| IED ID | IndEnz0002000001 |
| Enzyme Type ID | protease000001 |
| 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 CRARF1 PRSS5 |
| Organism | Homo sapiens (Human) |
| 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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MRWLLLYYALCFSLSKASAHTVELNNMFGQIQSPGYPDSYPSDSEVTWNITVPDGFRIKLYFMHFNLESSYLCEYDYVKVETEDQVLATFCGRETTDTEQTPGQEVVLSPGSFMSITFRSDFSNEERFTGFDAHYMAVDVDECKEREDEELSCDHYCHNYIGGYYCSCRFGYILHTDNRTCRVECSDNLFTQRTGVITSPDFPNPYPKSSECLYTIELEEGFMVNLQFEDIFDIEDHPEVPCPYDYIKIKVGPKVLGPFCGEKAPEPISTQSHSVLILFHSDNSGENRGWRLSYRAAGNECPELQPPVHGKIEPSQAKYFFKDQVLVSCDTGYKVLKDNVEMDTFQIECLKDGTWSNKIPTCKIVDCRAPGELEHGLITFSTRNNLTTYKSEIKYSCQEPYYKMLNNNTGIYTCSAQGVWMNKVLGRSLPTCLPVCGLPKFSRKLMARIFNGRPAQKGTTPWIAMLSHLNGQPFCGGSLLGSSWIVTAAHCLHQSLDPEDPTLRDSDLLSPSDFKIILGKHWRLRSDENEQHLGVKHTTLHPQYDPNTFENDVALVELLESPVLNAFVMPICLPEGPQQEGAMVIVSGWGKQFLQRFPETLMEIEIPIVDHSTCQKAYAPLKKKVTRDMICAGEKEGGKDACAGDSGGPMVTLNRERGQWYLVGTVSWGDDCGKKDRYGVYSYIHHNKDWIQRVTGVRN |
| Enzyme Length | 699 |
| Uniprot Accession Number | P48740 |
| Absorption | |
| Active Site | ACT_SITE 490; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 552; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 646; /note=Charge relay system; /evidence=ECO:0000250 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by SERPING1 and A2M. {ECO:0000269|PubMed:11527969, ECO:0000269|PubMed:12538697}. |
| 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 (PubMed:21258343). {ECO:0000269|PubMed:11485744, ECO:0000269|PubMed:21258343}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Alternative sequence (5); Beta strand (48); Chain (3); Disulfide bond (14); Domain (6); Erroneous initiation (1); Glycosylation (6); Helix (8); Metal binding (14); Modified residue (1); Mutagenesis (15); Natural variant (10); Region (3); Sequence conflict (16); Signal peptide (1); Site (1); Turn (11) |
| Keywords | 3D-structure;Alternative splicing;Autocatalytic cleavage;Calcium;Complement activation lectin pathway;Direct protein sequencing;Disease variant;Disulfide bond;EGF-like domain;Glycoprotein;Hydrolase;Hydroxylation;Immunity;Innate immunity;Metal-binding;Protease;Reference proteome;Repeat;Secreted;Serine protease;Signal;Sushi |
| Interact With | O00187-1; P11226; P48740-3; O00187-1; P11226; O00187-1; P11226; P11226 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11485744}. |
| Modified Residue | MOD_RES 159; /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 (By similarity). {ECO:0000250}.; 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. {ECO:0000269|PubMed:11290788}. |
| Signal Peptide | SIGNAL 1..19; /evidence=ECO:0000269|PubMed:11290788 |
| Structure 3D | X-ray crystallography (7) |
| Cross Reference PDB | 3DEM; 3GOV; 4AQB; 4DJZ; 4IGD; 4IW4; 4KKD; |
| Mapped Pubmed ID | 10639434; 10925294; 11012776; 11532276; 12367778; 12370377; 12396008; 12601245; 14280442; 14707097; 15078867; 15199963; 15728497; 15804047; 16102832; 16112196; 16116205; 17179669; 17215869; 17444953; 17897951; 17938215; 18343499; 18456010; 18676680; 18842294; 19170196; 19423540; 19564340; 19607727; 19625176; 19667088; 19692168; 19917686; 19939495; 20032467; 20053996; 20375619; 20375634; 20400674; 20406964; 20438785; 20673767; 21035106; 21054788; 21625439; 21730084; 21900206; 22238349; 22511776; 22536427; 22607836; 22670777; 22691502; 22854970; 22966085; 23220946; 23386610; 23402018; 23602568; 23785123; 23792966; 23841802; 23861840; 23911397; 24023860; 24189400; 24424083; 24472859; 24683193; 25533914; 25745807; 25862418; 26173080; 26260032; 26371246; 26536449; 26614707; 26645987; 26789649; 27055907; 27057739; 27219453; 27344311; 27404661; 27405496; 27535802; 27605007; 28216633; 28318015; 28720568; 29324883; 29407414; 29415992; 29475986; 29515573; 31130964; 31325724; 32240160; 32286427; 32441374; 32751929; 33780946; 33858964; 34650023; 6019133; 70787; 9153228; |
| Motif | |
| Gene Encoded By | |
| Mass | 79,247 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.10 mM for Ac-Gly-Lys-OMe (at 30 degrees Celsius) {ECO:0000269|PubMed:11527969, ECO:0000269|PubMed:12538697}; KM=310 uM for Bz-Arg-OEt (at 30 degrees Celsius) {ECO:0000269|PubMed:11527969, ECO:0000269|PubMed:12538697}; KM=4.8 uM for C2 (at 37 degrees Celsius) {ECO:0000269|PubMed:11527969, ECO:0000269|PubMed:12538697}; |
| Metal Binding | METAL 68; /note=Calcium 1; METAL 76; /note=Calcium 1; METAL 121; /note=Calcium 1; METAL 123; /note=Calcium 1; via carbonyl oxygen; METAL 139; /note=Calcium 2; METAL 140; /note=Calcium 2; via carbonyl oxygen; METAL 142; /note=Calcium 2; METAL 159; /note=Calcium 2; METAL 160; /note=Calcium 2; via carbonyl oxygen; METAL 163; /note=Calcium 2; via carbonyl oxygen; METAL 235; /note=Calcium 3; METAL 245; /note=Calcium 3; METAL 282; /note=Calcium 3; METAL 284; /note=Calcium 3; via carbonyl oxygen |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.B7; |