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Literature summary extracted from

  • Anastasiou, V.; Mikrou, A.; Papanastasiou, A.; Zarkadis, I.
    The molecular identification of factor H and factor I molecules in rainbow trout provides insights into complement C3 regulation (2011), Fish Shellfish Immunol., 31, 491-499.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.21.45
-
 Oncorhynchus mykiss

Organism

EC Number Organism UniProt Comment Textmining
3.4.21.45 Oncorhynchus mykiss E7BAR3
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.4.21.45 glycoprotein sequence contains three potential N-glycosylation sites Oncorhynchus mykiss
3.4.21.45 proteolytic modification CFI mRNA is translated in both a heavy and light chain which is further cleaved at a tetrapeptide processing site Oncorhynchus mykiss

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.21.45 brain low level of mRNA expression Oncorhynchus mykiss
-
3.4.21.45 intestine high level of mRNA expression Oncorhynchus mykiss
-
3.4.21.45 liver high level of mRNA expression Oncorhynchus mykiss
-
3.4.21.45 additional information no expression detected in heart, kidney and spleen Oncorhynchus mykiss
-

Subunits

EC Number Subunits Comment Organism
3.4.21.45 additional information CFI mRNA is translated in both a heavy and light chain which is further cleaved at a tetrapeptide processing site. The light chain of trout CFI comprises the serine protease domain, which contains the catalytic triad, His380-Asp429-Ser525 residues, human CFI numbering, as well as the Asp519 residue located at the bottom of the specificity pocket. All these residues are identical by composition and position in all species tested Oncorhynchus mykiss

Synonyms

EC Number Synonyms Comment Organism
3.4.21.45 CFI
-
 Oncorhynchus mykiss