Detail Information for IndEnz0002003279
IED ID IndEnz0002003279
Enzyme Type ID protease003279
Protein Name Complement component receptor 1-like protein
Complement regulatory protein Crry
Protein p65
Gene Name Cr1l Crry Cry
Organism Mus musculus (Mouse)
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 Mus Mus Mus musculus (Mouse)
Enzyme Sequence MEVSSRSSEPLDPVWLLVAFGRGGVKLEVLLLFLLPFTLGELRGGLGKHGHTVHREPAVNRLCADSKRWSGLPVSAQRPFPMGHCPAPSQLPSAKPINLTDESMFPIGTYLLYECLPGYIKRQFSITCKQDSTWTSAEDKCIRKQCKTPSDPENGLVHVHTGIQFGSRINYTCNQGYRLIGSSSAVCVITDQSVDWDTEAPICEWIPCEIPPGIPNGDFFSSTREDFHYGMVVTYRCNTDARGKALFNLVGEPSLYCTSNDGEIGVWSGPPPQCIELNKCTPPPYVENAVMLSENRSLFSLRDIVEFRCHPGFIMKGASSVHCQSLNKWEPELPSCFKGVICRLPQEMSGFQKGLGMKKEYYYGENVTLECEDGYTLEGSSQSQCQSDGSWNPLLAKCVSRSISGLIVGIFIGIIVFILVIIVFIWMILKYKKRNTTDEKYKEVGIHLNYKEDSCVRLQSLLTSQENSSTTSPARNSLTQEVS
Enzyme Length 483
Uniprot Accession Number Q64735
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. Plays a crucial role in early embryonic development by maintaining fetomaternal tolerance. Also acts as a costimulatory factor for T-cells which favors IL-4 secretion. {ECO:0000269|PubMed:10642554, ECO:0000269|PubMed:10779754, ECO:0000269|PubMed:11986227, ECO:0000269|PubMed:1730912, ECO:0000269|PubMed:7528766}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Alternative sequence (1); Chain (1); Disulfide bond (10); Domain (5); Frameshift (2); Glycosylation (2); Modified residue (5); Sequence conflict (9); Signal peptide (1); Topological domain (2); Transmembrane (1)
Keywords 3D-structure;Alternative splicing;Complement pathway;Developmental protein;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 454; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 460; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"; MOD_RES 463; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:19144319"; MOD_RES 468; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 477; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
Post Translational Modification
Signal Peptide SIGNAL 1..40; /evidence=ECO:0000255
Structure 3D X-ray crystallography (1)
Cross Reference PDB 1NTL;
Mapped Pubmed ID 10586048; 11217851; 11698469; 11907125; 11915940; 12393518; 12466851; 12902517; 12914820; 12973023; 14610273; 14670299; 1543915; 16002709; 16127466; 16301324; 16301687; 16444293; 16887189; 17015675; 17015743; 17082645; 17674370; 17916747; 18524992; 18684964; 18799693; 18947875; 19124833; 19136662; 19281793; 19740350; 20484840; 20660348; 20675597; 20941861; 21151910; 21215189; 21267068; 21380996; 2139460; 21677637; 21677750; 22219359; 23109726; 23153828; 23341629; 23382219; 23390291; 24194600; 24632830; 24850152; 25284781; 2528587; 2564419; 27165610; 27626380; 28057640; 28348233; 2952719; 30217731; 7898049; 8138038; 8335915; 8422330;
Motif
Gene Encoded By
Mass 53,763
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda