SpermatogenesisOnline 1.0

Tag Content
SG ID
SG00008764 
UniProt Accession
Theoretical PI
7.65  
Molecular Weight
93144 Da  
Genbank Nucleotide ID
Genbank Protein ID
Gene Name
Postn 
Gene Synonyms/Alias
Osf2 
Protein Name
Periostin 
Protein Synonyms/Alias
PN Osteoblast-specific factor 2;OSF-2Flags: Precursor 
Organism
Mus musculus (Mouse) 
NCBI Taxonomy ID
10090 
Chromosome Location
chr:3;54165031-54194961;1
View in Ensembl genome browser  
Function in Stage
Uncertain 
Function in Cell Type
Uncertain 
Probability (GAS) of Function in Spermatogenesis
0.136610657 
The probability was calculated by GAS algorithm, ranging from 0 to 1. The closer it is to 1, the more possibly it functions in spermatogenesis.
Description
Temporarily unavailable 
Abstract of related literatures
1. A cDNA library prepared from the mouse osteoblastic cell line MC3T3-E1 was screened for the presence of specifically expressed genes by employing a combined subtraction hybridization/differential screening approach. A cDNA was identified and sequenced which encodes a protein designated osteoblast-specific factor 2 (OSF-2) comprising 811 amino acids. OSF-2 has a typical signal sequence, followed by a cysteine-rich domain, a fourfold repeated domain and a C-terminal domain. The protein lacks a typical transmembrane region. The fourfold repeated domain of OSF-2 shows homology with the insect protein fasciclin I. RNA analyses revealed that OSF-2 is expressed in bone and to a lesser extent in lung, but not in other tissues. Mouse OSF-2 cDNA was subsequently used as a probe to clone the human counterpart. Mouse and human OSF-2 show a high amino acid sequence conservation except for the signal sequence and two regions in the C-terminal domain in which 'in-frame' insertions or deletions are observed, implying alternative splicing events. On the basis of the amino acid sequence homology with fasciclin I, we suggest that OSF-2 functions as a homophilic adhesion molecule in bone formation. PMID: [8363580] 

2. This study describes comprehensive polling of transcription start and termination sites and analysis of previously unidentified full-length complementary DNAs derived from the mouse genome. We identify the 5' and 3' boundaries of 181,047 transcripts with extensive variation in transcripts arising from alternative promoter usage, splicing, and polyadenylation. There are 16,247 new mouse protein-coding transcripts, including 5154 encoding previously unidentified proteins. Genomic mapping of the transcriptome reveals transcriptional forests, with overlapping transcription on both strands, separated by deserts in which few transcripts are observed. The data provide a comprehensive platform for the comparative analysis of mammalian transcriptional regulation in differentiation and development. PMID: [16141072] 

3. The National Institutes of Health's Mammalian Gene Collection (MGC) project was designed to generate and sequence a publicly accessible cDNA resource containing a complete open reading frame (ORF) for every human and mouse gene. The project initially used a random strategy to select clones from a large number of cDNA libraries from diverse tissues. Candidate clones were chosen based on 5'-EST sequences, and then fully sequenced to high accuracy and analyzed by algorithms developed for this project. Currently, more than 11,000 human and 10,000 mouse genes are represented in MGC by at least one clone with a full ORF. The random selection approach is now reaching a saturation point, and a transition to protocols targeted at the missing transcripts is now required to complete the mouse and human collections. Comparison of the sequence of the MGC clones to reference genome sequences reveals that most cDNA clones are of very high sequence quality, although it is likely that some cDNAs may carry missense variants as a consequence of experimental artifact, such as PCR, cloning, or reverse transcriptase errors. Recently, a rat cDNA component was added to the project, and ongoing frog (Xenopus) and zebrafish (Danio) cDNA projects were expanded to take advantage of the high-throughput MGC pipeline. PMID: [15489334] 

