SpermatogenesisOnline 1.0
 

Tag Content
SG ID
SG00002046 
UniProt Accession
Theoretical PI
5.14  
Molecular Weight
93439 Da  
Genbank Nucleotide ID
Genbank Protein ID
Gene Name
Pde4a 
Gene Synonyms/Alias
 
Protein Name
cAMP-specific 3',5'-cyclic phosphodiesterase 4A 
Protein Synonyms/Alias
EC=3.1.4.17 DPDE2; 
Organism
Rattus norvegicus (Rat) 
NCBI Taxonomy ID
10116 
Chromosome Location
chr:8;20192744-20241581;1
View in Ensembl genome browser  
Function in Stage
Function in Cell Type
Description
Temporarily unavailable 
The information of related literatures
1. M. Salanova, S. Y. Chun, S. Iona, C. Puri, M. Stefanini and M. Conti (1999) Type 4 cyclic adenosine monophosphate-specific phosphodiesterases are expressed in discrete subcellular compartments during rat spermiogenesis. Endocrinology 140(5): 2297-306. 

Abstract
The type 4 cAMP-specific phosphodiesterases (PDE4) are a family of closely related enzymes with similar catalytic domains and divergent amino- and carboxyl-terminus domains. Multiple PDE proteins with heterogeneous amino termini are derived from each gene. To understand the significance of this heterogeneity, the expression and localization of variants derived from PDE4A and PDE4D genes was investigated during spermatogenesis in the rat. RNase protection analysis with mRNA for testes at different ages of development showed that two transcripts (PDE4D1 and PDE4D2) are expressed at day 10 and 15 of age and become undetectable thereafter. An additional PDE4D transcript appears at day 30 and increased during testid maturation. This latter transcript codes for a long variant of the PDE4D gene and is expressed in germ cells as demonstrated by RNase protection with RNA from isolated pachytene spermatocytes and round spermatids. The presence of a corresponding PDE4D protein with a molecular mass of 98 kDa was established by immunoprecipitation and Western blot analysis with antibodies specific for PDE4D and by immunoaffinity chromatography purification of the 98 kDa variant from isolated germ cells. PDE4A transcripts were also expressed in pachytene spermatocytes and round spermatids. Two polypeptides encoded by these PDE4A transcripts were expressed in pachytene spermatocytes, reached a maximum in round spermatids, and declined thereafter. Immunofluorescence analysis demonstrated a localization of the PDE4D protein in the manchette and in a periacrosomal region of the developing spermatid, a localization confirmed by immunogold electron microscopy. Conversely, the PDE4A was mostly soluble in the cytoplasm of round spermatids. These data demonstrate that PDE4D and PDE4A variants are expressed at different stages and localized in distinct subcellular structures of developing spermatids. Different properties of the mRNAs derived from the two genes and localization signals are responsible for the temporal and spatial expression of the different PDE4 isoenzymes. PMID: [10218983] 

