pentoxifylline.
DB00203. Sildenafil.
DB00820. Tadalafil.
DB00277. Theophylline.
DB06267. Udenafil.
DB00862. Vardenafil.
GuidetoPHARMACOLOGYi1304.

Polymorphism and mutation databases

BioMutaiPDE5A.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001988231 – 875cGMP-specific 3',5'-cyclic phosphodiesteraseAdd BLAST875

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei102PhosphoserineSequence analysis1

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 similarity1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiO76074.
MaxQBiO76074.
PaxDbiO76074.
PeptideAtlasiO76074.
PRIDEiO76074.

PTM databases

iPTMnetiO76074.
PhosphoSitePlusiO76074.

Expressioni

Tissue specificityi

Expressed in aortic smooth muscle cells, heart, placenta, skeletal muscle and pancreas and, to a much lesser extent, in brain, liver and lung.

Gene expression databases

BgeeiENSG00000138735.
CleanExiHS_PDE5A.
ExpressionAtlasiO76074. baseline and differential.
GenevisibleiO76074. HS.

Organism-specific databases

HPAiHPA004729.
HPA012873.

Interactioni

Protein-protein interaction databases

DIPiDIP-46287N.
IntActiO76074. 2 interactors.
STRINGi9606.ENSP00000347046.

Chemistry databases

BindingDBiO76074.

Structurei

Secondary structure

1875
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi103 – 106Combined sources4
Beta strandi115 – 117Combined sources3
Turni118 – 120Combined sources3
Beta strandi121 – 124Combined sources4
Helixi148 – 160Combined sources13
Helixi165 – 177Combined sources13
Beta strandi182 – 192Combined sources11
Beta strandi198 – 205Combined sources8
Beta strandi208 – 210Combined sources3
Beta strandi213 – 218Combined sources6
Beta strandi221 – 224Combined sources4
Helixi228 – 236Combined sources9
Beta strandi240 – 243Combined sources4
Helixi245 – 247Combined sources3
Helixi254 – 259Combined sources6
Beta strandi266 – 272Combined sources7
Beta strandi278 – 287Combined sources10
Helixi299 – 340Combined sources42
Turni342 – 345Combined sources4
Helixi346 – 362Combined sources17
Beta strandi365 – 372Combined sources8
Beta strandi374 – 376Combined sources3
Beta strandi379 – 387Combined sources9
Turni388 – 390Combined sources3
Beta strandi391 – 393Combined sources3
Helixi400 – 403Combined sources4
Helixi407 – 409Combined sources3
Helixi410 – 418Combined sources9
Beta strandi422 – 425Combined sources4
Turni427 – 429Combined sources3
Beta strandi431 – 433Combined sources3
Beta strandi451 – 457Combined sources7
Beta strandi461 – 471Combined sources11
Turni476 – 478Combined sources3
Helixi486 – 506Combined sources21
Helixi535 – 545Combined sources11
Helixi551 – 554Combined sources4
Turni555 – 557Combined sources3
Helixi568 – 581Combined sources14
Helixi584 – 587Combined sources4
Helixi592 – 604Combined sources13
Turni606 – 608Combined sources3
Beta strandi610 – 614Combined sources5
Helixi615 – 630Combined sources16
Turni631 – 633Combined sources3
Helixi635 – 637Combined sources3
Helixi640 – 652Combined sources13
Turni653 – 656Combined sources4
Helixi662 – 667Combined sources6
Helixi671 – 675Combined sources5
Beta strandi677 – 679Combined sources3
Helixi680 – 694Combined sources15
Turni700 – 703Combined sources4
Helixi706 – 722Combined sources17
Helixi725 – 740Combined sources16
Beta strandi746 – 748Combined sources3
Helixi749 – 764Combined sources16
Helixi766 – 769Combined sources4
Helixi772 – 796Combined sources25
Helixi803 – 805Combined sources3
Helixi807 – 812Combined sources6
Helixi813 – 823Combined sources11
Helixi825 – 835Combined sources11
Helixi837 – 839Combined sources3
Helixi840 – 857Combined sources18