4. We had previously identified the cDNA for a novel protein called osteoblast-specific factor 2 (OSF-2) from an MC3T3-E1 cDNA library using subtraction hybridization and differential screening techniques. Here we describe the localization, regulation, and potential function of this protein. Immunohistochemistry using specific antiserum revealed that in adult mice, the protein is preferentially expressed in periosteum and periodontal ligament, indicating its tissue specificity and a potential role in bone and tooth formation and maintenance of structure. Based on this observation and the fact that other proteins have been called OSF-2, the protein was renamed "periostin." Western blot analysis showed that periostin is a disulfide linked 90 kDa protein secreted by osteoblasts and osteoblast-like cell lines. Nucleotide sequence revealed four periostin transcripts that differ in the length of the C-terminal domain, possibly caused by alternative splicing events. Reverse transcription- polymerase chain reaction analysis revealed that these isoforms are not expressed uniformly but are differentially expressed in various cell lines. Both purified periostin protein and the periostin-Fc recombinant protein supported attachment and spreading of MC3T3-E1 cells, and this effect was impaired by antiperiostin antiserum, suggesting that periostin is involved in cell adhesion. The protein is highly homologous to betaig-h3, a molecule induced by transforming growth factor beta (TGF-beta) that promotes the adhesion and spreading of fibroblasts. Because TGF-beta has dramatic effects on periosteal expansion and the recruitment of osteoblast precursors, this factor was tested for its effects on periostin expression. By Western blot analysis, TGF-beta increased periostin expression in primary osteoblast cells. Together, these data suggest that periostin may play a role in the recruitment and attachment of osteoblast precursors in the periosteum. PMID: [10404027] 

5. Osteoblast-specific factor 2 (OSF-2) is a approximately 90-kDa protein selectively expressed in bone. OSF-2 cDNA was recently isolated from mouse and human cDNA libraries and shows limited sequence homology with fasciclin I, a cell adhesion protein expressed in insect nerve cells. Here we describe the expression of recombinant murine OSF-2 (rmOSF-2) in a baculovirus/insect cell system. Western blotting analysis employing polyclonal antiserum raised against a C-terminal synthetic OSF-2 peptide detected a protein of approximately 90-kDa as early as 2 days after infection of Sf9 cells with the recombinant virus. Tunicamycin treatment of infected cells resulted in a mobility shift of OSF-2 (approximately 90-kDa band) on Western blots. N-Glycanase digestion resulted in the same mobility shift of OSF-2, indicating that rmOSF-2 expressed in insect cells is N-glycosylated. However, OSF-2 was insensitive to endoglycosidase H digestion while a major fraction of this protein had affinity for concanavalin A. Finally, it was demonstrated that rmOSF-2 was able to bind to heparin. This finding suggests that OSF-2 might be associated with the bone extracellular matrix after secretion by osteoblasts and participate in cell adhesion and/or cell communication. The establishment of the baculovirus expression system with a high productivity of recombinant OSF-2 (around 40 micrograms/ml at maximum) and its heparin binding properties should allow us to obtain large amounts of rmOSF-2. PMID: [7663166] 

6. Periostin was originally isolated as a osteoblast-specific factor that functions as a cell adhesion molecule for preosteoblasts and is thought to be involved in osteoblast recruitment, attachment and spreading. Additionally, periostin expression has previously been shown to be significantly increased by both transforming growth factor beta-1(TGFbeta1) and bone morphogenetic protein (BMP)-2. Likewise the endocardial cushions that form within embryonic heart tube (embryonic day (E)10-13) are formed by the recruitment, attachment and spreading of endocardial cells into the overlying extracellular matrix, in response to secreted growth factors of the TGFbeta and BMP families. In order to determine whether periostin is similarly involved in heart morphogenesis, in situ hybridization and reverse transcription-polymerase chain reaction were used to detect periostin mRNA expression in the developing mouse heart. We show for the first time that periostin mRNA is expressed in the developing mouse embryonic and fetal heart, and that it is localized to the endocardial cushions that ultimately divide the primitive heart tube into a four-chambered heart. PMID: [11335131] 

7. The modification of glutamic acid residues to gamma-carboxyglutamic acid (Gla) is a post-translational modification catalyzed by the vitamin K-dependent enzyme gamma-glutamylcarboxylase. Despite ubiquitous expression of the gamma-carboxylation machinery in mammalian tissues, only 12 Gla-containing proteins have so far been identified in humans. Because bone tissue is the second most abundant source of Gla-containing proteins after the liver, we sought to identify Gla proteins secreted by bone marrow-derived mesenchymal stromal cells (MSCs). We used a proteomics approach to screen the secretome of MSCs with a combination of two-dimensional gel electrophoresis and tandem mass spectrometry. The most abundant Gla-containing protein secreted by MSCs was identified as periostin, a previously unrecognized gamma-carboxylated protein. In silico amino acid sequence analysis of periostin demonstrated the presence of four consensus gamma-carboxylase recognition sites embedded within fasciclin-like protein domains. The carboxylation of periostin was confirmed by immunoprecipitation and purification of the recombinant protein. Carboxylation of periostin could be inhibited by warfarin in MSCs, demonstrating its dependence on the presence of vitamin K. We were able to demonstrate localization of carboxylated periostin to bone nodules formed by MSCs in vitro, suggesting a role in extracellular matrix mineralization. Our data also show that another fasciclin I-like protein, betaig-h3, contains Gla. In conclusion, periostin is a member of a novel vitamin K-dependent gamma-carboxylated protein family characterized by the presence of fasciclin domains. Furthermore, carboxylated periostin is produced by bone-derived cells of mesenchymal lineage and is abundantly found in mineralized bone nodules in vitro. PMID: [18450759] 

