About: Coagulin

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Coagulin is a gel-forming protein of hemolymph that hinders the spread of invaders by immobilising them. It is produced in the coagulogen form before being cleaved into the active form. In human medicine, coagulation of coagulin is the basis of detection of bacterial endotoxin in the LAL test for parenteral medications.

Attributes	Values
rdf:type	Thing Biomolecule Biomolecule Protein yago:Abstraction100002137 yago:Attribute100024264 yago:Environment113934596 protein yago:Situation113927383 yago:Sphere114514039 yago:State100024720 yago:WikicatProteinDomains
rdfs:label	Coagulin (en)
rdfs:comment	Coagulin is a gel-forming protein of hemolymph that hinders the spread of invaders by immobilising them. It is produced in the coagulogen form before being cleaved into the active form. In human medicine, coagulation of coagulin is the basis of detection of bacterial endotoxin in the LAL test for parenteral medications. (en)
name	Coagulin (en)
dcterms:subject	Protein domains
Wikipage page ID	29049590 (xsd:integer)
Wikipage revision ID	991508261 (xsd:integer)
Link from a Wikipage to another Wikipage	Blood coagulation Horseshoe crabs Beta-glucan Limulus amebocyte lysate Limulus clotting enzyme Crustaceans Transglutaminase Lipopolysaccharide Cystine knot Protein Protein domains Hemolymph Disulfide bonds Fibrin Fibrinogen Neurotrophin
sameAs	Coagulin Coagulin Coagulin Coagulin
dbp:wikiPageUsesTemplate	dbt:InterPro_content dbt:Not_a_typo dbt:Protein-stub dbt:Reflist dbt:PDB dbt:Pfam_box
SCOP	d1aoca_ (en)
InterPro	IPR000275 (en)
Pfam	PF02035 (en)
symbol	Coagulin (en)
has abstract	Coagulin is a gel-forming protein of hemolymph that hinders the spread of invaders by immobilising them. It is produced in the coagulogen form before being cleaved into the active form. In human medicine, coagulation of coagulin is the basis of detection of bacterial endotoxin in the LAL test for parenteral medications. The protein contains a single 175-residue polypeptide chain that is cleaved after Arg-18 and Arg-46 by a Limulus clotting enzyme contained in the hemocyte and activated by a bacterial endotoxin (lipopolysaccharide). Cleavage releases two chains of coagulin, A and B, linked by two disulfide bonds, together with the peptide C. Gel formation results from interlinking of coagulin molecules. The full-length structure of a coagulogen is known (PDB: 1AOC); it shares the same cystine-knot cytokine superfamily (fold) as neurotrophins, with several cystines conserved. The A-B fold wraps around the helical peptide C, forming a compact structure. In crustaceans, hemolymph coagulation depends on the transglutaminase-mediated cross-linking of specific plasma-clotting proteins, but without the proteolytic cascade. In horseshoe crabs, the proteolytic coagulation cascade triggered by lipopolysaccharides and beta-1,3-glucans leads to the conversion of coagulogen into coagulin, resulting in noncovalent coagulin homopolymers through head-to-tail interaction. However, horseshoe crab transglutaminase does not cross-link coagulins intermolecularly. Recently, coagulins were discovered to be cross-linked on hemocyte cell surface proteins called proxins. This indicates that a cross-linking reaction at the final stage of hemolymph coagulation is an important innate immune system of horseshoe crabs. In comparison, mammalian blood coagulation is based on the proteolytically induced polymerization of fibrinogens. Initially, fibrin monomers noncovalently interact with each other. The resulting homopolymers are further stabilized when the plasma transglutaminase cross-links epsilon-(gamma-glutamyl)lysine bonds between molecules. (en)
gold:hypernym	Protein
prov:wasDerivedFrom	wikipedia-en:Coagulin?oldid=991508261&ns=0
page length (characters) of wiki page	3970 (xsd:nonNegativeInteger)
Symbol	Coagulin
foaf:isPrimaryTopicOf	wikipedia-en:Coagulin
is Link from a Wikipage to another Wikipage of	Limulus clotting enzyme Limulus clotting factor C Coagulogen
is Wikipage redirect of	Coagulogen
is foaf:primaryTopic of	wikipedia-en:Coagulin

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