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Figures for illustrating the function of this protein/gene
Ref: M. Salanova, S. Y. Chun, S. Iona, C. Puri, M. Stefanini and M. Conti (1999) Type 4 cyclic adenosine monophosphate-specific phosphodiesterases are expressed in discrete subcellular compartments during rat spermiogenesis. Endocrinology 140(5): 2297-306. PMID: [10218983]
Ref: M. Salanova, S. Y. Chun, S. Iona, C. Puri, M. Stefanini and M. Conti (1999) Type 4 cyclic adenosine monophosphate-specific phosphodiesterases are expressed in discrete subcellular compartments during rat spermiogenesis. Endocrinology 140(5): 2297-306. PMID: [10218983]
Ref: M. Salanova, S. Y. Chun, S. Iona, C. Puri, M. Stefanini and M. Conti (1999) Type 4 cyclic adenosine monophosphate-specific phosphodiesterases are expressed in discrete subcellular compartments during rat spermiogenesis. Endocrinology 140(5): 2297-306. PMID: [10218983]
Ref: M. Salanova, S. Y. Chun, S. Iona, C. Puri, M. Stefanini and M. Conti (1999) Type 4 cyclic adenosine monophosphate-specific phosphodiesterases are expressed in discrete subcellular compartments during rat spermiogenesis. Endocrinology 140(5): 2297-306. PMID: [10218983]
Ref: M. Salanova, S. Y. Chun, S. Iona, C. Puri, M. Stefanini and M. Conti (1999) Type 4 cyclic adenosine monophosphate-specific phosphodiesterases are expressed in discrete subcellular compartments during rat spermiogenesis. Endocrinology 140(5): 2297-306. PMID: [10218983]
Function
Hydrolyzes the second messenger cAMP, which is a keyregulator of many important physiological processes (Bysimilarity). 
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Subcellular Location
Cytoplasm, perinuclear region (Bysimilarity). 
Tissue Specificity
Isoform 2 is testis specific. 
Gene Ontology
GO IDGO termEvidence
GO:0005634 C:nucleus IDA:RGD.
GO:0048471 C:perinuclear region of cytoplasm IDA:RGD.
GO:0004115 F:3',5'-cyclic-AMP phosphodiesterase activity IDA:RGD.
GO:0046872 F:metal ion binding IEA:UniProtKB-KW.
GO:0006198 P:cAMP catabolic process IDA:UniProtKB.
GO:0042493 P:response to drug IEP:RGD.
GO:0007165 P:signal transduction IEA:InterPro.
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Interpro
IPR003607;    HD/PDEase_dom.
IPR023088;    PDEase.
IPR002073;    PDEase_catalytic_dom.
IPR023174;    PDEase_CS.
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Pfam
PF00233;    PDEase_I;    1.
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SMART
SM00471;    HDc;    1.
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PROSITE
PS00126;    PDEASE_I;    1.
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PRINTS
PR00387;    PDIESTERASE1.;   
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Created Date
18-Oct-2012 
Record Type
Experiment identified 
Protein sequence Annotation
CHAIN         1    844       cAMP-specific 3',5'-cyclic
                             phosphodiesterase 4A.
                             /FTId=PRO_0000198808.
NP_BIND     419    423       cAMP (By similarity).
REGION      317    710       Catalytic (By similarity).
ACT_SITE    419    419       Proton donor (By similarity).
METAL       423    423       Divalent metal cation 1 (By similarity).
METAL       459    459       Divalent metal cation 1 (By similarity).
METAL       460    460       Divalent metal cation 1 (By similarity).
METAL       460    460       Divalent metal cation 2 (By similarity).
METAL       577    577       Divalent metal cation 1 (By similarity).
BINDING     460    460       cAMP (By similarity).
BINDING     577    577       cAMP (By similarity).
BINDING     628    628       cAMP (By similarity).
SITE         69     70       Cleavage; by caspase-3 (By similarity).
SITE        580    580       Binds AMP, but not cAMP (By similarity).
MOD_RES     147    147       Phosphoserine; by MAPKAPK2.
MOD_RES     160    160       Phosphoserine (By similarity).
MOD_RES     672    672       Phosphoserine (By similarity).
MOD_RES     674    674       Phosphoserine (By similarity).
CROSSLNK    344    344       Glycyl lysine isopeptide (Lys-Gly)
                             (interchain with G-Cter in SUMO) (By
                             similarity).
VAR_SEQ       1    318       Missing (in isoform 5).
                             /FTId=VSP_004569.
VAR_SEQ       1    259       Missing (in isoform 4).
                             /FTId=VSP_004568.
VAR_SEQ       1    234       Missing (in isoform 3).
                             /FTId=VSP_004566.
VAR_SEQ       1    102       MEPPAAPSERSLSLSLPGPREGQATLKPPPQHLWRQPRTPI
                             RIQQRGYPDSAERSETERSPHRPIERADAVDTGDRPGLRTT
                             RMSWPSSFHGTGTGGGSSRR -> MPSRKRLTLPRIFIVRK
                             NGNS (in isoform 2).
                             /FTId=VSP_004565.
VAR_SEQ       1    102       MEPPAAPSERSLSLSLPGPREGQATLKPPPQHLWRQPRTPI
                             RIQQRGYPDSAERSETERSPHRPIERADAVDTGDRPGLRTT
                             RMSWPSSFHGTGTGGGSSRR -> ALPLGPESLTHFSFSEE
                             DTLRHPPGRCVS (in isoform 6).
                             /FTId=VSP_038187.
VAR_SEQ     235    256       WCLEQLETMQTYRSVSEMASHK -> MPLVDFFCETCSKPW
                             LVGWWDQ (in isoform 3).
                             /FTId=VSP_004567.
VAR_SEQ     354    386       Missing (in isoform 5).
                             /FTId=VSP_004570.
MUTAGEN     147    147       S->A: Abolishes phosphorylation by
                             MAPKAPK2.
MUTAGEN     161    161       S->A: Does not affect phosphorylation by
                             MAPKAPK2.
CONFLICT    130    130       A -> R (in Ref. 5; AAF14352).
CONFLICT    465    466       GV -> AL (in Ref. 4; AAA41848/AAA41823).
CONFLICT    603    604       GD -> AH (in Ref. 4; AAA41848/AAA41823).
CONFLICT    833    833       A -> T (in Ref. 1; AAC37699/AAA41101/
                             AAA41102 and 5; AAF14352).
HELIX       781    787
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Nucleotide Sequence
Length: 2914 bp   Go to nucleotide: FASTA
Protein Sequence
Length: 844 bp   Go to amino acid: FASTA
The verified Protein-Protein interaction information
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