8TN9
Structural architecture of the acidic region of the B domain of coagulation factor V
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005507 | molecular_function | copper ion binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005615 | cellular_component | extracellular space |
| A | 0005788 | cellular_component | endoplasmic reticulum lumen |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0007596 | biological_process | blood coagulation |
| A | 0007599 | biological_process | hemostasis |
| A | 0008015 | biological_process | blood circulation |
| A | 0016020 | cellular_component | membrane |
| A | 0030134 | cellular_component | COPII-coated ER to Golgi transport vesicle |
| A | 0031091 | cellular_component | platelet alpha granule |
| A | 0031093 | cellular_component | platelet alpha granule lumen |
| A | 0032571 | biological_process | response to vitamin K |
| A | 0033116 | cellular_component | endoplasmic reticulum-Golgi intermediate compartment membrane |
| A | 0046872 | molecular_function | metal ion binding |
| A | 1903561 | cellular_component | extracellular vesicle |
Functional Information from PROSITE/UniProt
| site_id | PS00079 |
| Number of Residues | 21 |
| Details | MULTICOPPER_OXIDASE1 Multicopper oxidases signature 1. GkWiIsSlTPkhLqAGMqayI |
| Chain | Residue | Details |
| A | GLY276-ILE296 | |
| A | GLY1852-PHE1872 |
| site_id | PS01285 |
| Number of Residues | 34 |
| Details | FA58C_1 Coagulation factors 5/8 type C domain (FA58C) signature 1. AWsveklaaefaskp..WIqVDmqkeviItgIqTQG |
| Chain | Residue | Details |
| A | ALA1919-GLY1952 | |
| A | ALA2083-GLY2112 |
| site_id | PS01286 |
| Number of Residues | 17 |
| Details | FA58C_2 Coagulation factors 5/8 type C domain (FA58C) signature 2. Ptraynrpt..LRlELqGC |
| Chain | Residue | Details |
| A | PRO2017-CYS2033 | |
| A | PRO2177-CYS2193 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 299 |
| Details | Domain: {"description":"F5/8 type A 1"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 163 |
| Details | Domain: {"description":"Plastocyanin-like 1"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 126 |
| Details | Domain: {"description":"Plastocyanin-like 2"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 336 |
| Details | Domain: {"description":"F5/8 type A 2"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 178 |
| Details | Domain: {"description":"Plastocyanin-like 3"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 148 |
| Details | Domain: {"description":"Plastocyanin-like 4"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 329 |
| Details | Domain: {"description":"F5/8 type A 3"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 173 |
| Details | Domain: {"description":"Plastocyanin-like 5"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 146 |
| Details | Domain: {"description":"Plastocyanin-like 6"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 154 |
| Details | Domain: {"description":"F5/8 type C 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00081","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 155 |
| Details | Domain: {"description":"F5/8 type C 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00081","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 2 |
| Details | Site: {"description":"Cleavage; by activated protein C","evidences":[{"source":"PubMed","id":"7989361","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 1 |
| Details | Site: {"description":"Cleavage; by thrombin","evidences":[{"source":"PubMed","id":"3110773","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI16 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Sulfotyrosine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI17 |
| Number of Residues | 9 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI18 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16263699","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI19 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
