SpermatogenesisOnline 1.0

Tag Content
SG ID
SG00019597 
UniProt Accession
Theoretical PI
5.82  
Molecular Weight
28057 Da  
Genbank Nucleotide ID
Genbank Protein ID
Gene Name
Cfd 
Gene Synonyms/Alias
Adn, Df 
Protein Name
Complement factor D 
Protein Synonyms/Alias
EC=3.4.21.46 28 kDa adipocyte protein; Adipsin; C3 convertase activator; Properdin factor D;Flags: Precursor 
Organism
Mus musculus (Mouse) 
NCBI Taxonomy ID
10090 
Chromosome Location
chr:10;79353598-79355401;1
View in Ensembl genome browser  
Function in Stage
Uncertain 
Function in Cell Type
Uncertain 
Probability (GAS) of Function in Spermatogenesis
0.173353354 
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. When 3T3 cells undergo adipose differentiation, they are reprogrammed by changes in gene expression of sufficient magnitude to greatly alter the protein composition of the cells. Three participating genes encode glycerophosphate dehydrogenase, a lipid-binding protein, and a serine protease. These three genes have now been cloned and sequenced. Their exon/intron structures are described, together with some interesting peculiarities and some regions of common sequence. It remains to be demonstrated whether the information for common participation of the genes in the program of differentiation resides in controlling elements within the regions sequenced. PMID: [3015943] 

2. We have isolated, mapped and sequenced adipsin, the adipocyte differentiation-dependent serine protease gene. This gene, which is present in a single form in the mouse, spans 1.7 kilobases and contains five exons. While the basic exon structure characteristic of serine protease genes is conserved in adipsin, there is also a fusion of two exons that are separate in other serine proteases. The sequence data also suggests a mechanism of alternative splicing which appears to account for the generation of two adipsin mRNA species differing by only three nucleotides and encoding two different signal peptides. To investigate the control of adipsin expression we have examined the effects of tumor necrosis factor (TNF) on adipocytes. The level of adipsin RNA is dramatically decreased by hormone treatment, but the change occurs more slowly than for other fat cell mRNAs, such as glycerophosphate dehydrogenase. These results show that adipsin is a novel serine protease gene whose expression is regulated by a macrophage-derived factor which modulates expression of other adipocyte-specific RNAs. PMID: [3024123] 

3. We previously have isolated cDNA clones for several mRNAs that increase in abundance during the differentiation of 3T3 adipocytes but whose physiological role is unknown. We show here that a mRNA that is complementary to one of these clones and encodes a protein of 28 kDa is expressed abundantly in mouse fat pads but not in several other mouse tissues. Sequence analysis of the corresponding cDNA clone indicated that the encoded protein shows 30% overall amino acid homology to several serine proteases including trypsin, chymotrypsin, and elastase. Homology is much higher (64%) between the 28-kDa protein and regions that are strongly conserved among the members of the serine protease family. The derived protein also has key features characteristic of active serine proteases, including the histidine, aspartic acid, and serine residues, which comprise the charge relay system, and a potential cleavage site for activation of the zymogen. Primer extension analysis performed to obtain the sequence of the 5' end of mRNA that encodes the 28-kDa protein indicates that two forms of this mRNA exist and probably arise through alternative splicing. The two mRNAs encode signal sequences that differ by the deletion of one amino acid near the predicted cleavage site of the signal peptide. These results demonstrate that adipocyte differentiation is accompanied by the expression of mRNA encoding a serine protease homologue that can be synthesized with two different signal peptides. PMID: [3901003] 

4. A procedure to map N-glycosylation sites is presented here. It can be applied to purified proteins as well as to highly complex mixtures. The method exploits deglycosylation by PNGase F in a diagonal, reverse-phase chromatographic setup. When applied to 10 microL of mouse serum, affinity-depleted for its three most abundant components, 117 known or predicted sites were mapped in addition to 10 novel sites. Several sites were detected on soluble membrane or receptor components. Our method furthermore senses the nature of glycan structures and can detect differential glycosylation on a given site. These properties--high sensitivity and dependence on glycan imprinting--can be exploited for glycan-biomarker analysis. PMID: [16944957] 

