Reviewed,
UniProtKB/Swiss-Prot P14477 (FIBB_PIG)
Last modified
June 16, 2009.
Version 44.
History...
Clusters with 100%,
90%,
50% identity |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: Fibrinogen beta chain Cleaved into the following chain: 1- Recommended name: Fibrinopeptide B | ||
| Gene names |
| ||
| Organism | Sus scrofa (Pig) | ||
| Taxonomic identifier | 9823 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus |
Protein attributes
| Sequence length | 19 AA. |
| Sequence status | Fragment. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Fibrinogen has a double function: yielding monomers that polymerize into fibrin and acting as a cofactor in platelet aggregation. |
| Subunit structure | Heterohexamer; disulfide linked. Contains 2 sets of 3 non-identical chains (alpha, beta and gamma). The 2 heterotrimers are in head to head conformation with the N-termini in a small central domain By similarity. |
| Subcellular location | |
| Domain | A long coiled coil structure formed by 3 polypeptide chains connects the central nodule to the C-terminal domains (distal nodules). The long C-terminal ends of the alpha chains fold back, contributing a fourth strand to the coiled coil structure. |
| Post-translational modification | Conversion of fibrinogen to fibrin is triggered by thrombin, which cleaves fibrinopeptides A and B from alpha and beta chains, and thus exposes the N-terminal polymerization sites responsible for the formation of the soft clot. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Blood coagulation |
| Cellular component | Secreted |
| Domain | Coiled coil |
| PTM | Disulfide bond Sulfation |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | blood coagulation Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
References
| [1] | "Studies on fibrinopeptides from mammals." Blombaeck B., Blombaeck M., Grondahl N.J. Acta Chem. Scand. 19:1789-1791(1965) Cited for: PROTEIN SEQUENCE. |
Cross-references
3D structure databases | |
|---|---|
| ModBase | Search... |
Phylogenomic databases | |
| HOVERGEN | P14477. |
Family and domain databases | |
| InterPro | IPR002181. Fibrinogen_a/b/g_C. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | FIBB_PIG | ||||||||
| Accession | Primary (citable) accession number: P14477 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

Clusters with


