| IED ID | IndEnz0002000006 |
| Enzyme Type ID | protease000006 |
| Protein Name |
Mannan-binding lectin serine protease 2 EC 3.4.21.104 MBL-associated serine protease 2 Mannose-binding protein-associated serine protease 2 MASP-2 Cleaved into: Mannan-binding lectin serine protease 2 A chain; Mannan-binding lectin serine protease 2 B chain |
| Gene Name | Masp2 |
| 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 | MRLLIVLGLLWSLVATLLGSKWPEPVFGRLVSLGFPEKYGNHQDRSWTLTAPPGFRLRLYFTHFNLELSYRCEYDFVKLTSGTKVLATLCGQESTDTERAPGNDTFYSLGPSLKVTFHSDYSNEKPFTGFEAFYAAEDVDECRTSLGDSVPCDHYCHNYLGGYYCSCRVGYILHQNKHTCSALCSGQVFTGRSGFLSSPEYPQPYPKLSSCAYNIRLEEGFSITLDFVESFDVEMHPEAQCPYDSLKIQTDKREYGPFCGKTLPPRIETDSNKVTITFTTDESGNHTGWKIHYTSTAQPCPDPTAPPNGHISPVQATYVLKDSFSVFCKTGFELLQGSVPLKSFTAVCQKDGSWDRPIPECSIIDCGPPDDLPNGHVDYITGPEVTTYKAVIQYSCEETFYTMSSNGKYVCEADGFWTSSKGEKSLPVCKPVCGLSTHTSGGRIIGGQPAKPGDFPWQVLLLGETTAAGALIHDDWVLTAAHAVYGKTEAMSSLDIRMGILKRLSLIYTQAWPEAVFIHEGYTHGAGFDNDIALIKLKNKVTINRNIMPICLPRKEAASLMKTDFVGTVAGWGLTQKGFLARNLMFVDIPIVDHQKCATAYTKQPYPGAKVTVNMLCAGLDRGGKDSCRGDSGGALVFLDNETQRWFVGGIVSWGSINCGGSEQYGVYTKVTNYIPWIENIINNF |
| Enzyme Length | 685 |
| Uniprot Accession Number | Q9JJS8 |
| Absorption | |
| Active Site | ACT_SITE 482; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 531; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 632; /note=Charge relay system; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Selective cleavage after Arg-223 in complement component C2 (-Ser-Leu-Gly-Arg-|-Lys-Ile-Gln-Ile) and after Arg-76 in complement component C4 (-Gly-Leu-Gln-Arg-|-Ala-Leu-Glu-Ile).; EC=3.4.21.104; |
| DNA Binding | |
| EC Number | 3.4.21.104 |
| Enzyme Function | FUNCTION: Serum protease that plays an important role in the activation of the complement system via mannose-binding lectin. After activation by auto-catalytic cleavage it cleaves C2 and C4, leading to their activation and to the formation of C3 convertase. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Alternative sequence (2); Beta strand (24); Chain (3); Disulfide bond (12); Domain (6); Glycosylation (3); Helix (1); Metal binding (9); Modified residue (1); Sequence conflict (6); Signal peptide (1); Site (1); Turn (3) |
| Keywords | 3D-structure;Alternative splicing;Autocatalytic cleavage;Calcium;Complement pathway;Direct protein sequencing;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. |
| Modified Residue | MOD_RES 158; /note=(3R)-3-hydroxyasparagine; /evidence=ECO:0000269|PubMed:12743029 |
| Post Translational Modification | PTM: N-glycosylated. {ECO:0000269|PubMed:10913141, ECO:0000269|PubMed:12743029}.; PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. {ECO:0000250}. |
| Signal Peptide | SIGNAL 1..19; /evidence=ECO:0000269|PubMed:10913141 |
| Structure 3D | X-ray crystallography (4) |
| Cross Reference PDB | 1NT0; 5CIS; 5CKM; 5CKN; |
| Mapped Pubmed ID | 15060079; 16272342; 17204478; 17579066; 20118239; 28111019; |
| Motif | |
| Gene Encoded By | |
| Mass | 75,667 |
| Kinetics | |
| Metal Binding | METAL 67; /note=Calcium 1; /evidence=ECO:0000250; METAL 75; /note=Calcium 1; /evidence=ECO:0000250; METAL 120; /note=Calcium 1; /evidence=ECO:0000250; METAL 122; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 123; /note=Calcium 1; /evidence=ECO:0000250; METAL 138; /note=Calcium 2; METAL 139; /note=Calcium 2; via carbonyl oxygen; METAL 159; /note=Calcium 2; METAL 162; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.104; |