Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005576 | cellular_component | extracellular region |
| B | 0005576 | cellular_component | extracellular region |
| C | 0005576 | cellular_component | extracellular region |
| D | 0005576 | cellular_component | extracellular region |
| E | 0005576 | cellular_component | extracellular region |
| F | 0005576 | cellular_component | extracellular region |
| G | 0005576 | cellular_component | extracellular region |
| H | 0005576 | cellular_component | extracellular region |
| I | 0005576 | cellular_component | extracellular region |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE B 500 |
| Chain | Residue |
| B | ASP63 |
| B | TYR95 |
| B | TYR188 |
| B | HIS249 |
| B | CO3600 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE CO3 B 600 |
| Chain | Residue |
| B | ALA126 |
| B | GLY127 |
| B | TYR188 |
| B | HIS249 |
| B | FE500 |
| B | ASP63 |
| B | TYR95 |
| B | THR120 |
| B | ARG124 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE A 500 |
| Chain | Residue |
| A | ASP63 |
| A | TYR95 |
| A | TYR188 |
| A | HIS249 |
| A | CO3600 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE CO3 A 600 |
| Chain | Residue |
| A | ASP63 |
| A | TYR95 |
| A | THR120 |
| A | ARG124 |
| A | ALA126 |
| A | GLY127 |
| A | TYR188 |
| A | HIS249 |
| A | FE500 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE C 500 |
| Chain | Residue |
| C | ASP63 |
| C | TYR95 |
| C | TYR188 |
| C | HIS249 |
| C | CO3600 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE CO3 C 600 |
| Chain | Residue |
| C | ASP63 |
| C | TYR95 |
| C | THR120 |
| C | ARG124 |
| C | ALA126 |
| C | GLY127 |
| C | TYR188 |
| C | HIS249 |
| C | FE500 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE D 500 |
| Chain | Residue |
| D | ASP63 |
| D | TYR95 |
| D | TYR188 |
| D | HIS249 |
| D | CO3600 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE CO3 D 600 |
| Chain | Residue |
| D | ASP63 |
| D | TYR95 |
| D | THR120 |
| D | ARG124 |
| D | SER125 |
| D | ALA126 |
| D | GLY127 |
| D | TYR188 |
| D | HIS249 |
| D | FE500 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE E 500 |
| Chain | Residue |
| E | ASP63 |
| E | TYR95 |
| E | TYR188 |
| E | HIS249 |
| E | CO3600 |
| site_id | BC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE CO3 E 600 |
| Chain | Residue |
| E | ASP63 |
| E | TYR95 |
| E | THR120 |
| E | ARG124 |
| E | SER125 |
| E | ALA126 |
| E | GLY127 |
| E | TYR188 |
| E | HIS249 |
| E | FE500 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE F 500 |
| Chain | Residue |
| F | ASP63 |
| F | TYR95 |
| F | TYR188 |
| F | HIS249 |
| F | CO3600 |
| site_id | BC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE CO3 F 600 |
| Chain | Residue |
| F | ASP63 |
| F | TYR95 |
| F | THR120 |
| F | ARG124 |
| F | SER125 |
| F | ALA126 |
| F | GLY127 |
| F | TYR188 |
| F | HIS249 |
| F | FE500 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE G 500 |
| Chain | Residue |
| G | ASP63 |
| G | TYR95 |
| G | TYR188 |
| G | HIS249 |
| G | CO3600 |
| site_id | BC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE CO3 G 600 |
| Chain | Residue |
| G | TYR188 |
| G | FE500 |
| G | ASP63 |
| G | TYR95 |
| G | THR120 |
| G | ARG124 |
| G | SER125 |
| G | ALA126 |
| G | GLY127 |
| site_id | BC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE H 500 |
| Chain | Residue |
| H | ASP63 |
| H | TYR95 |
| H | TYR188 |
| H | HIS249 |
| H | CO3600 |
| site_id | BC7 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE CO3 H 600 |
| Chain | Residue |
| H | ASP63 |
| H | TYR95 |
| H | THR120 |
| H | ARG124 |
| H | SER125 |
| H | ALA126 |
| H | GLY127 |
| H | TYR188 |
| H | HIS249 |
| H | FE500 |
| site_id | BC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE I 500 |
| Chain | Residue |
| I | ASP63 |
| I | TYR95 |
| I | TYR188 |
| I | HIS249 |
| I | CO3600 |
| site_id | BC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE CO3 I 600 |
| Chain | Residue |
| I | ASP63 |
| I | TYR95 |
| I | THR120 |
| I | ARG124 |
| I | SER125 |
| I | ALA126 |
| I | GLY127 |
| I | TYR188 |
| I | FE500 |
Functional Information from PROSITE/UniProt
| site_id | PS00205 |
| Number of Residues | 10 |
| Details | TRANSFERRIN_LIKE_1 Transferrin-like domain signature 1. YyAVAVVKKD |
| Chain | Residue | Details |
| B | TYR95-ASP104 | |
| site_id | PS00206 |
| Number of Residues | 17 |
| Details | TRANSFERRIN_LIKE_2 Transferrin-like domain signature 2. YsGAFKCLkdgaGDVAF |
| Chain | Residue | Details |
| B | TYR188-PHE204 | |
| site_id | PS00207 |
| Number of Residues | 31 |
| Details | TRANSFERRIN_LIKE_3 Transferrin-like domain signature 3. QYeLLClDntrkp...VdeykdChlAqvpsHtVV |
| Chain | Residue | Details |
| B | GLN222-VAL252 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2898 |
| Details | Domain: {"description":"Transferrin-like 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00741","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 36 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22327295","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3V83","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 36 |
| Details | Binding site: {} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 9 |
| Details | Modified residue: {"description":"Dimethylated arginine","evidences":[{"source":"UniProtKB","id":"P12346","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 9 |
| Details | Glycosylation: {"description":"O-linked (GalNAc...) serine","featureId":"CAR_000073"} |