SpermatogenesisOnline 1.0

Tag Content
SG ID
SG00009748 
UniProt Accession
Theoretical PI
4.31  
Molecular Weight
32459 Da  
Genbank Nucleotide ID
Genbank Protein ID
Gene Name
Spp1 
Gene Synonyms/Alias
Eta-1, Op, Spp-1 
Protein Name
Osteopontin 
Protein Synonyms/Alias
2AR; Bone sialoprotein 1; Calcium oxalate crystal growth inhibitor protein; Early T-lymphocyte activation 1 protein; Minopontin; Secreted phosphoprotein 1;SPP-1Flags: Precursor 
Organism
Mus musculus (Mouse) 
NCBI Taxonomy ID
10090 
Chromosome Location
chr:5;104864137-104870069;1
View in Ensembl genome browser  
Function in Stage
Uncertain 
Function in Cell Type
Uncertain 
Probability (GAS) of Function in Spermatogenesis
0.155126558 
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 murine mRNA (provisionally called 2ar) is described whose abundance is greatly increased by the tumor promoter 12-O-tetradecanoylphorbol 13-acetate both in JB6 epidermal cells in vitro and in epidermis in vivo. We have previously shown induction of 2ar in epidermal or fibroblast cell lines by tumor promoters, growth factors, and transformation with H-ras. The 2ar mRNA appears to be derived from a single copy gene. It encodes the mouse homolog of rat osteopontin, a 41.5-kDa glycosylated bone phosphoprotein that binds to fibroblasts and osteosarcoma cells and to hydroxylapatite (bone matrix). The rat and mouse sequences are 84% identical at the amino acid level and 87% identical at the nucleotide level. Many of the primary structural features are conserved, including a run of 9-10 aspartic residues and a Gly-Arg-Gly-Asp-Ser cell adhesion sequence. Antiserum raised against portions of the predicted polypeptide immunoprecipitated proteins of apparent Mr 55,000-70,000 both from reticulocyte lysates containing the translation products of hybrid-selected mRNA and from cell culture medium containing metabolically labeled proteins secreted by JB6 cells. The results presented here demonstrate that osteopontin is identical to a transformation-associated phosphoprotein whose level of expression by cultured cells and abundance in human sera has been correlated with tumorigenicity. These results suggest a role for osteopontin in carcinogenesis. The murine version of osteopontin has been given the formal name "secreted phosphoprotein 1" and the designation spp. PMID: [2722855] 

2. We describe a murine cDNA, designated Early T lymphocyte activation 1 (ETA-1) which is abundantly expressed after activation of T cells. Eta-1 encodes a highly acidic secreted product having structural features of proteins that bind to cellular adhesion receptors. The Eta-1 gene maps to a locus on murine chromosome 5 termed Ric that confers resistance to infection by Rickettsia tsutsugamushi (RT), an obligate intracellular bacterium that is the etiological agent for human scrub typhus. With one exception, inbred mouse strains that expressed the Eta-1a allele were resistant to RT infection (RicR), and inbred strains expressing the Eta-1b allele were susceptible (RicS). These findings suggest that Eta-1 is the gene inferred from previous studies of the Ric locus (5). Genetic resistance to RT infection is associated with a strong Eta-1 response in vivo and inhibition of early bacterial replication. Eta-1 gene expression appears to be part of a surprisingly rapid T cell-dependent response to bacterial infection that may precede classical forms of T cell-dependent immunity. PMID: [2787378] 


