P14448 · FIBA_CHICK
- ProteinFibrinogen alpha chain
- GeneFGA
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids741 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Cleaved by the protease thrombin to yield monomers which, together with fibrinogen beta (FGB) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a major function in hemostasis as one of the primary components of blood clots.
Features
Showing features for site, binding site.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | fibrinogen complex | |
Molecular Function | metal ion binding | |
Molecular Function | protein-macromolecule adaptor activity | |
Molecular Function | signaling receptor binding | |
Biological Process | blood coagulation, common pathway | |
Biological Process | fibrinolysis | |
Biological Process | platelet aggregation | |
Biological Process | positive regulation of heterotypic cell-cell adhesion | |
Biological Process | protein polymerization |
Keywords
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameFibrinogen alpha chain
- Cleaved into 2 chains
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Archelosauria > Archosauria > Dinosauria > Saurischia > Theropoda > Coelurosauria > Aves > Neognathae > Galloanserae > Galliformes > Phasianidae > Phasianinae > Gallus
Accessions
- Primary accessionP14448
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for signal, modified residue, peptide, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-18 | |||||
Sequence: MIPVTILCVLLCLNLAWA | ||||||
Modified residue | 19 | Pyrrolidone carboxylic acid | ||||
Sequence: Q | ||||||
Peptide | PRO_0000009046 | 19-33 | Fibrinopeptide A | |||
Sequence: QDGKTTFEKEGGGGR | ||||||
Chain | PRO_0000009047 | 34-741 | Fibrinogen alpha chain | |||
Sequence: GPRILENMHESSCKYEKNWPICVDDDWGTKCPSCCRMQGIIDDTDQNYSQRIDNIRQQLADSQNKYKTSNRVIVETINILKPGLEGAQQLDENYGHVSTELRRRIVTLKQRVATQVNRIKALQNSIQEQVVEMKRLEVDIDIKIRACKGSCARSFDYQVDKEGYDNIQKHLTQASSIDMHPDFQTTTLSTLKMRPLKDSNVPEHFKLKPSPEMQAMSAFNNIKQMQVVLERPETDHVAEARGDSSPSHTGKLITSSHRRESPSLVDKTSSASSVHRCTRTVTKKVISGPDGPREEIVEKMVSSDGSDCSHLQGGREGSTYHFSGTGDFHKLDRLLPDLESFFTHDSVSTSSRHSIGSSTSSHVTGAGSSHLGTGGKDKFTDLGEEEEDDFGGLQPSGFAAGSASHSKTVLTSSSSSFNKGGSTFETKSLKTRETSEQLGGVQHDQSAEDTPDFKARSFRPAAMSTRRSYNGKDCDDIRQKHTSGAKSGIFKIKPEGSNKVLSVYCDQETTLGGWLLIQQRMDGSVNFNRTWQDYRRGFGSVDGKGQGELWLGNENIHLLTQNDTLLRVELEDWDGNAAYAEYIVQVGTEAEGYALTVSSYEGTAGDALVAGWLEEGSEYTSHAQMQFSTFDRDQDHWEESCAEVYGGGWWYNSCQAANLNGIYYPGGHYDPRYNVPYEIENGVVWIPFRASDYSLKVVRMKIRPLETL | ||||||
Disulfide bond | 46 | Interchain (with alpha chain) | ||||
Sequence: C | ||||||
Disulfide bond | 55 | Interchain (with beta chain) | ||||
Sequence: C | ||||||
Disulfide bond | 64 | Interchain (with gamma chain) | ||||
Sequence: C | ||||||
Disulfide bond | 68 | Interchain (with beta chain) | ||||
Sequence: C | ||||||
Disulfide bond | 180 | Interchain (with gamma chain) | ||||
Sequence: C | ||||||
Disulfide bond | 184 | Interchain (with beta chain) | ||||
Sequence: C | ||||||
Disulfide bond | 310↔341 | |||||
Sequence: CTRTVTKKVISGPDGPREEIVEKMVSSDGSDC | ||||||
Disulfide bond | 674↔687 | |||||
Sequence: CAEVYGGGWWYNSC |
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.
