| IED ID | IndEnz0002015874 |
| Enzyme Type ID | protease015874 |
| Protein Name |
Complement component receptor 1-like protein Antigen 5I2 Complement regulatory protein Crry |
| Gene Name | Cr1l Crry |
| 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 | MEASSPLDPVGRLVAFCRGGVHLAVLLLFLSPSTLGQCPAPPLFPYAKPINPTDESTFPVGTSLKYECRPGYIKRQFSITCEVNSVWTSPQDVCIRKQCETPLDPQNGIVHVNTDIRFGSSITYTCNEGYRLIGSSSAMCIISDQSVAWDAEAPICESIPCEIPPSIPNGDFFSPNREDFHYGMVVTYQCNTDARGKKLFNLVGEPSIHCTSIDGQVGVWSGPPPQCIELNKCTPPHVENAVIVSKNKSLFSLRDMVEFRCQDGFMMKGDSSVYCRSLNRWEPQLPSCFKVKSCGAFLGELPNGHVFVPQNLQLGAKVTFVCNTGYQLKGNSSSHCVLDGVESIWNSSVPVCEQVICKLPQDMSGFQKGLQMKKDYYYGDNVALECEDGYTLEGSSQSQCQSDASWDPPLPKCVSQVICKLPQDMSGFQKGLQMKKDYYYGDNVALECEDGYTLEGSSQSQCQSDASWDPPLPKCVSRSNSGLIAGIFIGIIVLILFIIFSYWMIMKFKKRNSTNEKCKEVGIYLNSKEDSCVQPQSLLTSQENNSTSSPARNSLTQEV |
| Enzyme Length | 559 |
| Uniprot Accession Number | Q63135 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Acts as a cofactor for complement factor I, a serine protease which protects autologous cells against complement-mediated injury by cleaving C3b and C4b deposited on host tissue. Also acts as a decay-accelerating factor, preventing the formation of C4b2a and C3bBb, the amplification convertases of the complement cascade. Seems to act as a costimulatory factor for T-cells. May play a crucial role in early embryonic development by maintaining fetomaternal tolerance. {ECO:0000269|PubMed:15474557, ECO:0000269|PubMed:7534798, ECO:0000269|PubMed:8144902}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (1); Beta strand (20); Chain (1); Disulfide bond (14); Domain (7); Glycosylation (2); Modified residue (5); Region (1); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (1) |
| Keywords | 3D-structure;Alternative splicing;Complement pathway;Developmental protein;Direct protein sequencing;Disulfide bond;Glycoprotein;Immunity;Innate immunity;Membrane;Phosphoprotein;Pregnancy;Receptor;Reference proteome;Repeat;Signal;Sushi;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. |
| Modified Residue | MOD_RES 527; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 531; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q64735; MOD_RES 537; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q64735; MOD_RES 540; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:Q64735; MOD_RES 554; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903 |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..35; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 2XRB; 2XRD; |
| Mapped Pubmed ID | 11861390; |
| Motif | |
| Gene Encoded By | |
| Mass | 61,680 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |