Reviewed,
UniProtKB/Swiss-Prot P12259 (FA5_HUMAN)
Last modified
November 25, 2008.
Version 121.
History...
Clusters with 100%,
90%,
50% identity |
Documents (7) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Coagulation factor V Alternative name(s): Activated protein C cofactor Cleaved into the following 2 chains: 1- Recommended name: Coagulation factor V heavy chain 2- Recommended name: Coagulation factor V light chain | ||
| Gene names |
| ||
| Organism | Homo sapiens (Human) | ||
| Taxonomic identifier | 9606 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 2224 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Coagulation factor V is a cofactor that participates with factor Xa to activate prothrombin to thrombin. |
| Subunit structure | Factor Va is composed of a heavy chain and a light chain, non-covalently bound. The interaction between the two chains is calcium-dependent. |
| Subcellular location | SecretedBy similarity. |
| Domain | Domain B contains 35 x 9 AA tandem repeats, and 2 x 17 AA repeats. |
| Post-translational modification | Thrombin activates factor V proteolytically to the active cofactor, factor Va (formation of a heavy chain at the N-terminus and a light chain at the C-terminus). Sulfation is required for efficient thrombin cleavage and activation and for full procoagulant activity. |
| Involvement in disease | Defects in F5 are the cause of factor V deficiency (FA5D) [MIM:227400]; also known as Owren parahemophilia. It is an hemorrhagic diastesis. Defects in F5 are the cause of thrombophilia due to activated protein C resistance (THR-APCR) [MIM:188055]. THR-APCR is a hemostatic disorder due to defective degradation of factor Va by activated protein C. It is characterized by a poor anticoagulant response to activated protein C resulting in tendency to thrombosis. Defects in F5 are a cause of susceptibility to Budd-Chiari syndrome [MIM:600880]. Budd-Chiari syndrome is a spectrum of disease states, including anatomic abnormalities and hypercoagulable disorders, resulting in hepatic venous outflow occlusion. Clinical manifestations observed in the majority of patients include hepatomegaly, right upper quadrant pain, and abdominal ascites. Defects in F5 may be a cause of susceptibility to ischemic stroke [MIM:601367]; also known as cerebrovascular accident or cerebral infarction. A stroke is an acute neurologic event leading to death of neural tissue of the brain and resulting in loss of motor, sensory and/or cognitive function. Ischemic strokes, resulting from vascular occlusion, is considered to be a highly complex disease consisting of a group of heterogeneous disorders with multiple genetic and environmental risk factors. |
| Sequence similarities | Belongs to the multicopper oxidase family. Contains 3 F5/8 type A domains. Contains 2 F5/8 type C domains. Contains 6 plastocyanin-like domains. |
Ontologies
Keywords | |
|---|---|
| Biological process | Blood coagulation |
| Cellular component | Secreted |
| Coding sequence diversity | Polymorphism |
| Disease | Disease mutation Thrombophilia |
| Domain | Repeat Signal |
| Ligand | Calcium Copper Metal-binding |
| PTM | Glycoprotein Phosphoprotein Sulfation Zymogen |
| Technical term | 3D-structure |
Gene Ontology (GO) | |
| Biological process | blood coagulation Traceable author statement. Source: ProtInc cell adhesionInferred from electronic annotation. Source: InterPro |
| Cellular component | extracellular region Non-traceable author statement. Source: UniProtKB plasma membraneInferred from Experiment. Source: Reactome platelet alpha granule lumenInferred from Experiment. Source: Reactome |
| Molecular function | calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW copper ion bindingInferred from electronic annotation. Source: InterPro oxidoreductase activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||
Molecule processing | ||||||||||
|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 28 | 28 | ||||||||
| Chain | 29 – 2224 | 2196 | Coagulation factor V | PRO_0000002978 | ||||||
| Chain | 29 – 737 | 709 | Coagulation factor V heavy chain | PRO_0000002979 | ||||||
| Propeptide | 738 – 1573 | 836 | Activation peptide (connecting region) | PRO_0000002980 | ||||||
| Chain | 1574 – 2224 | 651 | Coagulation factor V light chain | PRO_0000002981 | ||||||
Regions | ||||||||||
| Domain | 30 – 329 | 300 | F5/8 type A 1 | |||||||
| Domain | 30 – 193 | 164 | Plastocyanin-like 1 | |||||||
| Domain | 203 – 329 | 127 | Plastocyanin-like 2 | |||||||
| Domain | 348 – 684 | 337 | F5/8 type A 2 | |||||||
| Domain | 348 – 526 | 179 | Plastocyanin-like 3 | |||||||
| Domain | 536 – 684 | 149 | Plastocyanin-like 4 | |||||||
| Repeat | 895 – 911 | 17 | 1-1 | |||||||
| Repeat | 912 – 928 | 17 | 1-2 | |||||||
| Repeat | 1185 – 1193 | 9 | 2-1 | |||||||
| Repeat | 1194 – 1202 | 9 | 2-2 | |||||||
| Repeat | 1203 – 1211 | 9 | 2-3 | |||||||
| Repeat | 1212 – 1220 | 9 | 2-4 | |||||||
| Repeat | 1221 – 1229 | 9 | 2-5 | |||||||
| Repeat | 1230 – 1238 | 9 | 2-6 | |||||||
| Repeat | 1239 – 1247 | 9 | 2-7 | |||||||
| Repeat | 1248 – 1256 | 9 | 2-8 | |||||||
| Repeat | 1257 – 1265 | 9 | 2-9 | |||||||
| Repeat | 1266 – 1274 | 9 | 2-10 | |||||||
| Repeat | 1275 – 1283 | 9 | 2-11 | |||||||
| Repeat | 1284 – 1292 | 9 | 2-12 | |||||||
| Repeat | 1293 – 1301 | 9 | 2-13 | |||||||
| Repeat | 1302 – 1310 | 9 | 2-14 | |||||||
| Repeat | 1311 – 1319 | 9 | 2-15 | |||||||
| Repeat | 1320 – 1328 | 9 | 2-16 | |||||||
| Repeat | 1329 – 1337 | 9 | 2-17 | |||||||
| Repeat | 1338 – 1346 | 9 | 2-18 | |||||||
| Repeat | 1347 – 1355 | 9 | 2-19 | |||||||
| Repeat | 1356 – 1364 | 9 | 2-20 | |||||||
| Repeat | 1365 – 1373 | 9 | 2-21 | |||||||
| Repeat | 1374 – 1382 | 9 | 2-22 | |||||||
| Repeat | 1383 – 1391 | 9 | 2-23 | |||||||
| Repeat | 1392 – 1400 | 9 | 2-24 | |||||||
| Repeat | 1401 – 1409 | 9 | 2-25 | |||||||
| Repeat | 1410 – 1418 | 9 | 2-26 | |||||||
| Repeat | 1419 – 1427 | 9 | 2-27 | |||||||
| Repeat | 1428 – 1436 | 9 | 2-28 | |||||||
| Repeat | 1437 – 1445 | 9 | 2-29 | |||||||
| Repeat | 1446 – 1454 | 9 | 2-30 | |||||||
| Repeat | 1455 – 1463 | 9 | 2-31 | |||||||
| Repeat | 1464 – 1472 | 9 | 2-32 | |||||||
| Repeat | 1473 – 1481 | 9 | 2-33 | |||||||
| Repeat | 1482 – 1490 | 9 | 2-34 | |||||||
| Repeat | 1493 – 1501 | 9 | 2-35 | |||||||
| Domain | 1578 – 1907 | 330 | F5/8 type A 3 | |||||||
| Domain | 1578 – 1751 | 174 | Plastocyanin-like 5 | |||||||
