Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004866 | molecular_function | endopeptidase inhibitor activity |
| B | 0004866 | molecular_function | endopeptidase inhibitor activity |
| B | 0005576 | cellular_component | extracellular region |
| B | 0005615 | cellular_component | extracellular space |
| B | 0006954 | biological_process | inflammatory response |
| B | 0006956 | biological_process | complement activation |
| C | 0005576 | cellular_component | extracellular region |
| D | 0004866 | molecular_function | endopeptidase inhibitor activity |
| E | 0004866 | molecular_function | endopeptidase inhibitor activity |
| E | 0005576 | cellular_component | extracellular region |
| E | 0005615 | cellular_component | extracellular space |
| E | 0006954 | biological_process | inflammatory response |
| E | 0006956 | biological_process | complement activation |
| F | 0005576 | cellular_component | extracellular region |
| H | 0004252 | molecular_function | serine-type endopeptidase activity |
| H | 0006508 | biological_process | proteolysis |
| J | 0004252 | molecular_function | serine-type endopeptidase activity |
| J | 0006508 | biological_process | proteolysis |
Functional Information from PROSITE/UniProt
| site_id | PS00477 |
| Number of Residues | 9 |
| Details | ALPHA_2_MACROGLOBULIN Alpha-2-macroglobulin family thiolester region signature. PrGCGEQtM |
| Chain | Residue | Details |
| B | PRO1007-MET1015 |
| site_id | PS01177 |
| Number of Residues | 35 |
| Details | ANAPHYLATOXIN_1 Anaphylatoxin domain signature. CCqdGvtrlpmmrSCEqraarvq..QpdCrepfls.CC |
| Chain | Residue | Details |
| B | CYS702-CYS736 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12754519","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18780401","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27599733","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 68 |
| Details | Domain: {"description":"Anaphylatoxin-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU00022","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Site: {"description":"Cleavage; by C1S, MASP2 and GZMK","evidences":[{"source":"PubMed","id":"16169853","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine; by FAM20C","evidences":[{"source":"PubMed","id":"26091039","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27599733","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"O-linked (GalNAc...) threonine","evidences":[{"source":"PubMed","id":"23234360","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18780401","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19139490","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"14760718","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | Cross-link: {"description":"Isoglutamyl cysteine thioester (Cys-Gln)","evidences":[{"source":"PubMed","id":"12367531","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 294 |
| Details | Domain: {"description":"NTR","evidences":[{"source":"PROSITE-ProRule","id":"PRU00295","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 130 |
| Details | Domain: {"description":"Sushi 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00302","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 136 |
| Details | Domain: {"description":"Sushi 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00302","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 478 |
| Details | Domain: {"description":"Peptidase S1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00274","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 6 |
| Details | Active site: {"description":"Charge relay system"} |
| Chain | Residue | Details |