4. Murine macrophage cell lines and resident macrophages showed various levels of expression of the murine osteopontin (OP) gene, and macrophage stimulating agents were found to enhance transcription of the gene with kinetics which are unique for each stimulator. The organization of the murine OP gene was determined. The gene comprises six exons and five introns and spans approximately 4.8 kilobases. Exon 1 contains the 16 amino acids of the leader sequence. Exons 2, 3, 4, 5, and 6 encode 12, 27, 14, 94, and 129 amino acid residues, respectively. Exon 5 encodes regions containing 10 consecutive Asp amino acid residues and a Gly-Arg-Gly-Asp-Ser peptide. Exon 6 encodes the C-terminal half of OP and contains no 15- and 54-base pair nucleotide sequences which are deleted in murine OP cDNA compared to that of rat OP cDNA. Since Southern blot analysis indicated that the OP gene is a single copy, it is obvious that the murine OP cDNA has the sequence previously determined (Miyazaki, Y., Setoguchi, M., Yoshida, S., Higuchi, Y., Akizuki, S., and Yamamoto, S. (1989) Nucleic Acids Res. 17, 3298). A comparison with the cDNA sequences reported previously suggested the presence of nucleotide sequence polymorphisms. The 5' end of the murine OP gene was defined by primer extension and S1 nuclease mapping. Sequence analysis of the 5'-flanking DNA revealed the presence of many potential regulatory motifs. PMID: [2387863] 

5. 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] 

6. Urine contains proteins that inhibit the growth of calcium oxalate (CaOx) crystals and may prevent the formation of kidney stones. We have identified a potent crystal growth inhibitor in the conditioned media from primary cultures of mouse kidney cortical cells. Conditioned media, incubated with the kidney cells for 6-72 h, was assayed for crystal growth inhibition; inhibitory activity increased 15-fold by 24 h. Inhibitory activity was purified from serum-free media containing proteinase inhibitors using anion-exchange and gel-filtration chromatography. A single band of molecular weight 80,000 daltons was seen after SDS-polyacrylamide gel electrophoresis. The sequence of the N-terminal 21 amino acids of this protein matched that of osteopontin (OP), a phosphoprotein initially isolated from bone matrix. Antisera raised to fusion proteins produced by plasmids containing the N-terminal or C-terminal portions of OP cDNA also cross-reacted with the protein purified from cell culture media on western blots. The effect of the purified protein on the growth of CaOx crystals was measured using a constant composition assay. A 50% inhibition of growth occurred at a protein concentration of 0.85 micrograms/ml, and the dissociation constant of the protein with respect to CaOx crystal was 3.7 x 10(-8) M. The concentration of OP in mouse urine, measured using antibodies raised to the purified protein, was approximately 8 micrograms/ml. We conclude that OP is synthesized by kidney cortical tubule cells and functions as a crystal growth inhibitory protein in urine. PMID: [1414495] 

7. The Eta-1 gene specifies a secreted product of activated T cells and is associated with genetic resistance to infection by an obligate intracellular bacterium. Previous studies have suggested that eta-1 might affect the ability of macrophages to migrate to the site of bacterial infection and/or to inhibit intracellular bacterial growth. We therefore examined the interaction of eta-1 with macrophages in vitro and in vivo. We find that macrophages express approximately 10(4) eta-1 receptors/cell and each receptor has a Kd of approximately 5 x 10(-10) M. The subsequence of eta-1 containing an RGD motif is required for binding because a synthetic peptide containing the eta-1 RGD domain inhibited protein attachment to macrophages. We also found that subcutaneous inoculation of mice with eta-1 resulted in a cellular infiltrate comprised primarily of macrophages. We propose that the interaction between eta-1 and its receptor on macrophages results in a change in macrophage physiology resulting in accumulation of these cells at extravascular sites. PMID: [2351930] 

8. Cell-mediated (type-1) immunity is necessary for immune protection against most intracellular pathogens and, when excessive, can mediate organ-specific autoimmune destruction. Mice deficient in Eta-1 (also called osteopontin) gene expression have severely impaired type-1 immunity to viral infection [herpes simplex virus-type 1 (KOS strain)] and bacterial infection (Listeria monocytogenes) and do not develop sarcoid-type granulomas. Interleukin-12 (IL-12) and interferon-gamma production is diminished, and IL-10 production is increased. A phosphorylation-dependent interaction between the amino-terminal portion of Eta-1 and its integrin receptor stimulated IL-12 expression, whereas a phosphorylation-independent interaction with CD44 inhibited IL-10 expression. These findings identify Eta-1 as a key cytokine that sets the stage for efficient type-1 immune responses through differential regulation of macrophage IL-12 and IL-10 cytokine expression. PMID: [10657301] 