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Function
Binds to heparin. Induces cell attachment and spreadingand plays a role in cell adhesion. May play a role inextracellular matrix mineralization. 
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Subcellular Location
Secreted, extracellular space, extracellularmatrix. 
Tissue Specificity
Preferentially expressed in periosteum andperiodontal ligament. Also expressed in the developing and adultheart. 
Gene Ontology
GO IDGO termEvidence
GO:0005578 C:proteinaceous extracellular matrix IDA:UniProtKB.
GO:0008201 F:heparin binding IDA:UniProtKB.
GO:0007155 P:cell adhesion IDA:UniProtKB.
GO:0030198 P:extracellular matrix organization IMP:MGI.
GO:0008593 P:regulation of Notch signaling pathway IMP:MGI.
GO:0009888 P:tissue development IMP:MGI.
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Interpro
IPR011489;    EMI_domain.
IPR000782;    FAS1_domain.
IPR016666;    TGFb-ind_bIGH3/osteoblast_fac2.
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Pfam
PF02469;    Fasciclin;    4.
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SMART
SM00554;    FAS1;    4.
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PROSITE
PS51041;    EMI;    1.
PS50213;    FAS1;    4.
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PRINTS
Created Date
18-Oct-2012 
Record Type
GAS predicted 
Sequence Annotation
SIGNAL        1     23       Potential.
CHAIN        24    838       Periostin.
                             /FTId=PRO_0000008790.
DOMAIN       42     96       EMI.
DOMAIN       99    232       FAS1 1.
DOMAIN      236    367       FAS1 2.
DOMAIN      370    494       FAS1 3.
DOMAIN      498    630       FAS1 4.
MOD_RES     126    126       4-carboxyglutamate (Potential).
MOD_RES     127    127       4-carboxyglutamate (Potential).
MOD_RES     129    129       4-carboxyglutamate (Potential).
MOD_RES     142    142       4-carboxyglutamate (Potential).
MOD_RES     156    156       4-carboxyglutamate (Potential).
MOD_RES     162    162       4-carboxyglutamate (Potential).
MOD_RES     244    244       4-carboxyglutamate (Potential).
MOD_RES     246    246       4-carboxyglutamate (Potential).
MOD_RES     263    263       4-carboxyglutamate (Potential).
MOD_RES     279    279       4-carboxyglutamate (Potential).
MOD_RES     282    282       4-carboxyglutamate (Potential).
MOD_RES     290    290       4-carboxyglutamate (Potential).
MOD_RES     300    300       4-carboxyglutamate (Potential).
MOD_RES     315    315       4-carboxyglutamate (Potential).
MOD_RES     324    324       4-carboxyglutamate (Potential).
MOD_RES     327    327       4-carboxyglutamate (Potential).
MOD_RES     498    498       4-carboxyglutamate (Potential).
MOD_RES     519    519       4-carboxyglutamate (Potential).
MOD_RES     549    549       4-carboxyglutamate (Potential).
MOD_RES     550    550       4-carboxyglutamate (Potential).
MOD_RES     552    552       4-carboxyglutamate (Potential).
MOD_RES     580    580       4-carboxyglutamate (Potential).
CARBOHYD    601    601       N-linked (GlcNAc...) (Probable).
DISULFID     46     82       By similarity.
DISULFID     62     71       By similarity.
DISULFID     81     94       By similarity.
VAR_SEQ     672    699       TTKIITKVVEPKIKVIQGSLQPIIKTEG -> R (in
                             isoform 2 and isoform 5).
                             /FTId=VSP_050666.
VAR_SEQ     759    812       Missing (in isoform 4).
                             /FTId=VSP_050667.
VAR_SEQ     785    812       Missing (in isoform 3 and isoform 5).
                             /FTId=VSP_050668.
CONFLICT    346    346       K -> R (in Ref. 2; BAC27122).
CONFLICT    541    541       D -> N (in Ref. 2; BAC27122).
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Nucleotide Sequence
Length: 3187 bp   Go to nucleotide: FASTA
Protein Sequence
Length: 838 bp   Go to amino acid: FASTA
The verified Protein-Protein interaction information
UniProt
 Gene Symbol Ref Databases
Other Protein-Protein interaction resources
String database  
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