P14448 · FIBA_CHICK

  • Protein
    Fibrinogen alpha chain
  • Gene
    FGA
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

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.

1741100200300400500600700
TypeIDPosition(s)Description
Site33-34Cleavage; by thrombin; to release fibrinopeptide A
Binding site666Ca2+ (UniProtKB | ChEBI)
Binding site668Ca2+ (UniProtKB | ChEBI)
Binding site670Ca2+ (UniProtKB | ChEBI)
Binding site672Ca2+ (UniProtKB | ChEBI)

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentfibrinogen complex
Molecular Functionmetal ion binding
Molecular Functionprotein-macromolecule adaptor activity
Molecular Functionsignaling receptor binding
Biological Processblood coagulation, common pathway
Biological Processfibrinolysis
Biological Processplatelet aggregation
Biological Processpositive regulation of heterotypic cell-cell adhesion
Biological Processprotein polymerization

Keywords

Names & Taxonomy

Protein names

Gene names

    • Name
      FGA

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Archelosauria > Archosauria > Dinosauria > Saurischia > Theropoda > Coelurosauria > Aves > Neognathae > Galloanserae > Galliformes > Phasianidae > Phasianinae > Gallus

Accessions

  • Primary accession
    P14448

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for signal, modified residue, peptide, chain, disulfide bond.

TypeIDPosition(s)Description
Signal1-18
Modified residue19Pyrrolidone carboxylic acid
PeptidePRO_000000904619-33Fibrinopeptide A
ChainPRO_000000904734-741Fibrinogen alpha chain
Disulfide bond46Interchain (with alpha chain)
Disulfide bond55Interchain (with beta chain)
Disulfide bond64Interchain (with gamma chain)
Disulfide bond68Interchain (with beta chain)
Disulfide bond180Interchain (with gamma chain)
Disulfide bond184Interchain (with beta chain)
Disulfide bond310↔341
Disulfide bond674↔687

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

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

Family & Domains

Features

Showing features for coiled coil, region, compositional bias, domain.

TypeIDPosition(s)Description
Coiled coil67-506
Region270-307Disordered
Compositional bias280-307Polar residues
Compositional bias381-401Polar residues
Region381-510Disordered
Compositional bias432-477Polar residues
Domain498-739Fibrinogen C-terminal

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

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete
  • Sequence processing
    The 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.

  • Name
    1
  • Synonyms
    Alpha-E
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Length
    741
  • Mass (Da)
    82,438
  • Last updated
    1996-10-01 v4
  • Checksum
    A09F5F4F186DE3A6
MIPVTILCVLLCLNLAWAQDGKTTFEKEGGGGRGPRILENMHESSCKYEKNWPICVDDDWGTKCPSCCRMQGIIDDTDQNYSQRIDNIRQQLADSQNKYKTSNRVIVETINILKPGLEGAQQLDENYGHVSTELRRRIVTLKQRVATQVNRIKALQNSIQEQVVEMKRLEVDIDIKIRACKGSCARSFDYQVDKEGYDNIQKHLTQASSIDMHPDFQTTTLSTLKMRPLKDSNVPEHFKLKPSPEMQAMSAFNNIKQMQVVLERPETDHVAEARGDSSPSHTGKLITSSHRRESPSLVDKTSSASSVHRCTRTVTKKVISGPDGPREEIVEKMVSSDGSDCSHLQGGREGSTYHFSGTGDFHKLDRLLPDLESFFTHDSVSTSSRHSIGSSTSSHVTGAGSSHLGTGGKDKFTDLGEEEEDDFGGLQPSGFAAGSASHSKTVLTSSSSSFNKGGSTFETKSLKTRETSEQLGGVQHDQSAEDTPDFKARSFRPAAMSTRRSYNGKDCDDIRQKHTSGAKSGIFKIKPEGSNKVLSVYCDQETTLGGWLLIQQRMDGSVNFNRTWQDYRRGFGSVDGKGQGELWLGNENIHLLTQNDTLLRVELEDWDGNAAYAEYIVQVGTEAEGYALTVSSYEGTAGDALVAGWLEEGSEYTSHAQMQFSTFDRDQDHWEESCAEVYGGGWWYNSCQAANLNGIYYPGGHYDPRYNVPYEIENGVVWIPFRASDYSLKVVRMKIRPLETL

P14448-2

Features

Showing features for compositional bias, alternative sequence.

TypeIDPosition(s)Description
Compositional bias280-307Polar residues
Compositional bias381-401Polar residues
Compositional bias432-477Polar residues
Alternative sequenceVSP_001535506-509in isoform 2
Alternative sequenceVSP_001536510-741in isoform 2

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

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