9. Protein phosphorylation is a complex network of signaling and regulatory events that affects virtually every cellular process. Our understanding of the nature of this network as a whole remains limited, largely because of an array of technical challenges in the isolation and high-throughput sequencing of phosphorylated species. In the present work, we demonstrate that a combination of tandem phosphopeptide enrichment methods, high performance MS, and optimized database search/data filtering strategies is a powerful tool for surveying the phosphoproteome. Using our integrated analytical platform, we report the identification of 5,635 nonredundant phosphorylation sites from 2,328 proteins from mouse liver. From this list of sites, we extracted both novel and known motifs for specific Ser/Thr kinases including a "dipolar" motif. We also found that C-terminal phosphorylation was more frequent than at any other location and that the distribution of potential kinases for these sites was unique. Finally, we identified double phosphorylation motifs that may be involved in ordered phosphorylation. PMID: [17242355] 

10. Kinases play a prominent role in tumor development, pointing to the presence of specific phosphorylation patterns in tumor tissues. Here, we investigate whether recently developed high resolution mass spectrometric (MS) methods for proteome and phosphoproteome analysis can also be applied to solid tumors. As tumor model, we used TG3 mutant mice carrying skin melanomas. At total of 100 microg of solid tumor lysate yielded a melanoma proteome of 4443 identified proteins, including at least 88 putative melanoma markers previously found by cDNA microarray technology. Analysis of 2 mg of lysate from dissected melanoma with titansphere chromatography and 8 mg with strong cation exchange together resulted in the identification of more than 5600 phosphorylation sites on 2250 proteins. The phosphoproteome included many hits from pathways important in melanoma. One-month storage at -80 degrees C did not significantly decrease the number of identified phosphorylation sites. Thus, solid tumor can be analyzed by MS-based proteomics with similar efficiency as cell culture models and in amounts compatible with biopsies. PMID: [19367708] 

11. The ability of macrophages to clear pathogens and elicit a sustained immune response is regulated by various cytokines, including interferon-gamma (IFN-gamma). To investigate the molecular mechanisms by which IFN-gamma modulates phagosome functions, we profiled the changes in composition, abundance, and phosphorylation of phagosome proteins in resting and activated macrophages by using quantitative proteomics and bioinformatics approaches. We identified 2415 phagosome proteins together with 2975 unique phosphorylation sites with a high level of sensitivity. Using network analyses, we determined that IFN-gamma delays phagosomal acquisition of lysosomal hydrolases and peptidases for the gain of antigen presentation. Furthermore, this gain in antigen presentation is dependent on phagosomal networks of the actin cytoskeleton and vesicle-trafficking proteins, as well as Src kinases and calpain proteases. Major histocompatibility complex class I antigen-presentation assays validated the molecular participation of these networks in the enhanced capacity of IFN-gamma-activated macrophages to crosspresent exogenous antigens to CD8(+) T cells. PMID: [19144319] 

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Function
Acts as a cytokine involved in enhancing production ofinterferon-gamma and interleukin-12 and reducing production ofinterleukin-10 and is essential in the pathway that leads to typeI immunity. 
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Subcellular Location
Secreted. 
Tissue Specificity
 