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1RKPX-ray2.05A535-860[»]
1T9RX-ray2.10A531-875[»]
1T9SX-ray2.00A/B534-858[»]
1TBFX-ray1.30A534-858[»]
1UDTX-ray2.30A537-860[»]
1UDUX-ray2.83A/B537-860[»]
1UHOX-ray2.50A537-860[»]
1XOZX-ray1.37A534-875[»]
1XP0X-ray1.79A534-875[»]
2CHMX-ray1.60A534-656[»]
A682-858[»]
2H40X-ray1.85A535-860[»]
2H42X-ray2.30A/B/C535-860[»]
2H44X-ray1.80A535-860[»]
2XSSX-ray2.50A/B346-509[»]
3B2RX-ray2.07A/B535-860[»]
3BJCX-ray2.00A1-875[»]
3HC8X-ray1.79A536-657[»]
A682-858[»]
3HDZX-ray1.80A536-657[»]
A682-858[»]
3JWQX-ray2.87A/B/C/D535-786[»]
A/B/C/D827-860[»]
3JWRX-ray2.99A/B535-786[»]
A/B827-860[»]
3LFVX-ray2.80A/B98-518[»]
3MF0X-ray3.10A/B89-518[»]
3SHYX-ray2.65A535-860[»]
3SHZX-ray2.45A535-860[»]
3SIEX-ray1.93A/B535-860[»]
3TGEX-ray1.96A534-656[»]
A682-858[»]
3TGGX-ray1.91A534-660[»]
A662-858[»]
4G2WX-ray2.28A535-860[»]
4G2YX-ray2.40A535-860[»]
4I9ZX-ray2.08A535-860[»]
4IA0X-ray2.17A535-860[»]
4MD6X-ray2.00A535-860[»]
4OEWX-ray2.44A535-860[»]
4OEXX-ray2.14A535-860[»]
ProteinModelPortaliO76074.
SMRiO76074.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO76074.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini164 – 314GAF 1Add BLAST151
Domaini346 – 503GAF 2Add BLAST158

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni588 – 853CatalyticBy similarityAdd BLAST266

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi10 – 24Poly-GlnAdd BLAST15

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.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG3689. Eukaryota.
ENOG410XRI7. LUCA.
GeneTreeiENSGT00760000119066.
HOVERGENiHBG101207.
KOiK13762.
OMAiTREHDAN.
OrthoDBiEOG091G04JU.
PhylomeDBiO76074.
TreeFamiTF316499.

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. AlignAdd to basket

Isoform PDE5A1 (identifier: O76074-1) [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

        10         20         30         40         50
MERAGPSFGQ QRQQQQPQQQ KQQQRDQDSV EAWLDDHWDF TFSYFVRKAT
60 70 80 90 100
REMVNAWFAE RVHTIPVCKE GIRGHTESCS CPLQQSPRAD NSAPGTPTRK
110 120 130 140 150
ISASEFDRPL RPIVVKDSEG TVSFLSDSEK KEQMPLTPPR FDHDEGDQCS
160 170 180 190 200
RLLELVKDIS SHLDVTALCH KIFLHIHGLI SADRYSLFLV CEDSSNDKFL
210 220 230 240 250
ISRLFDVAEG STLEEVSNNC IRLEWNKGIV GHVAALGEPL NIKDAYEDPR
260 270 280 290 300
FNAEVDQITG YKTQSILCMP IKNHREEVVG VAQAINKKSG NGGTFTEKDE
310 320 330 340 350
KDFAAYLAFC GIVLHNAQLY ETSLLENKRN QVLLDLASLI FEEQQSLEVI
360 370 380 390 400
LKKIAATIIS FMQVQKCTIF IVDEDCSDSF SSVFHMECEE LEKSSDTLTR
410 420 430 440 450
EHDANKINYM YAQYVKNTME PLNIPDVSKD KRFPWTTENT GNVNQQCIRS
460 470 480 490 500
LLCTPIKNGK KNKVIGVCQL VNKMEENTGK VKPFNRNDEQ FLEAFVIFCG
510 520 530 540 550
LGIQNTQMYE AVERAMAKQM VTLEVLSYHA SAAEEETREL QSLAAAVVPS
560 570 580 590 600
AQTLKITDFS FSDFELSDLE TALCTIRMFT DLNLVQNFQM KHEVLCRWIL
610 620 630 640 650
SVKKNYRKNV AYHNWRHAFN TAQCMFAALK AGKIQNKLTD LEILALLIAA
660 670 680 690 700
LSHDLDHRGV NNSYIQRSEH PLAQLYCHSI MEHHHFDQCL MILNSPGNQI
710 720 730 740 750
LSGLSIEEYK TTLKIIKQAI LATDLALYIK RRGEFFELIR KNQFNLEDPH
760 770 780 790 800
QKELFLAMLM TACDLSAITK PWPIQQRIAE LVATEFFDQG DRERKELNIE
810 820 830 840 850
PTDLMNREKK NKIPSMQVGF IDAICLQLYE ALTHVSEDCF PLLDGCRKNR
860 870
QKWQALAEQQ EKMLINGESG QAKRN
Length:875
Mass (Da):99,985
Last modified:January 11, 2011 - v2
Checksum:i9E30C6C182F13388
GO
Isoform PDE5A2 (identifier: O76074-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-49: MERAGPSFGQQRQQQQPQQQKQQQRDQDSVEAWLDDHWDFTFSYFVRKA → MLPFGDK

