Detail Information for IndEnz0002010420
IED ID IndEnz0002010420
Enzyme Type ID protease010420
Protein Name Ribonuclease-like 3
RNase ZF-3
RNase-like 3
ZF-RNase-3
EC 3.1.27.-
Dr-RNase 1

Cleaved into: N-terminal peptide; LF-ZF3
Gene Name rnasel3
Organism Danio rerio (Zebrafish) (Brachydanio rerio)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Actinopterygii Actinopteri Neopterygii Teleostei Osteoglossocephalai Clupeocephala Otomorpha Ostariophysi Otophysi Cypriniphysae Cypriniformes (carps and others) Cyprinoidei Danionidae Danioninae Danio Danio rerio (Zebrafish) (Brachydanio rerio)
Enzyme Sequence MGIHQCTAVVLLLLCASLSTYGQPAEIRRRYEHFLTQHVYGGITEQTCDRVMRQRRITRFPTGNDCKEVNTFIQANGNHVRTVCTGGGTRQTDNRDLYMSNNQFTVITCTLRSGERHPNCRYRGKESSRKIVVACEGEWPTHYEKGVIV
Enzyme Length 149
Uniprot Accession Number A5HAK0
Absorption
Active Site ACT_SITE 38; /note=Proton acceptor; /evidence=ECO:0000269|PubMed:18508078; ACT_SITE 142; /note=Proton donor; /evidence=ECO:0000269|PubMed:18508078
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.1.27.-
Enzyme Function FUNCTION: Ribonuclease. Angiogenic. Plays a role in host defense. Exhibits strong antibacterial activity against Gram-negative bacteria but mild antibacterial activity against Gram-positive bacteria. The RNase activity is not required for the bactericidal activity. {ECO:0000269|PubMed:16861230, ECO:0000269|PubMed:17347156, ECO:0000269|PubMed:18508078, ECO:0000269|PubMed:20214681}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Beta strand (8); Chain (1); Disulfide bond (3); Helix (4); Modified residue (1); Natural variant (7); Peptide (2); Region (1); Sequence conflict (1); Signal peptide (1); Site (1)
Keywords 3D-structure;Angiogenesis;Antibiotic;Antimicrobial;Developmental protein;Differentiation;Direct protein sequencing;Disulfide bond;Endonuclease;Hydrolase;Immunity;Nuclease;Pyrrolidone carboxylic acid;Reference proteome;Secreted;Signal
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P34096}.
Modified Residue MOD_RES 23; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000250|UniProtKB:P34096
Post Translational Modification PTM: Cleavage between Arg-55 and Arg-56 is catalyzed by a membrane-localized Gram-negative bacterium protease (OmpT in E.coli). The excised fragment is then transported to the bacterium cytosol for cleavage of the disulfide bridge linking Cys-48 and Cys-109, thus separating the N-terminal and LF-ZF3. LF-ZF3 but not the N-terminal peptide possesses bactericidal activity. {ECO:0000269|PubMed:20214681}.
Signal Peptide SIGNAL 1..22; /evidence=ECO:0000269|PubMed:18508078
Structure 3D X-ray crystallography (1)
Cross Reference PDB 2VQ9;
Mapped Pubmed ID 18852033; 21050179;
Motif
Gene Encoded By
Mass 17,011
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda 4.6.1.18;