2XRC
Human complement factor I
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0002376 | biological_process | immune system process |
A | 0004252 | molecular_function | serine-type endopeptidase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005576 | cellular_component | extracellular region |
A | 0005615 | cellular_component | extracellular space |
A | 0006508 | biological_process | proteolysis |
A | 0006956 | biological_process | complement activation |
A | 0006958 | biological_process | complement activation, classical pathway |
A | 0008233 | molecular_function | peptidase activity |
A | 0008236 | molecular_function | serine-type peptidase activity |
A | 0016020 | cellular_component | membrane |
A | 0016787 | molecular_function | hydrolase activity |
A | 0045087 | biological_process | innate immune response |
A | 0046872 | molecular_function | metal ion binding |
A | 0070062 | cellular_component | extracellular exosome |
B | 0002376 | biological_process | immune system process |
B | 0004252 | molecular_function | serine-type endopeptidase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005576 | cellular_component | extracellular region |
B | 0005615 | cellular_component | extracellular space |
B | 0006508 | biological_process | proteolysis |
B | 0006956 | biological_process | complement activation |
B | 0006958 | biological_process | complement activation, classical pathway |
B | 0008233 | molecular_function | peptidase activity |
B | 0008236 | molecular_function | serine-type peptidase activity |
B | 0016020 | cellular_component | membrane |
B | 0016787 | molecular_function | hydrolase activity |
B | 0045087 | biological_process | innate immune response |
B | 0046872 | molecular_function | metal ion binding |
B | 0070062 | cellular_component | extracellular exosome |
C | 0002376 | biological_process | immune system process |
C | 0004252 | molecular_function | serine-type endopeptidase activity |
C | 0005515 | molecular_function | protein binding |
C | 0005576 | cellular_component | extracellular region |
C | 0005615 | cellular_component | extracellular space |
C | 0006508 | biological_process | proteolysis |
C | 0006956 | biological_process | complement activation |
C | 0006958 | biological_process | complement activation, classical pathway |
C | 0008233 | molecular_function | peptidase activity |
C | 0008236 | molecular_function | serine-type peptidase activity |
C | 0016020 | cellular_component | membrane |
C | 0016787 | molecular_function | hydrolase activity |
C | 0045087 | biological_process | innate immune response |
C | 0046872 | molecular_function | metal ion binding |
C | 0070062 | cellular_component | extracellular exosome |
D | 0002376 | biological_process | immune system process |
D | 0004252 | molecular_function | serine-type endopeptidase activity |
D | 0005515 | molecular_function | protein binding |
D | 0005576 | cellular_component | extracellular region |
D | 0005615 | cellular_component | extracellular space |
D | 0006508 | biological_process | proteolysis |
D | 0006956 | biological_process | complement activation |
D | 0006958 | biological_process | complement activation, classical pathway |
D | 0008233 | molecular_function | peptidase activity |
D | 0008236 | molecular_function | serine-type peptidase activity |
D | 0016020 | cellular_component | membrane |
D | 0016787 | molecular_function | hydrolase activity |
D | 0045087 | biological_process | innate immune response |
D | 0046872 | molecular_function | metal ion binding |
D | 0070062 | cellular_component | extracellular exosome |
Functional Information from PROSITE/UniProt
site_id | PS00134 |
Number of Residues | 6 |
Details | TRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC |
Chain | Residue | Details |
A | LEU358-CYS363 |
site_id | PS00135 |
Number of Residues | 12 |
Details | TRYPSIN_SER Serine proteases, trypsin family, serine active site. DAckGDSGGPLV |
Chain | Residue | Details |
A | ASP501-VAL512 |
site_id | PS01209 |
Number of Residues | 23 |
Details | LDLRA_1 LDL-receptor class A (LDLRA) domain signature. CIpsqyq.CNgevDCitg.EDEvg...C |
Chain | Residue | Details |
A | CYS253-CYS275 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 212 |
Details | Domain: {"description":"Kazal-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU00798","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 196 |
Details | Domain: {"description":"SRCR","evidences":[{"source":"PROSITE-ProRule","id":"PRU00196","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 108 |
Details | Domain: {"description":"LDL-receptor class A 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00124","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 11 |
Details | Active site: {"description":"Charge relay system","evidences":[{"source":"UniProtKB","id":"P00750","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 48 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"21768352","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2XRC","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 10 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21768352","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2XRC","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 4 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19139490","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19838169","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21768352","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2XRC","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 4 |
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":"21768352","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2XRC","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI9 |
Number of Residues | 4 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"21768352","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2XRC","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |