Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004252 | molecular_function | serine-type endopeptidase activity |
| A | 0006508 | biological_process | proteolysis |
| B | 0004672 | molecular_function | protein kinase activity |
| B | 0004713 | molecular_function | protein tyrosine kinase activity |
| B | 0004714 | molecular_function | transmembrane receptor protein tyrosine kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006468 | biological_process | protein phosphorylation |
| B | 0007169 | biological_process | cell surface receptor protein tyrosine kinase signaling pathway |
| B | 0016020 | cellular_component | membrane |
| B | 0017154 | molecular_function | semaphorin receptor activity |
| B | 0071526 | biological_process | semaphorin-plexin signaling pathway |
Functional Information from PROSITE/UniProt
| site_id | PS00021 |
| Number of Residues | 14 |
| Details | KRINGLE_1 Kringle domain signature. YCRNprgeeggpWC |
| Chain | Residue | Details |
| A | TYR176-CYS189 | |
| A | TYR259-CYS271 | |
| A | TYR353-CYS365 | |
| A | TYR439-CYS452 | |
| site_id | PS00107 |
| Number of Residues | 27 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGRGHFGCVYhGtlldndgkkih.......CAVK |
| Chain | Residue | Details |
| B | ILE1084-LYS1110 | |
| site_id | PS00109 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FVHrDLAARNCML |
| Chain | Residue | Details |
| B | PHE1200-LEU1212 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 78 |
| Details | Domain: {"description":"Kringle 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00121","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 77 |
| Details | Domain: {"description":"Kringle 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00121","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 226 |
| Details | Domain: {"description":"Peptidase S1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00274","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","featureId":"CAR_000022","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","featureId":"CAR_000024","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","featureId":"CAR_000025","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 7 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19196183","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"O-linked (Man) threonine","evidences":[{"source":"PubMed","id":"37186866","evidenceCode":"ECO:0000269"}]} |
