Detail Information for IndEnz0002006664
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