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Search results 101 to 133 out of 133 for Hrg

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Type Details Score
Protein
F6YCM8
Organism: Mus musculus/domesticus
Length: 477  
Fragment?: true
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Protein
F6UV57
Organism: Mus musculus/domesticus
Length: 433  
Fragment?: true
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Protein
F8WIH0
Organism: Mus musculus/domesticus
Length: 690  
Fragment?: true
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Publication
11358523 | -
First Author: Valente RH
Year: 2001
Journal: Eur J Biochem
Title: BJ46a, a snake venom metalloproteinase inhibitor. Isolation, characterization, cloning and insights into its mechanism of action.
Volume: 268
Issue: 10
Pages: 3042-52
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Publication
1478916 | -
First Author: Yamakawa Y
Year: 1992
Journal: J Biochem
Title: Primary structure of the antihemorrhagic factor in serum of the Japanese Habu: a snake venom metalloproteinase inhibitor with a double-headed cystatin domain.
Volume: 112
Issue: 5
Pages: 583-9
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Publication
14644044 | -
First Author: Ray S
Year: 2003
Journal: Biochim Biophys Acta
Title: Members of the cystatin superfamily interact with MMP-9 and protect it from autolytic degradation without affecting its gelatinolytic activities.
Volume: 1652
Issue: 2
Pages: 91-102
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Protein Domain
IPR001363 | Prot_inh_fetuin_CS
Type: Conserved_site
Description: The cystatins are a superfamily of similar proteins present in mammals, birds, fish, insects, plants and protozoa. In general they are potent peptidase inhibitors [, , , ]belonging to MEROPS inhibitor family I25, clan IH. The type 1 cystatins or stefins (A and B) are mainly intracellular, the type 2 cystatins (C, D, E/M, F, G, S, SN and SA) are extracellular, and the type 3 cystatins (L- and H-kininogens) are intravascular proteins. All true cystatins inhibit cysteine peptidases of the papain family(MEROPS peptidase family C1), and some also inhibit legumain family enzymes (MEROPS peptidase family C13). These peptidases play key roles in physiological processes, such as intracellular protein degradation (cathepsins B, H and L), are pivotal in the remodelling of bone (cathepsin K), and may be important in the control of antigen presentation (cathepsin S, mammalian legumain). Moreover, the activities of such peptidases are increased in pathophysiological conditions, such as cancer metastasis and inflammation. Additionally, such peptidases are essential for several pathogenic parasites and bacteria. Thus in animals cystatins not only have capacity to regulate normal body processes and perhaps cause disease when down-regulated, but in other organisms may also participate in defence against biotic and abiotic stress.This family of proteinase inhibitors are cystatins belonging to MEROPS inhibitor family I25 (clan IH), subfamily I25C. They are primarily metalloprotease inhibitors, which include snake venom anti-hemorrhagic factors and the mammalian fetuins, for example:Anti-hemorrhagic factor BJ46a, which is a potent inhibitor of atrolysin and jararhagin (MEROPS peptidase family M12) from the venomous snake Bothrops jararaca [].Anti-hemorrhagic factor, HSF, from the Japanese Habu snake (Trimeresurus flavoviridis). HSF contains two N-terminal cystatin domains which show a remarkable sequence homology (about 50%) to those of plasma glycoproteins such as alpha 2-HS (human) and fetuin (bovine) and to a lesser extent to that of HRG (human). In spite of the presence of cystatin domains, HSF does not inhibit cysteine proteinases such as papain and cathepsin B but does inhibit several metalloproteases in Habu venom [].Mammalian fetuins have been demonstrated to bind to matrix metalloproteinase (MMPs, MEROPS peptidase family M10). This binding protects the MMPs from autolytic degradation without interfering with their enzymatic activity [].Fetuins are known to consist of three domains: two tandemly arranged N-terminal cystatin domains (D1 and D2) and an unrelated domain (D3) located in the C-terminal region [, ]. When compared with the other members of this family, D3, especially its N-terminal half, varies greatly due to deletions, insertions or substitutions. Sequence comparisons suggest that the conformation of the human alpha2HS glycoprotein differs greatly from that of other members of this family. Human fetuin is a heterodimer of chains A and B, which are derived by cleavage of a connecting peptide from a common precursor. It is synthesised in the liver and selectively concentrated in bone matrix. It has a wide functional diversity having been shown to be involved in immune response, bone formation and resorption. Mammalian fetuin also called alpha-2-HS-glycoprotein, bone sialic acid-containing protein (BSP), countertrypin or PP63, is expressed in a tissue- and development-specific pattern, which seems to be significantly different between species [, ].
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Protein
Q9QXC1
Organism: Mus musculus/domesticus
Length: 388  
Fragment?: false
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Publication
1373325 | J:31552
First Author: Yang F
Year: 1992
Journal: Biochim Biophys Acta
Title: Human alpha 2-HS-glycoprotein/bovine fetuin homologue in mice: identification and developmental regulation of the gene.
Volume: 1130
Issue: 2
Pages: 149-56
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Protein
P29699
Organism: Mus musculus/domesticus
Length: 345  
Fragment?: false
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Protein
Q3URD3
Organism: Mus musculus/domesticus
Length: 845  
Fragment?: false
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Protein
Q3UEK9
Organism: Mus musculus/domesticus
Length: 345  
Fragment?: false
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Protein
H7BX64
Organism: Mus musculus/domesticus
Length: 828  
Fragment?: false
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Protein
Q3TIU3
Organism: Mus musculus/domesticus
Length: 345  
Fragment?: false
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Protein
Q8CB17
Organism: Mus musculus/domesticus
Length: 388  
Fragment?: false
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Protein
A0A338P7H5
Organism: Mus musculus/domesticus
Length: 301  
Fragment?: false
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Protein
Q3UEK5
Organism: Mus musculus/domesticus
Length: 345  
Fragment?: false
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Protein
A0A338P7G1
Organism: Mus musculus/domesticus
Length: 294  
Fragment?: false
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Protein
O35399
Organism: Mus musculus/domesticus
Length: 191  
Fragment?: true
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Protein
D3Z7V3
Organism: Mus musculus/domesticus
Length: 790  
Fragment?: false
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Protein
A0A338P6Y6
Organism: Mus musculus/domesticus
Length: 123  
Fragment?: false
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Protein
Q6YJU2
Organism: Mus musculus/domesticus
Length: 403  
Fragment?: false
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Protein
A0A338P703
Organism: Mus musculus/domesticus
Length: 266  
Fragment?: false
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Protein
A0A338P7B8
Organism: Mus musculus/domesticus
Length: 232  
Fragment?: true
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Protein
Q6YJU1
Organism: Mus musculus/domesticus
Length: 308  
Fragment?: false
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Publication
1707273 | -
 