5. A comprehensive understanding of the mouse plasma proteome is important for studies using mouse models to identify protein markers of human disease. To enhance our analysis of the mouse plasma proteome, we have developed a method for isolating low-abundance proteins using a cysteine-containing glycopeptide strategy. This method involves two orthogonal affinity capture steps. First, glycoproteins are coupled to an azlactone copolymer gel using hydrazide chemistry and cysteine residues are then biotinylated. After trypsinization and extensive washing, tethered N-glycosylated tryptic peptides are released from the gel using PNGase F. Biotinylated cysteinyl-containing glycopeptides are then affinity selected using a monomeric avidin gel and analyzed by LC-MS/MS. We have applied the method to a proteome analysis of mouse plasma. In two independent analyses using 200 muL each of C57BL mouse plasma, 51 proteins were detected. Only 42 proteins were seen when the same plasma sample was analyzed by glycopeptides only. A total of 104 N-glycosylation sites were identified. Of these, 17 sites have hitherto not been annotated in the Swiss-Prot database whereas 48 were considered probable, potential, or by similarity - i.e., based on little or no experimental evidence. We show that analysis by cysteine-containing glycopeptides allows detection of low-abundance proteins such as the epidermal growth factor receptor, the Vitamin K-dependent protein Z, the hepatocyte growth factor activator, and the lymphatic endothelium-specific hyaluronan receptor as these proteins were not detected in the glycopeptide control analysis. PMID: [17330941] 

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Function
Factor D cleaves factor B when the latter is complexedwith factor C3b, activating the C3bbb complex, which then becomesthe C3 convertase of the alternate pathway. Its function ishomologous to that of C1s in the classical pathway. 
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Subcellular Location
Secreted. 
Tissue Specificity
 
Gene Ontology
GO IDGO termEvidence
GO:0005615 C:extracellular space IDA:MGI.
GO:0004252 F:serine-type endopeptidase activity IEA:InterPro.
GO:0006957 P:complement activation, alternative pathway IEA:UniProtKB-KW.
GO:0007219 P:Notch signaling pathway IEA:Compara.
GO:0006508 P:proteolysis IEA:UniProtKB-KW.
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Interpro
IPR009003;    Pept_cys/ser_Trypsin-like.
IPR018114;    Peptidase_S1/S6_AS.
IPR001254;    Peptidase_S1_S6.
IPR001314;    Peptidase_S1A.
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Pfam
PF00089;    Trypsin;    1.
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SMART
SM00020;    Tryp_SPc;    1.
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PROSITE
PS50240;    TRYPSIN_DOM;    1.
PS00134;    TRYPSIN_HIS;    1.
PS00135;    TRYPSIN_SER;    1.
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PRINTS
PR00722;    CHYMOTRYPSIN.;   
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Created Date
18-Oct-2012 
Record Type
GAS predicted 
Sequence Annotation
SIGNAL        1     20       Potential.
PROPEP       21     25       Activation peptide (Potential).
                             /FTId=PRO_0000027562.
CHAIN        26    259       Complement factor D.
                             /FTId=PRO_0000027563.
DOMAIN       26    254       Peptidase S1.
ACT_SITE     66     66       Charge relay system.
ACT_SITE    115    115       Charge relay system.
ACT_SITE    209    209       Charge relay system.
CARBOHYD     46     46       N-linked (GlcNAc...) (Potential).
CARBOHYD    124    124       N-linked (GlcNAc...).
CARBOHYD    176    176       N-linked (GlcNAc...).
CARBOHYD    251    251       N-linked (GlcNAc...) (Potential).
CARBOHYD    256    256       N-linked (GlcNAc...) (Potential).
DISULFID     51     67       By similarity.
DISULFID    149    215       By similarity.
DISULFID    180    196       By similarity.
DISULFID    205    230       By similarity.
VAR_SEQ      20     20       Missing (in isoform 2).
                             /FTId=VSP_005382.
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Nucleotide Sequence
Length: 862 bp   Go to nucleotide: FASTA
Protein Sequence
Length: 259 bp   Go to amino acid: FASTA
The verified Protein-Protein interaction information
UniProt
 Gene Symbol Ref Databases
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String database  
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