IED ID | IndEnz0002006664 |
Enzyme Type ID | protease006664 |
Protein Name |
Mannose-binding protein C MBP-C Mannan-binding protein Ra-reactive factor polysaccharide-binding component p28A RaRF p28A |
Gene Name | Mbl2 |
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 | MSLFTSFLLLCVLTAVYAETLTEGAQSSCPVIACSSPGLNGFPGKDGHDGAKGEKGEPGQGLRGLQGPPGKVGPAGPPGNPGSKGATGPKGDRGESVEFDTTNIDLEIAALRSELRAMRKWVLLSMSENVGKKYFMSSVRRMPLNRAKALCSELQGTVATPRNAEENRAIQNVAKDVAFLGITDQRTENVFEDLTGNRVRYTNWNEGEPNNVGSGENCVVLLTNGKWNDVPCSDSFLVVCEFSD |
Enzyme Length | 244 |
Uniprot Accession Number | P08661 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | |
Enzyme Function | FUNCTION: Calcium-dependent lectin involved in innate immune defense. Binds mannose, fucose and N-acetylglucosamine on different microorganisms and activates the lectin complement pathway. Binds to late apoptotic cells, as well as to apoptotic blebs and to necrotic cells, but not to early apoptotic cells, facilitating their uptake by macrophages (By similarity). {ECO:0000250}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Beta strand (7); Chain (1); Coiled coil (1); Disulfide bond (4); Domain (2); Helix (2); Modified residue (5); Region (1); Sequence conflict (1); Signal peptide (1) |
Keywords | 3D-structure;Calcium;Coiled coil;Collagen;Complement activation lectin pathway;Complement pathway;Direct protein sequencing;Disulfide bond;Hydroxylation;Immunity;Innate immunity;Lectin;Mannose-binding;Reference proteome;Repeat;Secreted;Signal |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. |
Modified Residue | MOD_RES 43; /note=4-hydroxyproline; /evidence=ECO:0000255; MOD_RES 58; /note=4-hydroxyproline; /evidence=ECO:0000255; MOD_RES 69; /note=4-hydroxyproline; /evidence=ECO:0000255; MOD_RES 78; /note=4-hydroxyproline; /evidence=ECO:0000255; MOD_RES 81; /note=4-hydroxyproline; /evidence=ECO:0000255 |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..18 |
Structure 3D | X-ray crystallography (13) |
Cross Reference PDB | 1BV4; 1KZA; 1KZB; 1KZC; 1KZD; 1KZE; 1RDI; 1RDJ; 1RDK; 1RDL; 1RDM; 1RDN; 1RDO; |
Mapped Pubmed ID | 10589993; 11337510; 11850428; 20118239; 3124748; 9230118; 9315725; 9920905; 9922165; 9922166; |
Motif | |
Gene Encoded By | |
Mass | 26,014 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |