Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| A | 0031418 | molecular_function | L-ascorbic acid binding |
| A | 0032963 | biological_process | collagen metabolic process |
| C | 0000413 | biological_process | protein peptidyl-prolyl isomerization |
| C | 0003755 | molecular_function | peptidyl-prolyl cis-trans isomerase activity |
| C | 0006457 | biological_process | protein folding |
Functional Information from PROSITE/UniProt
| site_id | PS00014 |
| Number of Residues | 4 |
| Details | ER_TARGET Endoplasmic reticulum targeting sequence. KDEL |
| Chain | Residue | Details |
| A | LYS733-LEU736 | |
| site_id | PS00170 |
| Number of Residues | 18 |
| Details | CSA_PPIASE_1 Cyclophilin-type peptidyl-prolyl cis-trans isomerase signature. YknSkFHRVIkdFMiQGG |
| Chain | Residue | Details |
| C | TYR56-GLY73 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 33 |
| Details | Repeat: {"description":"TPR 1"} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 33 |
| Details | Repeat: {"description":"TPR 2"} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 33 |
| Details | Repeat: {"description":"TPR 3"} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 33 |
| Details | Repeat: {"description":"TPR 4"} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 114 |
| Details | Domain: {"description":"Fe2OG dioxygenase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00805","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Active site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 3 |
| Details | Binding site: {} |
| site_id | SWS_FT_FI8 |
| Number of Residues | 5 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI10 |
| Number of Residues | 157 |
| Details | Domain: {"description":"PPIase cyclophilin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00156","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI11 |
| Number of Residues | 3 |
| Details | Motif: {"description":"Prevents secretion from ER"} |
| site_id | SWS_FT_FI12 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q99KR7","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI13 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q99KR7","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI14 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"S-nitrosocysteine","evidences":[{"source":"UniProtKB","id":"Q99KR7","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI15 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P24369","evidenceCode":"ECO:0000250"}]} |
