A0A0D9R054 · A0A0D9R054_CHLSB

Function

function

Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C. Functions in blood homeostasis, inflammation and wound healing. Thrombin triggers the production of pro-inflammatory cytokines, such as MCP-1/CCL2 and IL8/CXCL8, in endothelial cells.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

Catalytic activity

  • Selective cleavage of Arg-|-Gly bonds in fibrinogen to form fibrin and release fibrinopeptides A and B.
    EC:3.4.21.5 (UniProtKB | ENZYME | Rhea)

Features

Showing features for site.

159650100150200250300350400450500550
TypeIDPosition(s)Description
Site206-207Cleavage; by thrombin
Site335-336Cleavage; by factor Xa
Site371-372Cleavage; by factor Xa

GO annotations

AspectTerm
Cellular Componentcollagen-containing extracellular matrix
Cellular Componentendoplasmic reticulum lumen
Cellular Componentexternal side of plasma membrane
Cellular Componentextracellular space
Molecular Functioncalcium ion binding
Molecular Functionheparin binding
Molecular Functionlipopolysaccharide binding
Molecular Functionreceptor ligand activity
Molecular Functionserine-type endopeptidase activity
Molecular Functionthrombospondin receptor activity
Biological Processacute-phase response
Biological Processantimicrobial humoral immune response mediated by antimicrobial peptide
Biological Processcell surface receptor signaling pathway
Biological Processcytolysis by host of symbiont cells
Biological Processfibrinolysis
Biological ProcessG protein-coupled receptor signaling pathway
Biological Processligand-gated ion channel signaling pathway
Biological Processnegative regulation of astrocyte differentiation
Biological Processnegative regulation of cytokine production involved in inflammatory response
Biological Processnegative regulation of proteolysis
Biological Processneutrophil-mediated killing of gram-negative bacterium
Biological Processplatelet activation
Biological Processpositive regulation of blood coagulation
Biological Processpositive regulation of cell growth
Biological Processpositive regulation of cell population proliferation
Biological Processpositive regulation of collagen biosynthetic process
Biological Processpositive regulation of insulin secretion
Biological Processpositive regulation of lipid kinase activity
Biological Processpositive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
Biological Processpositive regulation of phospholipase C-activating G protein-coupled receptor signaling pathway
Biological Processpositive regulation of protein localization to nucleus
Biological Processpositive regulation of protein phosphorylation
Biological Processpositive regulation of reactive oxygen species metabolic process
Biological Processpositive regulation of release of sequestered calcium ion into cytosol
Biological Processproteolysis
Biological Processregulation of cell shape
Biological Processregulation of cytosolic calcium ion concentration

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Prothrombin
  • EC number
  • Alternative names
    • Coagulation factor II

Gene names

    • Name
      F2

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Cercopithecidae > Cercopithecinae > Chlorocebus

Accessions

  • Primary accession
    A0A0D9R054

Proteomes

PTM/Processing

Features

Showing features for signal, chain, disulfide bond, glycosylation.

Type
IDPosition(s)Description
Signal1-24
ChainPRO_500234433025-596Prothrombin
Disulfide bond68↔73
Disulfide bond98↔111
Disulfide bond116↔194
Glycosylation129N-linked (GlcNAc...) (complex) asparagine
Disulfide bond137↔177
Glycosylation151N-linked (GlcNAc...) (complex) asparagine
Disulfide bond165↔189
Disulfide bond221↔299
Disulfide bond242↔282
Disulfide bond270↔294
Disulfide bond399↔415
Glycosylation424N-linked (GlcNAc...) (complex) asparagine
Disulfide bond510↔524
Disulfide bond538↔568

Keywords

PTM databases

Expression

Gene expression databases

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain51-97Gla
Domain115-194Kringle
Domain220-299Kringle
Domain372-592Peptidase S1

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    596
  • Mass (Da)
    66,622
  • Last updated
    2015-05-27 v1
  • MD5 Checksum
    BBC186D4313EF3C1DB04884285A807B8
MAHVRGLQLPGCLALAALCSLVHSQHVFLAPPQVFLAPQQALSLLQRVRRANSGFVEELRKGNLERECVEETCSYEEAFEALESSTATDAFWAKYTACETARTSRDTLAACLEGNCAEGLGTNYRGHVNITRSGIECQLWRSRYPHKPEINSTTHPGADLQENFCRNPDGSTTGPWCYTTDPTVRREECSIPVCGQDQVTVAMTPRSRGSSVTLSPPSEECVPDRGRQYQGRLAVTTHGLPCLAWASAQAKALSKHQDFDSAVQLVENFCRNPDGDEEGVWCYVAGKPGDFEYCDLNYCEEAVDEETGDGLGEDPDRAIEGRTATSEYQTFFDPRTFGLGEADCGLRPLFEKKSLEDKTEGELLESYIDGRIVEGWDAEIGMSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPWDKNFTENDLLVRIGKHSRTRYERNIEKISMLEKIYIHPRETAASLFQAGYKGRVAGWGNLKETWTANVGKVQPSVLQVVNLPIVERSVCKDSTRIRITDNMFCAGYKPGEGKRGDACEGDSGGPFVMKNPLNKRWYQMGIVSWGEGCDRDGKYGFYTHVFRLKKWIQKVIDQFGD

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AQIB01081125
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AQIB01081126
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AQIB01081127
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AQIB01081128
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AQIB01081129
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AQIB01081130
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.

Genome annotation databases

Similar Proteins

Disclaimer

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