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Protein

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

Gene

PDE7A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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.1 Publication

Catalytic activityi

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

Cofactori

a divalent metal cation1 PublicationNote: 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.1 Publication

Enzyme regulationi

Insensitive to all selective PDE inhibitors.

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. cAMP-specific 3',5'-cyclic phosphodiesterase 4C (PDE4C), cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A (PDE10A), cAMP-specific 3',5'-cyclic phosphodiesterase 4A (PDE4A), High affinity cAMP-specific 3',5'-cyclic phosphodiesterase 7A (PDE7A), cAMP-specific 3',5'-cyclic phosphodiesterase 7B (PDE7B), cAMP-specific 3',5'-cyclic phosphodiesterase 4D (PDE4D), cAMP-specific 3',5'-cyclic phosphodiesterase 4B (PDE4B), High affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8B (PDE8B), High affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8A (PDE8A)
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 sitei212Proton donorBy similarity1
Metal bindingi216Divalent metal cation 11
Metal bindingi252Divalent metal cation 11
Metal bindingi253Divalent metal cation 11
Metal bindingi253Divalent metal cation 21
Metal bindingi362Divalent metal cation 11

GO - Molecular functioni

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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

cAMP, Metal-binding

Enzyme and pathway databases

BioCyciZFISH:HS02610-MONOMER.
BRENDAi3.1.4.53. 2681.
ReactomeiR-HSA-418555. G alpha (s) signalling events.
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):
HCP1
TM22
Gene namesi
Name:PDE7A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:8791. PDE7A.

Subcellular locationi

Isoform PDE7A1 :
  • Cytoplasmcytosol

  • Note: PDE7A1 (57 kDa) is located mostly to soluble cellular fractions.
Isoform PDE7A2 :
  • Cytoplasm

  • Note: PDE7A2 (50 kDa) is located to particulate cellular fractions.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

DisGeNETi5150.
OpenTargetsiENSG00000205268.
PharmGKBiPA33139.

Chemistry databases

ChEMBLiCHEMBL3012.
DrugBankiDB00201. Caffeine.
DB00651. Dyphylline.
DB00920. Ketotifen.
GuidetoPHARMACOLOGYi1305.

Polymorphism and mutation databases

BioMutaiPDE7A.
DMDMi3182958.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001988331 – 482High affinity cAMP-specific 3',5'-cyclic phosphodiesterase 7AAdd BLAST482

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei84PhosphoserineSequence analysis1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ13946.
MaxQBiQ13946.
PaxDbiQ13946.
PeptideAtlasiQ13946.
PRIDEiQ13946.

PTM databases

iPTMnetiQ13946.
PhosphoSitePlusiQ13946.

Expressioni

Tissue specificityi

PDE7A1 is found at high levels in skeletal muscle and at low levels in a variety of tissues including brain and heart. It is expressed as well in two T-cell lines. PDE7A2 is found abundantly in skeletal muscle and at low levels in heart.

Developmental stagei

Developmentally regulated. PDE7A1 and PDE7A2 are found in several fetal tissues, expression is reduced throughout development. It persists strongly only in adult skeletal muscle.

Gene expression databases

BgeeiENSG00000205268.
CleanExiHS_PDE7A.
ExpressionAtlasiQ13946. baseline and differential.
GenevisibleiQ13946. HS.

Organism-specific databases

HPAiCAB018770.
HPA027340.

Interactioni

Subunit structurei

Interacts with CBFA2T3.3 Publications

Protein-protein interaction databases

BioGridi111176. 4 interactors.
IntActiQ13946. 1 interactor.
STRINGi9606.ENSP00000385632.

Chemistry databases

BindingDBiQ13946.

Structurei

Secondary structure

1482
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi140 – 148Combined sources9
Turni149 – 152Combined sources4
Helixi158 – 164Combined sources7
Helixi169 – 180Combined sources12
Helixi183 – 186Combined sources4
Helixi191 – 203Combined sources13
Beta strandi209 – 213Combined sources5
Helixi214 – 228Combined sources15
Helixi231 – 234Combined sources4
Helixi239 – 251Combined sources13
Turni252 – 255Combined sources4
Helixi261 – 266Combined sources6
Helixi270 – 274Combined sources5
Turni275 – 277Combined sources3
Helixi280 – 296Combined sources17
Turni297 – 301Combined sources5
Helixi304 – 319Combined sources16
Helixi323 – 325Combined sources3
Helixi326 – 339Combined sources14
Helixi347 – 362Combined sources16
Helixi365 – 367Combined sources3
Helixi370 – 393Combined sources24
Turni404 – 406Combined sources3
Helixi409 – 419Combined sources11
Helixi421 – 431Combined sources11
Helixi435 – 453Combined sources19

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ZKLX-ray1.67A130-482[»]
3G3NX-ray2.40A139-456[»]
4PM0X-ray2.10A130-482[»]
4Y2BX-ray2.20A130-482[»]
ProteinModelPortaliQ13946.
SMRiQ13946.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13946.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni187 – 451CatalyticBy similarityAdd BLAST265

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi28 – 33Poly-Ser6

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.
GeneTreeiENSGT00760000118889.
HOGENOMiHOG000220881.
HOVERGENiHBG053543.
KOiK18436.
OMAiLCDRQTE.
OrthoDBiEOG091G05SK.
PhylomeDBiQ13946.
TreeFamiTF314638.

