| IED ID | IndEnz0002000003 |
| Enzyme Type ID | protease000003 |
| Protein Name |
Mannan-binding lectin serine protease 1 EC 3.4.21.- Complement factor MASP-3 Complement-activating component of Ra-reactive factor Mannose-binding lectin-associated serine protease 1 MASP-1 Mannose-binding protein-associated serine protease Ra-reactive factor serine protease p100 RaRF Serine protease 5 Cleaved into: Mannan-binding lectin serine protease 1 heavy chain; Mannan-binding lectin serine protease 1 light chain |
| Gene Name | Masp1 Crarf Masp3 |
| 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 | MRFLSFRRLLLYHVLCLTLTEVSAHTVELNEMFGQIQSPGYPDSYPSDSEVTWNITVPEGFRVQLYFMHFNLESSYLCEYDYVKVETEDQVLATFCGRETTDTEQTPGQEVVLSPGSFMSVTFRSDFSNEERFTGFDAHYMAVDVDECKEREDEELSCDHYCHNYIGGYYCSCRFGYILHTDNRTCRVECSGNLFTQRTGTITSPDYPNPYPKSSECSYTIDLEEGFMVTLQFEDIFDIEDHPEVPCPYDYIKIKAGSKVWGPFCGEKSPEPISTQSHSIQILFRSDNSGENRGWRLSYRAAGNECPKLQPPVYGKIEPSQAVYSFKDQVLISCDTGYKVLKDNEVMDTFQIECLKDGAWSNKIPTCKIVDCGVPAVLKHGLVTFSTRNNLTTYKSEIRYSCQQPYYKMLHNTTGVYTCSAHGTWTNEVLKRSLPTCLPVCGLPKFSRKHISRIFNGRPAQKGTTPWIAMLSQLNGQPFCGGSLLGSNWVLTAAHCLHHPLDPEEPILHNSHLLSPSDFKIIMGKHWRRRSDEDEQHLHVKHIMLHPLYNPSTFENDLGLVELSESPRLNDFVMPVCLPEHPSTEGTMVIVSGWGKQFLQRLPENLMEIEIPIVNYHTCQEAYTPLGKKVTQDMICAGEKEGGKDACAGDSGGPMVTKDAERDQWYLVGVVSWGEDCGKKDRYGVYSYIYPNKDWIQRVTGVRN |
| Enzyme Length | 704 |
| Uniprot Accession Number | Q8CHN8 |
| Absorption | |
| Active Site | ACT_SITE 495; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 557; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 651; /note=Charge relay system; /evidence=ECO:0000250 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by SERPING1 and A2M. {ECO:0000250}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Functions in the lectin pathway of complement, which performs a key role in innate immunity by recognizing pathogens through patterns of sugar moieties and neutralizing them. The lectin pathway is triggered upon binding of mannan-binding lectin (MBL) and ficolins to sugar moieties which leads to activation of the associated proteases MASP1 and MASP2. Functions as an endopeptidase and may activate MASP2 or C2 or directly activate C3 the key component of complement reaction. Isoform 2 may have an inhibitory effect on the activation of the lectin pathway of complement or may cleave IGFBP5. Also plays a role in development. {ECO:0000250|UniProtKB:P48740}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Alternative sequence (4); Beta strand (10); Chain (3); Disulfide bond (14); Domain (6); Glycosylation (6); Metal binding (14); Modified residue (1); Mutagenesis (1); Region (4); Sequence conflict (2); Signal peptide (1); Site (1); Turn (1) |
| Keywords | 3D-structure;Alternative splicing;Autocatalytic cleavage;Calcium;Complement activation lectin pathway;Disulfide bond;EGF-like domain;Glycoprotein;Hydrolase;Hydroxylation;Immunity;Innate immunity;Metal-binding;Protease;Reference proteome;Repeat;Secreted;Serine protease;Signal;Sushi |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12847554}. |
| Modified Residue | MOD_RES 164; /note=(3R)-3-hydroxyasparagine; /evidence=ECO:0000255 |
| Post Translational Modification | PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. {ECO:0000250}.; PTM: N-glycosylated. Some N-linked glycan are of the complex-type. {ECO:0000269|PubMed:10913141}.; PTM: Autoproteolytic processing of the proenzyme produces the active enzyme composed on the heavy and the light chain held together by a disulfide bond. Isoform 1 but not isoform 2 is activated through autoproteolytic processing (By similarity). {ECO:0000250}. |
| Signal Peptide | SIGNAL 1..24; /evidence=ECO:0000250 |
| Structure 3D | X-ray crystallography (7) |
| Cross Reference PDB | 3POB; 3POE; 3POF; 3POG; 3POI; 3POJ; 5CKQ; |
| Mapped Pubmed ID | 22078562; 28111019; |
| Motif | |
| Gene Encoded By | |
| Mass | 80,097 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=13 uM for C2 (at 37 degrees Celsius) {ECO:0000269|PubMed:15060079}; |
| Metal Binding | METAL 73; /note=Calcium 1; /evidence=ECO:0000250; METAL 81; /note=Calcium 1; /evidence=ECO:0000250; METAL 126; /note=Calcium 1; /evidence=ECO:0000250; METAL 128; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 144; /note=Calcium 2; /evidence=ECO:0000250; METAL 145; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 147; /note=Calcium 2; /evidence=ECO:0000250; METAL 164; /note=Calcium 2; /evidence=ECO:0000250; METAL 165; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 168; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 240; /note=Calcium 3; /evidence=ECO:0000250; METAL 250; /note=Calcium 3; /evidence=ECO:0000250; METAL 287; /note=Calcium 3; /evidence=ECO:0000250; METAL 289; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.B7; |