IED ID | IndEnz0002019204 |
Enzyme Type ID | protease019204 |
Protein Name |
Complement C1r subcomponent-like protein C1r-LP C1r-like protein EC 3.4.21.- |
Gene Name | C1rl |
Organism | Rattus norvegicus (Rat) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Rattus Rattus norvegicus (Rat) |
Enzyme Sequence | MCWLLLWGILHTCPTQASVLLAQQFPQQLTSPGYPEPYIKGQESHADIEAPEGFAVRLIFQDFDLEPSPGCEGDSVTISTRGTDATRLCGQQGSSLGSPPNQMEFVSSGRSLRLTFRAHSSKNKVTHLHKGFLALYQAAVSQPNGDAEAFTTPGANPPEIQNHCPGPYYKEEQTGTLSCPSSRKWKDRQRGEEVPECVPVCGRPVVPIAENPNTFGSSRAKPGNFPWQAFTSIYGRGGGALLGDRWILTAAHTIFPKDSIYLRKNKTVNVFLGHTDVDELLKLGNHPVRRVVVHPDYRQEESHNFDGDIALLELEHRVPLGPSLLPVCLPDNETLYHSGLWGYISGFGVEMGWLTTKLKYSKLPVAPREACEAWLRQRQRTEVFSDNMFCVGEEMQVNSVCQGDSGSVYVVWDDRALRWVATGIVSWGVGCGKGYGFYTKVLSYVDWIKGVIECKDRCPEA |
Enzyme Length | 461 |
Uniprot Accession Number | Q6IE64 |
Absorption | |
Active Site | ACT_SITE 252; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 308; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 405; /note=Charge relay system; /evidence=ECO:0000250 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.4.21.- |
Enzyme Function | FUNCTION: Mediates the proteolytic cleavage of HP/haptoglobin in the endoplasmic reticulum. {ECO:0000250}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (3); Chain (1); Disulfide bond (4); Domain (3); Glycosylation (2); Signal peptide (1) |
Keywords | Complement pathway;Disulfide bond;Glycoprotein;Hydrolase;Immunity;Innate immunity;Protease;Reference proteome;Secreted;Serine protease;Signal;Sushi |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..22; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 51,107 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |