P14448 (FIBA_CHICK) Reviewed, UniProtKB/Swiss-Prot
Last modified
September 21, 2011.
Version 95.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Fibrinogen alpha chain Cleaved into the following 2 chains: | ||
| Gene names |
| ||
| Organism | Gallus gallus (Chicken) | ||
| Taxonomic identifier | 9031 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus |
Protein attributes
| Sequence length | 741 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 | 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. The soft clot is converted into the hard clot by factor XIIIA which catalyzes the epsilon-(gamma-glutamyl)lysine cross-linking between gamma chains (stronger) and between alpha chains (weaker) of different monomers. Forms F13A-mediated cross-links between a glutamine and the epsilon-amino group of a lysine residue, forming fibronectin-fibrinogen heteropolymers. |
| Sequence similarities | Contains 1 fibrinogen C-terminal domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Blood coagulation |
| Cellular component | Secreted |
| Coding sequence diversity | Alternative splicing |
| Domain | Coiled coil Signal |
| PTM | Disulfide bond Pyrrolidone carboxylic acid |
| Technical term | 3D-structure Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Biological process | platelet activation Inferred from electronic annotation. Source: InterPro protein polymerizationInferred from electronic annotation. Source: InterPro signal transductionInferred from electronic annotation. Source: InterPro |
| Cellular component | fibrinogen complex Inferred from electronic annotation. Source: InterPro |
| Molecular function | protein binding, bridging Inferred from electronic annotation. Source: InterPro receptor bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Alternative products
| This entry describes 2 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: P14448-1) Also known as: Alpha-E; This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Isoform 2 (identifier: P14448-2) Also known as: Alpha; The sequence of this isoform differs from the canonical sequence as follows: 506-509: DCDD → GTQK 510-741: Missing. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||
Molecule processing | ||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 18 | 18 | Ref.3 | |||||||||||||||||||
| Peptide | 19 – 33 | 15 | Fibrinopeptide A Ref.3 | PRO_0000009046 | ||||||||||||||||||
| Chain | 34 – 741 | 708 | Fibrinogen alpha chain | PRO_0000009047 | ||||||||||||||||||
Regions | ||||||||||||||||||||||
| Domain | 498 – 739 | 242 | Fibrinogen C-terminal | |||||||||||||||||||
| Coiled coil | 67 – 506 | 440 | ||||||||||||||||||||
Sites | ||||||||||||||||||||||
| Site | 33 – 34 | 2 | Cleavage; by thrombin; to release fibrinopeptide A | |||||||||||||||||||
Amino acid modifications | ||||||||||||||||||||||
| Modified residue | 19 | 1 | Pyrrolidone carboxylic acid | |||||||||||||||||||
| Disulfide bond | 46 | Interchain (with alpha chain) | ||||||||||||||||||||
| Disulfide bond | 55 | Interchain (with beta chain) | ||||||||||||||||||||
| Disulfide bond | 64 | Interchain (with gamma chain) | ||||||||||||||||||||
| Disulfide bond | 68 | Interchain (with beta chain) | ||||||||||||||||||||
| Disulfide bond | 180 | Interchain (with gamma chain) | ||||||||||||||||||||
| Disulfide bond | 184 | Interchain (with beta chain) | ||||||||||||||||||||
| Disulfide bond | 310 ↔ 341 | By similarity | ||||||||||||||||||||
Natural variations | ||||||||||||||||||||||
| Alternative sequence | 506 – 509 | 4 | DCDD → GTQK in isoform 2. | VSP_001535 | ||||||||||||||||||
| Alternative sequence | 510 – 741 | 232 | Missing in isoform 2. | VSP_001536 | ||||||||||||||||||
Secondary structure | ||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||
| Turn | 60 – 62 | 3 | ||||||||||||||||||||
| Helix | 70 – 97 | 28 | ||||||||||||||||||||
| Turn | 98 – 100 | 3 | ||||||||||||||||||||
| Helix | 101 – 178 | 78 | ||||||||||||||||||||
| Turn | 179 – 183 | 5 | ||||||||||||||||||||
| Beta strand | 184 – 186 | 3 | ||||||||||||||||||||
| Turn | 194 – 197 | 4 | ||||||||||||||||||||
| Helix | 198 – 207 | 10 | ||||||||||||||||||||
| Turn | 232 – 235 | 4 | ||||||||||||||||||||
Sequences
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References
| [1] | Greininger G. Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE OF 1-4. |
| [2] | "Bipartite mRNA for chicken alpha-fibrinogen potentially encodes an amino acid sequence homologous to beta- and gamma-fibrinogens." Weissbach L., Grieninger G. Proc. Natl. Acad. Sci. U.S.A. 87:5198-5202(1990) [PubMed: 2367530] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 5-741. |
| [3] | "Amino acid sequence of chicken fibrinopeptide A." Takagi T., Finlayson J.S., Iwanaga S. Biochim. Biophys. Acta 534:161-164(1978) [PubMed: 656462] [Abstract] Cited for: PROTEIN SEQUENCE OF 19-33. |
| [4] | "Crystal structure of native chicken fibrinogen at 5.5-A resolution." Yang Z., Mochalkin I., Veerapandian L., Riley M., Doolittle R.F. Proc. Natl. Acad. Sci. U.S.A. 97:3907-3912(2000) [PubMed: 10737772] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (5.5 ANGSTROMS) OF 19-509. |
| [5] | "Crystal structure of native chicken fibrinogen at 2.7 A resolution." Yang Z., Kollman J.M., Pandi L., Doolittle R.F. Biochemistry 40:12515-12523(2001) [PubMed: 11601975] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 19-509. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | U20803 U20802 Genomic DNA. Translation: AAB60686.1.U20803 U20802 Genomic DNA. Translation: AAB60685.1.M34096 mRNA. Translation: AAA99306.1. M34096 mRNA. Translation: AAA99307.1. | ||||||||||||||||||
| IPI | IPI00571323. IPI00589899. | ||||||||||||||||||
| UniGene | Gga.34280. | ||||||||||||||||||
3D structure databases | |||||||||||||||||||
| PDBe RCSB PDB PDBj |
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| ProteinModelPortal | P14448. | ||||||||||||||||||
| SMR | P14448. Positions 45-238, 545-740. | ||||||||||||||||||
| DisProt | DP00233. | ||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||
| STRING | P14448. | ||||||||||||||||||
Protocols and materials databases | |||||||||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||
| eggNOG | veNOG06112. | ||||||||||||||||||
| GeneTree | ENSGT00600000084399. | ||||||||||||||||||
| HOGENOM | HBG716848. | ||||||||||||||||||
| HOVERGEN | HBG005668. | ||||||||||||||||||
| InParanoid | P14448. | ||||||||||||||||||
| OrthoDB | EOG4XPQFB. | ||||||||||||||||||
Family and domain databases | |||||||||||||||||||
| InterPro | IPR002181. Fibrinogen_a/b/g_C. IPR014716. Fibrinogen_a/b/g_C_1. IPR014715. Fibrinogen_a/b/g_C_2. IPR012290. Fibrinogen_a/b/g_coil_dom. IPR021996. Fibrinogen_aC. IPR020837. Fibrinogen_CS. [Graphical view] | ||||||||||||||||||
| Gene3D | G3DSA:3.90.215.10. Fibrinogen_a/b/g_C_1. 1 hit. G3DSA:4.10.530.10. Fibrinogen_a/b/g_C_2. 1 hit. G3DSA:1.20.5.50. Fibrinogen_a/b/g_coil. 1 hit. | ||||||||||||||||||
| Pfam | PF08702. Fib_alpha. 1 hit. PF12160. Fibrinogen_aC. 1 hit. PF00147. Fibrinogen_C. 1 hit. [Graphical view] | ||||||||||||||||||
| SMART | SM00186. FBG. 1 hit. [Graphical view] | ||||||||||||||||||
| SUPFAM | SSF56496. Fibrinogen_a/b/g_C. 1 hit. | ||||||||||||||||||
| PROSITE | PS00514. FIBRINOGEN_C_1. 1 hit. PS51406. FIBRINOGEN_C_2. 1 hit. [Graphical view] | ||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||
Entry information
| Entry name | FIBA_CHICK | ||||||||
| Accession | Primary (citable) accession number: P14448 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with