SpermatogenesisOnline 1.0

Tag Content
SG ID
SG00006262 
UniProt Accession
Theoretical PI
6.34  
Molecular Weight
73102 Da  
Genbank Nucleotide ID
Genbank Protein ID
Gene Name
Kng1 
Gene Synonyms/Alias
Kng 
Protein Name
Kininogen-1 Kininogen-1 heavy chain Bradykinin Kininogen-1 light chain 
Protein Synonyms/Alias
Contains:Contains:Contains:Flags: Precursor 
Organism
Mus musculus (Mouse) 
NCBI Taxonomy ID
10090 
Chromosome Location
chr:16;23057938-23082141;1
View in Ensembl genome browser  
Function in Stage
Uncertain 
Function in Cell Type
Uncertain 
Probability (GAS) of Function in Spermatogenesis
0.181184097 
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. We isolated cDNAs encoding low-molecular-weight (L-) and high-molecular-weight (H-) prekininogens from a mouse liver cDNA library using rat T-kininogen cDNA and rat H-kininogen cDNA respectively, as probes. The signal peptide, the heavy chain, and the bradykinin moiety, which are common between the two prekininogens, consist of 20, 359, and 9 amino acids, respectively, while the light chains of the L- and H-prekininogens are composed of 44 and 273 amino acids, respectively. All 19 cysteine residues present in both mouse prekininogens are located at the same positions relative to those of human origin. The light chain of H-prekininogen contains a characteristic 15-repeated His-Gly sequence and a conserved sequence for binding prekallikrein or factor XI. Northern blotting or reverse transcription-polymerase chain reaction followed by Southern blotting using mouse L- and H-kininogen cDNAs demonstrated that both L- and H-kininogens are predominantly expressed in the liver and kidney. L-Kininogen mRNA was also expressed in other tissues, such as the adrenal gland, brain, spinal cord, testis, lung, heart, and skin, while levels of H-kininogen mRNA in these tissues were too low to detect, suggesting that L-kininogen is synthesized in various tissues of mouse, while H-kininogen is exclusively synthesized in the liver and kidney. A genomic Southern blot using H-prekininogen cDNA revealed that the L- and H-prekininogen mRNAs in mouse are probably encoded by a single gene, as is the case in both human and bovine. PMID: [9199253] 

2. Kininogens serve dual functions by forming a scaffold for the assembly of the protein complex initiating the surface-activated blood coagulation cascade and as precursors for the kinin hormones. While rats have three kininogen genes, for mice, cattle, and humans only one gene has been described. Here, we present sequence and expression data of a second mouse kininogen gene. The two genes, kininogen-I and kininogen-II, are located in close proximity on chromosome 16 in a head-to-head arrangement. In liver and kidney, both genes are expressed and for each gene three alternative splice variants are synthesized. Two of them are the expected high and low molecular weight isoforms known from all mammalian kininogens. However, for both genes also a third, hitherto unknown splice variant was detected which lacks part of the high molecular weight mRNA due to splicing from the low molecular weight donor site to alternative splice acceptor sites in exon 10. The physiological functions of the six kininogen isoforms predicted by these findings need to be determined. PMID: [15134344] 

3. 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] 

4. 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] 

5.

BACKGROUND:

CRISP-3 was previously shown to be bound to alpha(1)B-glycoprotein (A1BG) in human serum/plasma. All mammalian sera are supposed to contain A1BG, although its presence in rodent sera is not well-documented. Since animal sera are often used to supplement buffers in experiments, in particular such that involve cell cultures, binding proteins present in sera might interfere in the experiments. PMID: [20116414] 

6. 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] 

