| IED ID | IndEnz0002004161 |
| Enzyme Type ID | protease004161 |
| Protein Name |
Mannose-binding protein A MBP-A Mannan-binding protein Ra-reactive factor polysaccharide-binding component p28B RaRF p28B |
| Gene Name | Mbl1 |
| 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 | MLLLPLLPVLLCVVSVSSSGSQTCEDTLKTCSVIACGRDGRDGPKGEKGEPGQGLRGLQGPPGKLGPPGSVGSPGSPGPKGQKGDHGDNRAIEEKLANMEAEIRILKSKLQLTNKLHAFSMGKKSGKKLFVTNHEKMPFSKVKSLCTELQGTVAIPRNAEENKAIQEVATGIAFLGITDEATEGQFMYVTGGRLTYSNWKKDEPNNHGSGEDCVIILDNGLWNDISCQASFKAVCEFPA |
| Enzyme Length | 239 |
| Uniprot Accession Number | P39039 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Calcium-dependent lectin. Plays a role in the innate immune response by binding mannose, fucose and N-acetylglucosamine moieties on different microorganisms and mediating activation of the lectin complement pathway (By similarity). 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, ECO:0000250|UniProtKB:P19999}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (1); Chain (1); Disulfide bond (2); Domain (2); Glycosylation (4); Metal binding (9); Modified residue (10); Region (2); Signal peptide (1) |
| Keywords | Alternative splicing;Calcium;Collagen;Complement activation lectin pathway;Complement pathway;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydroxylation;Immunity;Innate immunity;Lectin;Mannose-binding;Metal-binding;Reference proteome;Repeat;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1637828, ECO:0000269|PubMed:25419660}. |
| Modified Residue | MOD_RES 44; /note=4-hydroxyproline; /evidence=ECO:0000255; MOD_RES 45; /note=5-hydroxylysine; /evidence=ECO:0000250|UniProtKB:P19999; MOD_RES 48; /note=5-hydroxylysine; /evidence=ECO:0000250|UniProtKB:P19999; MOD_RES 51; /note=4-hydroxyproline; /evidence=ECO:0000250|UniProtKB:P19999; MOD_RES 62; /note=4-hydroxyproline; /evidence=ECO:0000250; MOD_RES 68; /note=4-hydroxyproline; /evidence=ECO:0000250; MOD_RES 74; /note=4-hydroxyproline; /evidence=ECO:0000250; MOD_RES 79; /note=4-hydroxyproline; /evidence=ECO:0000255; MOD_RES 80; /note=5-hydroxylysine; /evidence=ECO:0000250|UniProtKB:P19999; MOD_RES 83; /note=5-hydroxylysine; /evidence=ECO:0000250|UniProtKB:P19999 |
| Post Translational Modification | PTM: Hydroxylated on lysine and proline residues within the collagen-like domain. {ECO:0000250|UniProtKB:P19999}.; PTM: O-glycosylated. O-linked glycans on hydroxylysine residues consist of Glc-Gal disaccharides bound to the oxygen atom of post-translationally added hydroxyl groups. {ECO:0000250|UniProtKB:P19999}. |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000269|PubMed:1637828 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10047541; 10423401; 10679100; 10806358; 11021254; 11309157; 12270724; 12417723; 12466851; 14761934; 15148336; 15498041; 15735014; 15749852; 15879138; 15882434; 15972690; 16299314; 16424207; 16602821; 16982912; 17114482; 17363917; 17404294; 17475881; 17485663; 17681821; 17785849; 18180310; 18493734; 18501966; 18672286; 19112490; 19380618; 19476514; 19749170; 19843088; 20140243; 20305659; 20375621; 20585009; 20810984; 21257205; 21943708; 22079428; 22156595; 22457620; 22566568; 22792067; 23032324; 23139754; 23427256; 23478320; 23936347; 24167262; 24743949; 25008177; 25482922; 26631482; 27106289; 27733776; 28700732; 28819174; 29497373; 30351498; 30354247; 30573546; 30706943; 30723261; 31175160; 31578522; 31869396; 33927296; 34547288; 7499852; 7894166; 8961631; 9417917; 9828146; |
| Motif | |
| Gene Encoded By | |
| Mass | 25,396 |
| Kinetics | |
| Metal Binding | METAL 179; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:P19999; METAL 183; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:P19999; METAL 203; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:P19999; METAL 205; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:P19999; METAL 211; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P19999; METAL 211; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:P19999; METAL 212; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:P19999; METAL 223; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:P19999; METAL 224; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:P19999 |
| Rhea ID | |
| Cross Reference Brenda |