Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005615 | cellular_component | extracellular space |
| A | 0005623 | cellular_component | obsolete cell |
| A | 0005769 | cellular_component | early endosome |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006811 | biological_process | monoatomic ion transport |
| A | 0006826 | biological_process | iron ion transport |
| A | 0006879 | biological_process | intracellular iron ion homeostasis |
| A | 0006953 | biological_process | acute-phase response |
| A | 0008199 | molecular_function | ferric iron binding |
| A | 0009410 | biological_process | response to xenobiotic stimulus |
| A | 0019730 | biological_process | antimicrobial humoral response |
| A | 0019731 | biological_process | antibacterial humoral response |
| A | 0032496 | biological_process | response to lipopolysaccharide |
| A | 0034755 | biological_process | iron ion transmembrane transport |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0055037 | cellular_component | recycling endosome |
| A | 1990377 | cellular_component | organomineral extracellular matrix |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE AL A 687 |
| Chain | Residue |
| A | ASP60 |
| A | TYR92 |
| A | TYR191 |
| A | HIS250 |
| A | BCT688 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE BCT A 688 |
| Chain | Residue |
| A | SER122 |
| A | ALA123 |
| A | GLY124 |
| A | TYR191 |
| A | HIS250 |
| A | AL687 |
| A | ASP60 |
| A | TYR92 |
| A | THR117 |
| A | ARG121 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE AL A 689 |
| Chain | Residue |
| A | ASP395 |
| A | TYR431 |
| A | TYR524 |
| A | HIS592 |
| A | BCT690 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE BCT A 690 |
| Chain | Residue |
| A | ASP395 |
| A | TYR431 |
| A | THR456 |
| A | ARG460 |
| A | THR461 |
| A | ALA462 |
| A | GLY463 |
| A | TYR524 |
| A | HIS592 |
| A | AL689 |
Functional Information from PROSITE/UniProt
| site_id | PS00205 |
| Number of Residues | 10 |
| Details | TRANSFERRIN_LIKE_1 Transferrin-like domain signature 1. YyAVAVVKKG |
| Chain | Residue | Details |
| A | TYR92-GLY101 | |
| A | TYR431-ASP440 | |
| site_id | PS00206 |
| Number of Residues | 17 |
| Details | TRANSFERRIN_LIKE_2 Transferrin-like domain signature 2. YsGAFHCLkdgkGDVAF |
| Chain | Residue | Details |
| A | TYR191-PHE207 | |
| A | TYR524-PHE539 | |
| site_id | PS00207 |
| Number of Residues | 31 |
| Details | TRANSFERRIN_LIKE_3 Transferrin-like domain signature 3. EYeLLClDgsrqp...VdnyktCnwArvaaHaVV |
| Chain | Residue | Details |
| A | GLU223-VAL253 | |
| A | ASP565-VAL595 | |
| site_id | PS00962 |
| Number of Residues | 12 |
| Details | RIBOSOMAL_S2_1 Ribosomal protein S2 signature 1. VpSLMDSQLYLG |
| Chain | Residue | Details |
| A | VAL310-GLY321 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 326 |
| Details | Domain: {"description":"Transferrin-like 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00741","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | Binding site: {} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"6895872","evidenceCode":"ECO:0000269"}]} |