Show »
Length:833
Mass (Da):94,805
Checksum:i41D0B4B1BAB57D6D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti159I → V in AAP31235 (PubMed:10393044).Curated1
Sequence conflicti310C → G in AAP31235 (PubMed:10393044).Curated1
Sequence conflicti381S → F in AAP31235 (PubMed:10393044).Curated1
Sequence conflicti406K → R in AAP31235 (PubMed:10393044).Curated1
Sequence conflicti642E → G in BAA81667 (Ref. 4) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02777593A → V.5 PublicationsCorresponds to variant rs3733526dbSNPEnsembl.1
Natural variantiVAR_027776181S → A.Corresponds to variant rs17051276dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0045911 – 49MERAG…FVRKA → MLPFGDK in isoform PDE5A2. 3 PublicationsAdd BLAST49

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF043731 mRNA. Translation: AAC63967.1.
AF043732 mRNA. Translation: AAC63968.1.
AB001635 Genomic DNA. Translation: BAA33372.2.
D89094 mRNA. Translation: BAA28945.1.
AJ004865 mRNA. Translation: CAA06170.1.
AB015656 mRNA. Translation: BAA81667.1.
AY264918 mRNA. Translation: AAP21809.1.
AK290189 mRNA. Translation: BAF82878.1.
AC093752 Genomic DNA. No translation available.
AC080089 Genomic DNA. No translation available.
BC126233 mRNA. Translation: AAI26234.1.
AY266363 mRNA. Translation: AAP31235.1.
CCDSiCCDS34055.1. [O76074-2]
CCDS3713.1. [O76074-1]
PIRiJW0106.
RefSeqiNP_001074.2. NM_001083.3. [O76074-1]
NP_236914.2. NM_033430.2. [O76074-2]
NP_246273.2. NM_033437.3.
UniGeneiHs.647971.

Genome annotation databases

EnsembliENST00000264805; ENSP00000264805; ENSG00000138735. [O76074-2]
ENST00000354960; ENSP00000347046; ENSG00000138735. [O76074-1]
GeneIDi8654.
KEGGihsa:8654.
UCSCiuc003idf.4. human. [O76074-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF043731 mRNA. Translation: AAC63967.1.
AF043732 mRNA. Translation: AAC63968.1.
AB001635 Genomic DNA. Translation: BAA33372.2.
D89094 mRNA. Translation: BAA28945.1.
AJ004865 mRNA. Translation: CAA06170.1.
AB015656 mRNA. Translation: BAA81667.1.
AY264918 mRNA. Translation: AAP21809.1.
AK290189 mRNA. Translation: BAF82878.1.
AC093752 Genomic DNA. No translation available.
AC080089 Genomic DNA. No translation available.
BC126233 mRNA. Translation: AAI26234.1.
AY266363 mRNA. Translation: AAP31235.1.
CCDSiCCDS34055.1. [O76074-2]
CCDS3713.1. [O76074-1]
PIRiJW0106.
RefSeqiNP_001074.2. NM_001083.3. [O76074-1]
NP_236914.2. NM_033430.2. [O76074-2]
NP_246273.2. NM_033437.3.
UniGeneiHs.647971.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1RKPX-ray2.05A535-860[»]
1T9RX-ray2.10A531-875[»]
1T9SX-ray2.00A/B534-858[»]
1TBFX-ray1.30A534-858[»]
1UDTX-ray2.30A537-860[»]
1UDUX-ray2.83A/B537-860[»]
1UHOX-ray2.50A537-860[»]
1XOZX-ray1.37A534-875[»]
1XP0X-ray1.79A534-875[»]
2CHMX-ray1.60A534-656[»]
A682-858[»]
2H40X-ray1.85A535-860[»]
2H42X-ray2.30A/B/C535-860[»]
2H44X-ray1.80A535-860[»]
2XSSX-ray2.50A/B346-509[»]
3B2RX-ray2.07A/B535-860[»]
3BJCX-ray2.00A1-875[»]
3HC8X-ray1.79A536-657[»]
A682-858[»]
3HDZX-ray1.80A536-657[»]
A682-858[»]
3JWQX-ray2.87A/B/C/D535-786[»]
A/B/C/D827-860[»]
3JWRX-ray2.99A/B535-786[»]
A/B827-860[»]
3LFVX-ray2.80A/B98-518[»]
3MF0X-ray3.10A/B89-518[»]
3SHYX-ray2.65A535-860[»]
3SHZX-ray2.45A535-860[»]
3SIEX-ray1.93A/B535-860[»]
3TGEX-ray1.96A534-656[»]
A682-858[»]
3TGGX-ray1.91A534-660[»]
A662-858[»]
4G2WX-ray2.28A535-860[»]
4G2YX-ray2.40A535-860[»]
4I9ZX-ray2.08A535-860[»]
4IA0X-ray2.17A535-860[»]
4MD6X-ray2.00A535-860[»]
4OEWX-ray2.44A535-860[»]
4OEXX-ray2.14A535-860[»]
ProteinModelPortaliO76074.
SMRiO76074.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-46287N.
IntActiO76074. 2 interactors.
STRINGi9606.ENSP00000347046.