Gene Ontology
GO IDGO termEvidence
GO:0045177 C:apical part of cell IDA:MGI.
GO:0042995 C:cell projection IEA:Compara.
GO:0005737 C:cytoplasm IDA:MGI.
GO:0005576 C:extracellular region NAS:UniProtKB.
GO:0005615 C:extracellular space IEA:UniProtKB-KW.
GO:0031988 C:membrane-bounded vesicle IEA:Compara.
GO:0048471 C:perinuclear region of cytoplasm IEA:Compara.
GO:0050840 F:extracellular matrix binding IDA:MGI.
GO:0006916 P:anti-apoptosis NAS:UniProtKB.
GO:0031214 P:biomineral tissue development IEA:UniProtKB-KW.
GO:0007155 P:cell adhesion IEA:UniProtKB-KW.
GO:0006954 P:inflammatory response IEA:Compara.
GO:0048685 P:negative regulation of collateral sprouting of intact axon in response to injury IEA:Compara.
GO:0030593 P:neutrophil chemotaxis IDA:MGI.
GO:0001649 P:osteoblast differentiation IEA:Compara.
GO:0045780 P:positive regulation of bone resorption IEA:Compara.
GO:0010811 P:positive regulation of cell-substrate adhesion IDA:MGI.
GO:0048545 P:response to steroid hormone stimulus IEA:Compara.
GO:0033280 P:response to vitamin D IEA:Compara.
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Interpro
IPR002038;    Osteopontin.
IPR019841;    Osteopontin_CS.
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Pfam
PF00865;    Osteopontin;    1.
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SMART
SM00017;    OSTEO;    1.
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PROSITE
PS00884;    OSTEOPONTIN;    1.
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PRINTS
PR00216;    OSTEOPONTIN.;   
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Created Date
18-Oct-2012 
Record Type
GAS predicted 
Sequence Annotation
SIGNAL        1     16       Potential.
CHAIN        17    294       Osteopontin.
                             /FTId=PRO_0000020322.
MOTIF       144    146       Cell attachment site.
MOD_RES      24     24       Phosphoserine (By similarity).
MOD_RES      26     26       Phosphoserine.
MOD_RES      27     27       Phosphoserine.
MOD_RES      61     61       Phosphoserine.
MOD_RES      62     62       Phosphoserine.
MOD_RES      75     75       Phosphoserine (By similarity).
MOD_RES      80     80       Phosphoserine (By similarity).
MOD_RES     106    106       Phosphoserine (By similarity).
MOD_RES     109    109       Phosphoserine (By similarity).
MOD_RES     112    112       Phosphoserine (By similarity).
MOD_RES     115    115       Phosphoserine (By similarity).
MOD_RES     118    118       Phosphoserine (By similarity).
MOD_RES     170    170       Phosphothreonine (By similarity).
MOD_RES     176    176       Phosphoserine (By similarity).
MOD_RES     180    180       Phosphoserine (By similarity).
MOD_RES     200    200       Phosphoserine (By similarity).
MOD_RES     209    209       Phosphoserine (By similarity).
MOD_RES     213    213       Phosphoserine (By similarity).
MOD_RES     219    219       Phosphoserine (By similarity).
MOD_RES     231    231       Phosphoserine.
MOD_RES     234    234       Phosphoserine.
MOD_RES     243    243       Phosphoserine (By similarity).
MOD_RES     247    247       Phosphoserine (By similarity).
MOD_RES     255    255       Phosphoserine (By similarity).
MOD_RES     260    260       Phosphoserine (By similarity).
MOD_RES     283    283       Phosphoserine.
MOD_RES     288    288       Phosphoserine.
MOD_RES     290    290       Phosphoserine.
CARBOHYD     78     78       N-linked (GlcNAc...) (Potential).
CARBOHYD    123    123       O-linked (GalNAc...) (By similarity).
CARBOHYD    132    132       O-linked (GalNAc...) (By similarity).
CARBOHYD    137    137       O-linked (GalNAc...) (By similarity).
CONFLICT     43     43       L -> P (in Ref. 2; CAA34276).
CONFLICT     99     99       E -> G (in Ref. 1; AAA57265).
CONFLICT    100    100       S -> N (in Ref. 5; AAH14284).
CONFLICT    122    122       V -> F (in Ref. 3; CAA32165 and 5;
                             AAH14284).
CONFLICT    142    142       N -> D (in Ref. 5; AAH14284).
CONFLICT    171    171       D -> Y (in Ref. 5; AAH14284).
CONFLICT    188    188       D -> N (in Ref. 5; AAH14284).
CONFLICT    207    207       K -> R (in Ref. 5; AAH14284).
CONFLICT    224    224       R -> S (in Ref. 5; AAH14284).
CONFLICT    232    232       Q -> H (in Ref. 5; AAH14284).
CONFLICT    277    277       Y -> H (in Ref. 5; AAH14284).
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Nucleotide Sequence
Length: 1385 bp   Go to nucleotide: FASTA
Protein Sequence
Length: 294 bp   Go to amino acid: FASTA
The verified Protein-Protein interaction information
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