Family and domain databases

Gene3Di1.10.1300.10. 1 hit.
InterProiIPR003607. HD/PDEase_dom.
IPR023088. PDEase.
IPR002073. PDEase_catalytic_dom.
IPR023174. PDEase_CS.
[Graphical view]
PfamiPF00233. PDEase_I. 1 hit.
[Graphical view]
PRINTSiPR00387. PDIESTERASE1.
SMARTiSM00471. HDc. 1 hit.
[Graphical view]
PROSITEiPS00126. PDEASE_I. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform PDE7A1 (identifier: Q13946-1) [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
MEVCYQLPVL PLDRPVPQHV LSRRGAISFS SSSALFGCPN PRQLSQRRGA
60 70 80 90 100
ISYDSSDQTA LYIRMLGDVR VRSRAGFESE RRGSHPYIDF RIFHSQSEIE
110 120 130 140 150
VSVSARNIRR LLSFQRYLRS SRFFRGTAVS NSLNILDDDY NGQAKCMLEK
160 170 180 190 200
VGNWNFDIFL FDRLTNGNSL VSLTFHLFSL HGLIEYFHLD MMKLRRFLVM
210 220 230 240 250
IQEDYHSQNP YHNAVHAADV TQAMHCYLKE PKLANSVTPW DILLSLIAAA
260 270 280 290 300
THDLDHPGVN QPFLIKTNHY LATLYKNTSV LENHHWRSAV GLLRESGLFS
310 320 330 340 350
HLPLESRQQM ETQIGALILA TDISRQNEYL SLFRSHLDRG DLCLEDTRHR
360 370 380 390 400
HLVLQMALKC ADICNPCRTW ELSKQWSEKV TEEFFHQGDI EKKYHLGVSP
410 420 430 440 450
LCDRHTESIA NIQIGFMTYL VEPLFTEWAR FSNTRLSQTM LGHVGLNKAS
460 470 480
WKGLQREQSS SEDTDAAFEL NSQLLPQENR LS
Length:482
Mass (Da):55,505
Last modified:July 15, 1998 - v2
Checksum:i3B3C8F6E9154F88C
GO
Isoform PDE7A2 (identifier: Q13946-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-46: MEVCYQLPVLPLDRPVPQHVLSRRGAISFSSSSALFGCPNPRQLSQ → MGITLIWCLALVLIKWITSK

Show »
Length:456
Mass (Da):52,725
Checksum:iCAA62B0BFEF074AF
GO
Isoform PDE7A3 (identifier: Q13946-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     416-424: FMTYLVEPL → NYTYLDIAG
     425-482: Missing.

Show »
Length:424
Mass (Da):48,828
Checksum:iA7DBF40D08A7B561
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti204D → G in BAF83490 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05666176G → E.Corresponds to variant rs11557049dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0045931 – 46MEVCY…RQLSQ → MGITLIWCLALVLIKWITSK in isoform PDE7A2. 2 PublicationsAdd BLAST46
Alternative sequenceiVSP_038645416 – 424FMTYLVEPL → NYTYLDIAG in isoform PDE7A3. 1 Publication9
Alternative sequenceiVSP_038646425 – 482Missing in isoform PDE7A3. 1 PublicationAdd BLAST58

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L12052 mRNA. Translation: AAA35644.2.
U67932 mRNA. Translation: AAB65772.1.
AF332652 mRNA. Translation: AAK57640.1.
AK290801 mRNA. Translation: BAF83490.1.
AK292680 mRNA. Translation: BAF85369.1.
AC055822 Genomic DNA. No translation available.
AC100812 Genomic DNA. No translation available.
BC126360 mRNA. Translation: AAI26361.1.
CCDSiCCDS34901.1. [Q13946-2]
CCDS56538.1. [Q13946-1]
RefSeqiNP_001229247.1. NM_001242318.2. [Q13946-1]
NP_002594.1. NM_002603.3. [Q13946-2]
XP_011515842.1. XM_011517540.2. [Q13946-2]
UniGeneiHs.527119.