7. 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
(1) Kininogens are inhibitors of thiol proteases; (2)HMW-kininogen plays an important role in blood coagulation byhelping to position optimally prekallikrein and factor XI next tofactor XII; (3) HMW-kininogen inhibits the thrombin- and plasmin-induced aggregation of thrombocytes; (4) the active peptidebradykinin that is released from HMW-kininogen shows a variety ofphysiological effects: (4A) influence in smooth musclecontraction, (4B) induction of hypotension, (4C) natriuresis anddiuresis, (4D) decrease in blood glucose level, (4E) it is amediator of inflammation and causes (4E1) increase in vascularpermeability, (4E2) stimulation of nociceptors (4E3) release ofother mediators of inflammation (e.g. prostaglandins), (4F) it hasa cardioprotective effect (directly via bradykinin action,indirectly via endothelium-derived relaxing factor action); (5)LMW-kininogen inhibits the aggregation of thrombocytes; (6) LMW-kininogen is in contrast to HMW-kininogen not involved in bloodclotting (By similarity). 
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Subcellular Location
Secreted, extracellular space. 
Tissue Specificity
Plasma. 
Gene Ontology
GO IDGO termEvidence
GO:0005615 C:extracellular space IEA:UniProtKB-SubCell.
GO:0004869 F:cysteine-type endopeptidase inhibitor activity IEA:UniProtKB-KW.
GO:0007596 P:blood coagulation IEA:UniProtKB-KW.
GO:0006954 P:inflammatory response IEA:UniProtKB-KW.
GO:0042311 P:vasodilation IEA:UniProtKB-KW.
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Interpro
IPR002395;    Kininogen.
IPR000010;    Prot_inh_cystat.
IPR018073;    Prot_inh_cystat_CS.
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Pfam
PF00031;    Cystatin;    3.
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SMART
SM00043;    CY;    3.
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PROSITE
PS00287;    CYSTATIN;    1.
PS51647;    CYSTATIN_KININOGEN;    3.
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PRINTS
PR00334;    KININOGEN.;   
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Created Date
18-Oct-2012 
Record Type
GAS predicted 
Sequence Annotation
SIGNAL        1     20
CHAIN        21    661       Kininogen-1.
                             /FTId=PRO_0000006691.
CHAIN        21    379       Kininogen-1 heavy chain.
                             /FTId=PRO_0000006692.
PEPTIDE     380    388       Bradykinin.
                             /FTId=PRO_0000006693.
CHAIN       389    661       Kininogen-1 light chain.
                             /FTId=PRO_0000006694.
DOMAIN       28    131       Cystatin kininogen-type 1.
DOMAIN      150    253       Cystatin kininogen-type 2.
DOMAIN      272    375       Cystatin kininogen-type 3.
COMPBIAS    439    524       His-rich.
MOD_RES     325    325       Phosphothreonine (By similarity).
MOD_RES     328    328       Phosphoserine (By similarity).
MOD_RES     331    331       Phosphoserine (By similarity).
CARBOHYD     82     82       N-linked (GlcNAc...).
CARBOHYD    168    168       N-linked (GlcNAc...).
CARBOHYD    204    204       N-linked (GlcNAc...).
CARBOHYD    242    242       N-linked (GlcNAc...).
DISULFID     28    631       Interchain (between heavy and light
                             chains) (By similarity).
DISULFID     83     94       By similarity.
DISULFID    107    125       By similarity.
DISULFID    141    144       By similarity.
DISULFID    205    217       By similarity.
DISULFID    228    247       By similarity.
DISULFID    263    266       By similarity.
DISULFID    327    339       By similarity.
DISULFID    350    369       By similarity.
VAR_SEQ     401    581       Missing (in isoform 3).
                             /FTId=VSP_037159.
VAR_SEQ     401    432       VSPPYIAREQEERDAETEQGPTHGHGWLHEKQ -> RLLRA
                             CEYKGRLSKAGAEPAPERQAESSQVKQ (in isoform
                             LMW).
                             /FTId=VSP_001263.
VAR_SEQ     433    661       Missing (in isoform LMW).
                             /FTId=VSP_001264.
CONFLICT    642    642       E -> K (in Ref. 5; AAI08937).
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Nucleotide Sequence
Length: 1436 bp   Go to nucleotide: FASTA
Protein Sequence
Length: 661 bp   Go to amino acid: FASTA
The verified Protein-Protein interaction information
UniProt
 Gene Symbol Ref Databases
Kcnma1IntAct 
EnamIntAct 
Other Protein-Protein interaction resources
String database  
View Microarray data
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