Keywords
- PTM
Proteomic databases
Interaction
Subunit
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.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for coiled coil, region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Coiled coil | 67-506 | |||||
Sequence: CCRMQGIIDDTDQNYSQRIDNIRQQLADSQNKYKTSNRVIVETINILKPGLEGAQQLDENYGHVSTELRRRIVTLKQRVATQVNRIKALQNSIQEQVVEMKRLEVDIDIKIRACKGSCARSFDYQVDKEGYDNIQKHLTQASSIDMHPDFQTTTLSTLKMRPLKDSNVPEHFKLKPSPEMQAMSAFNNIKQMQVVLERPETDHVAEARGDSSPSHTGKLITSSHRRESPSLVDKTSSASSVHRCTRTVTKKVISGPDGPREEIVEKMVSSDGSDCSHLQGGREGSTYHFSGTGDFHKLDRLLPDLESFFTHDSVSTSSRHSIGSSTSSHVTGAGSSHLGTGGKDKFTDLGEEEEDDFGGLQPSGFAAGSASHSKTVLTSSSSSFNKGGSTFETKSLKTRETSEQLGGVQHDQSAEDTPDFKARSFRPAAMSTRRSYNGKD | ||||||
Region | 270-307 | Disordered | ||||
Sequence: VAEARGDSSPSHTGKLITSSHRRESPSLVDKTSSASSV | ||||||
Compositional bias | 280-307 | Polar residues | ||||
Sequence: SHTGKLITSSHRRESPSLVDKTSSASSV | ||||||
Compositional bias | 381-401 | Polar residues | ||||
Sequence: STSSRHSIGSSTSSHVTGAGS | ||||||
Region | 381-510 | Disordered | ||||
Sequence: STSSRHSIGSSTSSHVTGAGSSHLGTGGKDKFTDLGEEEEDDFGGLQPSGFAAGSASHSKTVLTSSSSSFNKGGSTFETKSLKTRETSEQLGGVQHDQSAEDTPDFKARSFRPAAMSTRRSYNGKDCDDI | ||||||
Compositional bias | 432-477 | Polar residues | ||||
Sequence: AAGSASHSKTVLTSSSSSFNKGGSTFETKSLKTRETSEQLGGVQHD | ||||||
Domain | 498-739 | Fibrinogen C-terminal | ||||
Sequence: TRRSYNGKDCDDIRQKHTSGAKSGIFKIKPEGSNKVLSVYCDQETTLGGWLLIQQRMDGSVNFNRTWQDYRRGFGSVDGKGQGELWLGNENIHLLTQNDTLLRVELEDWDGNAAYAEYIVQVGTEAEGYALTVSSYEGTAGDALVAGWLEEGSEYTSHAQMQFSTFDRDQDHWEESCAEVYGGGWWYNSCQAANLNGIYYPGGHYDPRYNVPYEIENGVVWIPFRASDYSLKVVRMKIRPLE |
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.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 2 isoforms produced by Alternative splicing.
P14448-1
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.
- Name1
- SynonymsAlpha-E
- Length741
- Mass (Da)82,438
- Last updated1996-10-01 v4
- ChecksumA09F5F4F186DE3A6
P14448-2
- Name2
- SynonymsAlpha
Features
Showing features for compositional bias, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 280-307 | Polar residues | ||||
Sequence: SHTGKLITSSHRRESPSLVDKTSSASSV | ||||||
Compositional bias | 381-401 | Polar residues | ||||
Sequence: STSSRHSIGSSTSSHVTGAGS | ||||||
Compositional bias | 432-477 | Polar residues | ||||
Sequence: AAGSASHSKTVLTSSSSSFNKGGSTFETKSLKTRETSEQLGGVQHD | ||||||
Alternative sequence | VSP_001535 | 506-509 | in isoform 2 | |||
Sequence: DCDD → GTQK | ||||||
Alternative sequence | VSP_001536 | 510-741 | in isoform 2 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U20803 EMBL· GenBank· DDBJ | AAB60686.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U20799 EMBL· GenBank· DDBJ | AAB60686.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U20800 EMBL· GenBank· DDBJ | AAB60686.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U20801 EMBL· GenBank· DDBJ | AAB60686.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U20802 EMBL· GenBank· DDBJ | AAB60686.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U20803 EMBL· GenBank· DDBJ | AAB60685.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U20799 EMBL· GenBank· DDBJ | AAB60685.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U20800 EMBL· GenBank· DDBJ | AAB60685.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U20801 EMBL· GenBank· DDBJ | AAB60685.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U20802 EMBL· GenBank· DDBJ | AAB60685.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M34096 EMBL· GenBank· DDBJ | AAA99306.1 EMBL· GenBank· DDBJ | mRNA | ||
M34096 EMBL· GenBank· DDBJ | AAA99307.1 EMBL· GenBank· DDBJ | mRNA |