Chemistry databases

BindingDBiO76074.
ChEMBLiCHEMBL1827.
DrugBankiDB06237. Avanafil.
DB00201. Caffeine.
DB00975. Dipyridamole.
DB00806. Pentoxifylline.
DB00203. Sildenafil.
DB00820. Tadalafil.
DB00277. Theophylline.
DB06267. Udenafil.
DB00862. Vardenafil.
GuidetoPHARMACOLOGYi1304.

PTM databases

iPTMnetiO76074.
PhosphoSitePlusiO76074.

Polymorphism and mutation databases

BioMutaiPDE5A.

Proteomic databases

EPDiO76074.
MaxQBiO76074.
PaxDbiO76074.
PeptideAtlasiO76074.
PRIDEiO76074.

Protocols and materials databases

DNASUi8654.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000264805; ENSP00000264805; ENSG00000138735. [O76074-2]
ENST00000354960; ENSP00000347046; ENSG00000138735. [O76074-1]
GeneIDi8654.
KEGGihsa:8654.
UCSCiuc003idf.4. human. [O76074-1]

Organism-specific databases

CTDi8654.
DisGeNETi8654.
GeneCardsiPDE5A.
HGNCiHGNC:8784. PDE5A.
HPAiHPA004729.
HPA012873.
MIMi603310. gene.
neXtProtiNX_O76074.
OpenTargetsiENSG00000138735.
PharmGKBiPA33132.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3689. Eukaryota.
ENOG410XRI7. LUCA.
GeneTreeiENSGT00760000119066.
HOVERGENiHBG101207.
KOiK13762.
OMAiTREHDAN.
OrthoDBiEOG091G04JU.
PhylomeDBiO76074.
TreeFamiTF316499.

Enzyme and pathway databases

UniPathwayiUPA00763; UER00748.
BioCyciZFISH:HS06542-MONOMER.
BRENDAi3.1.4.35. 2681.
ReactomeiR-HSA-418457. cGMP effects.
SIGNORiO76074.

Miscellaneous databases

ChiTaRSiPDE5A. human.
EvolutionaryTraceiO76074.
GeneWikiiCGMP-specific_phosphodiesterase_type_5.
GenomeRNAii8654.
PROiO76074.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000138735.
CleanExiHS_PDE5A.
ExpressionAtlasiO76074. baseline and differential.
GenevisibleiO76074. HS.

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]
ProtoNetiSearch...

Entry informationi

Entry nameiPDE5A_HUMAN
AccessioniPrimary (citable) accession number: O76074
Secondary accession number(s): A0AV69
, A8K2C4, O75026, O75887, Q86UI0, Q86V66, Q9Y6Z6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 11, 2011
Last modified: November 30, 2016
This is version 165 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Caution

Was initially thought to act as a major regulator of cardiac hypertrophy in myocytes and muscle and investigations have been made on selective PDE5A inhibitors that could protect against cardiovascular disease. However, while PDE5A regulates nitric-oxide-generated cGMP, nitric oxide signaling is often depressed by heart disease, limiting its effect. Moreover, clinical trial using PDE5A inhibitors were disappointing.1 Publication

Keywords - Technical termi

3D-structure, Allosteric enzyme, Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.