| Domain | 1761 – 1907 | 147 | Plastocyanin-like 6 | |||||||
| Domain | 1907 – 2061 | 155 | F5/8 type C 1 | |||||||
| Domain | 2066 – 2221 | 156 | F5/8 type C 2 | |||||||
| Region | 692 – 1573 | 882 | B | |||||||
| Region | 895 – 928 | 34 | 2 X 17 AA tandem repeats | |||||||
| Region | 1185 – 1501 | 317 | 35 X 9 AA approximate tandem repeats of [TNP]-L-S-P-D-L-S-Q-T | |||||||
Sites | ||||||||||
| Metal binding | 139 | 1 | Calcium By similarity | |||||||
| Metal binding | 140 | 1 | Calcium By similarity | |||||||
| Metal binding | 1843 | 1 | Copper By similarity | |||||||
| Metal binding | 1845 | 1 | Copper By similarity | |||||||
| Site | 737 – 738 | 2 | Cleavage; by thrombin | |||||||
| Site | 1046 – 1047 | 2 | Cleavage; by thrombin | |||||||
| Site | 1573 – 1574 | 2 | Cleavage; by thrombin | |||||||
Amino acid modifications | ||||||||||
| Modified residue | 693 | 1 | Sulfotyrosine Potential | |||||||
| Modified residue | 724 | 1 | Sulfotyrosine Potential | |||||||
| Modified residue | 726 | 1 | Sulfotyrosine Potential | |||||||
| Modified residue | 1150 | 1 | Phosphoserine | |||||||
| Modified residue | 1522 | 1 | Sulfotyrosine Potential | |||||||
| Modified residue | 1538 | 1 | Sulfotyrosine Potential | |||||||
| Modified residue | 1543 | 1 | Sulfotyrosine Potential | |||||||
| Modified residue | 1593 | 1 | Sulfotyrosine Potential | |||||||
| Glycosylation | 51 | 1 | N-linked (GlcNAc...) Potential | |||||||
| Glycosylation | 55 | 1 | N-linked (GlcNAc...) Potential | |||||||
| Glycosylation | 239 | 1 | N-linked (GlcNAc...) Potential | |||||||
| Glycosylation | 297 | 1 | N-linked (GlcNAc...) | |||||||
| Glycosylation | 382 | 1 | N-linked (GlcNAc...) Potential | |||||||
| Glycosylation | 460 | 1 | N-linked (GlcNAc...) | |||||||
| Glycosylation | 468 | 1 | N-linked (GlcNAc...) Potential | |||||||
| Glycosylation | 554 | 1 | N-linked (GlcNAc...) Potential | |||||||
| Glycosylation | 741 | 1 | N-linked (GlcNAc...) Potential | |||||||
| Glycosylation | 752 | 1 | N-linked (GlcNAc...) Potential | |||||||
| Glycosylation | 760 | 1 | N-linked (GlcNAc...) Potential | |||||||
| Glycosylation | 776 | 1 | N-linked (GlcNAc...) Potential | |||||||
| Glycosylation | 782 | 1 | N-linked (GlcNAc...) Potential | |||||||
| Glycosylation | 821 | 1 | N-linked (GlcNAc...) | |||||||
| Glycosylation | 938 | 1 | N-linked (GlcNAc...) Potential | |||||||
| Glycosylation | 977 | 1 | N-linked (GlcNAc...) | |||||||
| Glycosylation | 1074 | 1 | N-linked (GlcNAc...) Potential | |||||||
| Glycosylation | 1083 | 1 | N-linked (GlcNAc...) Potential | |||||||
| Glycosylation | 1103 | 1 | N-linked (GlcNAc...) Potential | |||||||
| Glycosylation | 1106 | 1 | N-linked (GlcNAc...) Potential | |||||||
| Glycosylation | 1479 | 1 | N-linked (GlcNAc...) Potential | |||||||
| Glycosylation | 1499 | 1 | N-linked (GlcNAc...) Potential | |||||||
| Glycosylation | 1559 | 1 | N-linked (GlcNAc...) | |||||||
| Glycosylation | 1703 | 1 | N-linked (GlcNAc...) Potential | |||||||
| Glycosylation | 2010 | 1 | N-linked (GlcNAc...) Potential | |||||||
| Glycosylation | 2209 | 1 | N-linked (GlcNAc...) Potential | |||||||
| Disulfide bond | 167 ↔ 193 | By similarity | ||||||||

Clusters with