Genome annotation databases

EnsembliENST00000379419; ENSP00000368730; ENSG00000205268. [Q13946-2]
ENST00000396642; ENSP00000379881; ENSG00000205268. [Q13946-3]
ENST00000401827; ENSP00000385632; ENSG00000205268. [Q13946-1]
GeneIDi5150.
KEGGihsa:5150.
UCSCiuc003xvp.4. human. [Q13946-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L12052 mRNA. Translation: AAA35644.2.
U67932 mRNA. Translation: AAB65772.1.
AF332652 mRNA. Translation: AAK57640.1.
AK290801 mRNA. Translation: BAF83490.1.
AK292680 mRNA. Translation: BAF85369.1.
AC055822 Genomic DNA. No translation available.
AC100812 Genomic DNA. No translation available.
BC126360 mRNA. Translation: AAI26361.1.
CCDSiCCDS34901.1. [Q13946-2]
CCDS56538.1. [Q13946-1]
RefSeqiNP_001229247.1. NM_001242318.2. [Q13946-1]
NP_002594.1. NM_002603.3. [Q13946-2]
XP_011515842.1. XM_011517540.2. [Q13946-2]
UniGeneiHs.527119.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ZKLX-ray1.67A130-482[»]
3G3NX-ray2.40A139-456[»]
4PM0X-ray2.10A130-482[»]
4Y2BX-ray2.20A130-482[»]
ProteinModelPortaliQ13946.
SMRiQ13946.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111176. 4 interactors.
IntActiQ13946. 1 interactor.
STRINGi9606.ENSP00000385632.

Chemistry databases

BindingDBiQ13946.
ChEMBLiCHEMBL3012.
DrugBankiDB00201. Caffeine.
DB00651. Dyphylline.
DB00920. Ketotifen.
GuidetoPHARMACOLOGYi1305.

PTM databases

iPTMnetiQ13946.
PhosphoSitePlusiQ13946.

Polymorphism and mutation databases

BioMutaiPDE7A.
DMDMi3182958.

Proteomic databases

EPDiQ13946.
MaxQBiQ13946.
PaxDbiQ13946.
PeptideAtlasiQ13946.
PRIDEiQ13946.

Protocols and materials databases

DNASUi5150.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000379419; ENSP00000368730; ENSG00000205268. [Q13946-2]
ENST00000396642; ENSP00000379881; ENSG00000205268. [Q13946-3]
ENST00000401827; ENSP00000385632; ENSG00000205268. [Q13946-1]
GeneIDi5150.
KEGGihsa:5150.
UCSCiuc003xvp.4. human. [Q13946-1]

Organism-specific databases

CTDi5150.
DisGeNETi5150.
GeneCardsiPDE7A.
HGNCiHGNC:8791. PDE7A.
HPAiCAB018770.
HPA027340.
MIMi171885. gene.
neXtProtiNX_Q13946.
OpenTargetsiENSG00000205268.
PharmGKBiPA33139.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3689. Eukaryota.
ENOG410XRI7. LUCA.
GeneTreeiENSGT00760000118889.
HOGENOMiHOG000220881.
HOVERGENiHBG053543.
KOiK18436.
OMAiLCDRQTE.
OrthoDBiEOG091G05SK.
PhylomeDBiQ13946.
TreeFamiTF314638.

Enzyme and pathway databases

UniPathwayiUPA00762; UER00747.
BioCyciZFISH:HS02610-MONOMER.
BRENDAi3.1.4.53. 2681.
ReactomeiR-HSA-418555. G alpha (s) signalling events.

Miscellaneous databases

ChiTaRSiPDE7A. human.
EvolutionaryTraceiQ13946.
GeneWikiiPDE7A.
GenomeRNAii5150.
PROiQ13946.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000205268.
CleanExiHS_PDE7A.
ExpressionAtlasiQ13946. baseline and differential.
GenevisibleiQ13946. HS.

Family and domain databases

Gene3Di1.10.1300.10. 1 hit.
InterProiIPR003607. HD/PDEase_dom.
IPR023088. PDEase.
IPR002073. PDEase_catalytic_dom.
IPR023174. PDEase_CS.
[Graphical view]
PfamiPF00233. PDEase_I. 1 hit.
[Graphical view]
PRINTSiPR00387. PDIESTERASE1.
SMARTiSM00471. HDc. 1 hit.
[Graphical view]
PROSITEiPS00126. PDEASE_I. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPDE7A_HUMAN
AccessioniPrimary (citable) accession number: Q13946
Secondary accession number(s): A0AVH6
, A8K436, A8K9G5, O15380, Q96T72
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1998
Last modified: November 2, 2016
This is version 158 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: 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.