Tag Content
SG ID
SG00001994 
UniProt Accession
Theoretical PI
9.03  
Molecular Weight
47268 Da  
Genbank Nucleotide ID
Genbank Protein ID
Gene Name
Cnp 
Gene Synonyms/Alias
Cnp1 
Protein Name
2',3'-cyclic-nucleotide 3'-phosphodiesterase 
Protein Synonyms/Alias
CNPCNPaseEC=3.1.4.37 
Organism
Rattus norvegicus (Rat) 
NCBI Taxonomy ID
10116 
Chromosome Location
chr:10;89519419-89525977;1
View in Ensembl genome browser  
Function in Stage
Function in Cell Type
Description
Temporarily unavailable 
The information of related literatures
1. W. Xia, D. D. Mruk and C. Y. Cheng (2007) C-type natriuretic peptide regulates blood-testis barrier dynamics in adult rat testes. Proc Natl Acad Sci U S A 104(10): 3841-6. 

Abstract
In adult rat testes, the blood-testis barrier (BTB) in the seminiferous epithelium must "open" (or "disassemble") to accommodate the migration of preleptotene spermatocytes from the basal to the adluminal compartment that occurs at stage VIII of the epithelial cycle. However, the molecule(s) and/or mechanism(s) that regulate this event are unknown. In this report, C-type natriuretic peptide (CNP) was shown to be a regulator of BTB dynamics. Although Sertoli and germ cells contributed to the pool of CNP in the seminiferous epithelium, its receptor, natriuretic peptide receptor B, resided almost exclusively in Sertoli cells. CNP also expressed stage-specifically and localized predominantly at the BTB in the seminiferous epithelium at stage VIII of the epithelial cycle. A synthetic CNP-22 peptide, when added to Sertoli cell cultures, was shown to perturb Sertoli cell tight junction in vitro, causing disappearance of BTB-associated proteins (JAM-A, occludin, N-cadherin, and beta-catenin) from the cell-cell interface. This inhibitory effect of CNP on the tight junction was confirmed by transient overexpression of CNP in these cells, which was mediated, at least in part, by accelerating the internalization of BTB integral membrane proteins. To validate these in vitro findings, CNP-22 was administered to testes at a dose of 0.35 or 3.5 mug per testis, which was shown to perturb the BTB integrity In vivo when the barrier function was assessed by monitoring the diffusion of a small molecular probe across the BTB. In summary, CNP secreted by Sertoli and germ cells into the BTB microenvironment regulates BTB dynamics during spermatogenesis. PMID: [17360440] 

2. D. H. Huang, S. W. Zhang, H. Zhao and L. Zhang (2011) The role of C-type natriuretic peptide in rat testes during spermatogenesis. Asian J Androl 13(2): 275-80. 

Abstract
C-type natriuretic peptide (CNP) is a 22-amino acid peptide and act as a local paracrine or autocrine regulator. There is growing evidence that CNP is involved in male reproductive processes. To investigate the role of CNP during spermatogenesis, we measured the mRNA expression of CNP and its specific membrane-bound natriuretic peptide receptor-B (NPR-B) using real-time RT-PCR in the testes of normal rats on different postnatal days. After that spermatogenesis dysfunction model induced by ornidazole was established with the aim to study the correlation of CNP with spermatogenic dysfunction. Then, Sertoli cells from 18- to 22-day-old healthy male rats were cultured in the presence of different CNP concentrations (1x10(-6), 1x10(-7) and 1x10(-8) mol l(-1)), and the mRNA expression levels of androgen-binding protein, inhibin B and transferrin were examined at 0 min, 30 min, 1 h, 2 h, 4 h, 8 h, 12 h, 24 h and 48 h. During the postnatal development of rat testes, the highest mRNA expression levels of CNP and NPR-B were found at postnatal D(0), and the levels then declined gradually, with a second CNP peak at postnatal D(35). In the ornidazole-induced infertile rat testes, CNP gene expression was lower than in the uninduced rats (P<0.05), while NPR-B gene expression was greater (P<0.05). In cultured Sertoli cells, supplementation with CNP stimulated the gene expression of androgen-binding protein/inhibin B/transferrin, particularly at 12 h, and 1x10(-7) mol l(-1) CNP had the highest upregulation effect. The gene expression levels of CNP/NPR-B in rat testes at different postnatal stages and in infertile rat testes indicated that CNP may participate in the physiology and/or pathology related to spermatogenesis. Moreover, CNP regulated endocrine function in Sertoli cells. Taken together, these results showed that CNP is closely tied to spermatogenesis. PMID: [21170077] 