First Author: Haasemann M
Year: 1991
Journal: Biochem J
Title: Rat tyrosine kinase inhibitor shows sequence similarity to human alpha 2-HS glycoprotein and bovine fetuin.
Volume: 274 ( Pt 3)
Pages: 899-902
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Publication
1372866 | -
First Author: Brown WM
Year: 1992
Journal: Eur J Biochem
Title: The nucleotide and deduced amino acid structures of sheep and pig fetuin. Common structural features of the mammalian fetuin family.
Volume: 205
Issue: 1
Pages: 321-31
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Publication
9133634 | J:39421
First Author: Goto K
Year: 1997
Journal: J Biochem
Title: Molecular cloning and sequencing of cDNA encoding plasma countertrypin, a member of mammalian fetuin family, from the Mongolian gerbil, Meriones unguiculatus.
Volume: 121
Issue: 3
Pages: 619-25
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Publication
3555466 | -
First Author: Barrett AJ
Year: 1986
Journal: Biomed Biochim Acta
Title: The cystatins: a diverse superfamily of cysteine peptidase inhibitors.
Volume: 45
Issue: 11-12
Pages: 1363-74
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Publication
1855589 | -
First Author: Turk V
Year: 1991
Journal: FEBS Lett
Title: The cystatins: protein inhibitors of cysteine proteinases.
Volume: 285
Issue: 2
Pages: 213-9
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Publication
2107324 | -
First Author: Rawlings ND
Year: 1990
Journal: J Mol Evol
Title: Evolution of proteins of the cystatin superfamily.
Volume: 30
Issue: 1
Pages: 60-71
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Publication
14587292 | -
 
First Author: Abrahamson M
Year: 2003
Journal: Biochem Soc Symp
Title: Cystatins.
Issue: 70
Pages: 179-99
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Publication
22731697 | -
 
First Author: Zhang D
Year: 2012
Journal: Biol Direct
Title: Polymorphic toxin systems: Comprehensive characterization of trafficking modes, processing, mechanisms of action, immunity and ecology using comparative genomics.
Volume: 7
Pages: 18
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