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Figures for illustrating the function of this protein/gene
Ref: W. Xia, D. D. Mruk and C. Y. Cheng (2007) C-type natriuretic peptide regulates blood-testis barrier dynamics in adult rat testes. Proc Natl Acad Sci U S A 104(10): 3841-6. PMID: [17360440]
Ref: W. Xia, D. D. Mruk and C. Y. Cheng (2007) C-type natriuretic peptide regulates blood-testis barrier dynamics in adult rat testes. Proc Natl Acad Sci U S A 104(10): 3841-6. PMID: [17360440]
Ref: W. Xia, D. D. Mruk and C. Y. Cheng (2007) C-type natriuretic peptide regulates blood-testis barrier dynamics in adult rat testes. Proc Natl Acad Sci U S A 104(10): 3841-6. PMID: [17360440]
Ref: W. Xia, D. D. Mruk and C. Y. Cheng (2007) C-type natriuretic peptide regulates blood-testis barrier dynamics in adult rat testes. Proc Natl Acad Sci U S A 104(10): 3841-6. PMID: [17360440]
Function
May participate in RNA metabolism in the myelinatingcell, CNP is the third most abundant protein in central nervoussystem myelin (By similarity). 
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Subcellular Location
Membrane; Lipid-anchor. Melanosome (Bysimilarity). Note=Firmly bound to membrane structures of brainwhite matter. 
Tissue Specificity
 
Gene Ontology
GO IDGO termEvidence
GO:0005615 C:extracellular space IEA:Compara.
GO:0042470 C:melanosome IEA:UniProtKB-SubCell.
GO:0005624 C:membrane fraction IEA:Compara.
GO:0005874 C:microtubule IEA:Compara.
GO:0005902 C:microvillus IDA:RGD.
GO:0005743 C:mitochondrial inner membrane IDA:RGD.
GO:0005741 C:mitochondrial outer membrane IDA:RGD.
GO:0035748 C:myelin sheath abaxonal region IDA:RGD.
GO:0035749 C:myelin sheath adaxonal region IDA:RGD.
GO:0048471 C:perinuclear region of cytoplasm IDA:RGD.
GO:0005886 C:plasma membrane IDA:RGD.
GO:0031143 C:pseudopodium IDA:RGD.
GO:0004113 F:2',3'-cyclic-nucleotide 3'-phosphodiesterase activity IDA:RGD.
GO:0030551 F:cyclic nucleotide binding IDA:RGD.
GO:0003723 F:RNA binding IEA:UniProtKB-KW.
GO:0008344 P:adult locomotory behavior IEA:Compara.
GO:0007568 P:aging IEP:RGD.
GO:0007409 P:axonogenesis IEA:Compara.
GO:0009214 P:cyclic nucleotide catabolic process IEA:InterPro.
GO:0030900 P:forebrain development IEP:RGD.
GO:0000226 P:microtubule cytoskeleton organization IMP:RGD.
GO:0046902 P:regulation of mitochondrial membrane permeability IMP:RGD.
GO:0032496 P:response to lipopolysaccharide IEP:RGD.
GO:0009636 P:response to toxin IEA:Compara.
GO:0016070 P:RNA metabolic process IEA:InterPro.
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Interpro
IPR008431;    CNPase.
IPR009097;    RNA_ligase/cNuc_Pdiesterase.
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Pfam
PF05881;    CNPase;    1.
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SMART
PROSITE
PRINTS
Created Date
18-Oct-2012 
Record Type
Experiment identified 
Protein sequence Annotation
CHAIN         1    420       2',3'-cyclic-nucleotide 3'-
                             phosphodiesterase.
                             /FTId=PRO_0000089963.
ACT_SITE    250    250       Proton acceptor.
ACT_SITE    329    329       Proton donor.
BINDING     252    252       Substrate (By similarity).
BINDING     331    331       Substrate (By similarity).
MOD_RES     110    110       Phosphotyrosine (By similarity).
MOD_RES     169    169       Phosphoserine (By similarity).
MOD_RES     372    372       Phosphotyrosine (By similarity).
LIPID       417    417       S-farnesyl cysteine (Probable).
MUTAGEN     250    250       H->L: Reduces activity 15000-fold.
MUTAGEN     252    252       T->A: Reduces activity 100-fold.
MUTAGEN     329    329       H->L: Reduces activity 15000-fold.
MUTAGEN     331    331       T->A: Reduces activity 700-fold.
MUTAGEN     344    344       G->A: Alters secondary structure and
                             lowers activity.
MUTAGEN     417    417       C->S: Abolishes binding to myelin.
STRAND      187    193
HELIX       195    213
HELIX       216    219
HELIX       222    225
STRAND      229    231
HELIX       237    240
STRAND      250    255
TURN        257    260
STRAND      261    263
HELIX       264    268
HELIX       271    276
STRAND      280    290
STRAND      295    299
HELIX       303    307
STRAND      313    315
STRAND      317    320
STRAND      326    331
HELIX       340    355
STRAND      361    366
STRAND      369    373
STRAND      379    396
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Nucleotide Sequence
Length: 2019 bp   Go to nucleotide: FASTA
Protein Sequence
Length: 420 bp   Go to amino acid: FASTA
The verified Protein-Protein interaction information
UniProt
Gene Symbol Ref Databases
Rad23bIntAct 
Other Protein-Protein interaction resources
String database  
View Microarray data
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