Q5FVW1 · Q5FVW1_XENTR

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 active site.

160750100150200250300350400450500550600
TypeIDPosition(s)Description
Active site392Charge relay system
Active site448Charge relay system
Active site553Charge relay system

GO annotations

AspectTerm
Cellular Componentextracellular region
Molecular Functioncalcium ion binding
Molecular Functionserine-type endopeptidase activity
Biological Processacute-phase response
Biological Processblood coagulation
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

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

Gene names

    • Name
      f2

Organism names

Accessions

  • Primary accession
    Q5FVW1

Proteomes

Organism-specific databases

Subcellular Location

PTM/Processing

Features

Showing features for signal, chain, disulfide bond.

Type
IDPosition(s)Description
Signal1-22
ChainPRO_503320617123-607Prothrombin
Disulfide bond58↔63
Disulfide bond88↔101
Disulfide bond108↔184
Disulfide bond129↔167
Disulfide bond155↔179
Disulfide bond208↔285
Disulfide bond229↔268
Disulfide bond256↔280
Disulfide bond322↔468Interchain (between light and heavy chains)
Disulfide bond377↔393
Disulfide bond521↔535
Disulfide bond549↔579

Keywords

Proteomic databases

Expression

Gene expression databases

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain41-87Gla
Domain107-184Kringle
Domain207-285Kringle
Domain350-603Peptidase S1

Sequence similarities

Belongs to the peptidase S1 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    607
  • Mass (Da)
    69,503
  • Last updated
    2005-03-01 v1
  • Checksum
    681C15339E41947A
MQPRDHIIGGLLLAATLSLVHCQNVFLNSKEAMSVLKRSRRANSYLEEIRQGNMERECIEEICSYEELREIKESKVETDIFWAKYKDCEPEKKTRNDREDCLKGTSTCAEGTGTHYRGNVSVTRSGRECQYWISNYPHKTKFNPTTNPSLVKNYCRNPNDNPTGPWCYTKDPQKQWEECVIPLCGTNKTTVEPLIQKVPDQSVKKEPCEREFGLHYEGKLAVTISGLPCLPWDSPSVQQHSRKDFIKEVKLQENYCRNPDNDGEGLWCYVSHPNLTYDYCPMNYCDSPIDEEVLNRPAGRTTTEEHQTFFDEKSFGSGEAVCGLRPLFEQKSVEDKGEKELLESYMQGRIVKGETAEPGSAPWQVMLFKKSPQELLCGASLLSDRWVLSAAHCIFYPPWDKNYTTDDILVRIGKHFRTKYERATERIAQLERIIVHPKYNWKENLDRDIALIQLKRPVAFSNYIHPVCLPTKDTVVKLLAAGYKGRVTGWGNLQETWTSGAQNLPQALQQINLPIVDQETCKSSTNIKVTDNMFCAGYNPEDSKRGDACEGDSGGPFVMKDPDTGRWVQLGIVSWGEGCDRDNKYGFYVHVHRMRKWIMKTVEKFGS

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BC089747
EMBL· GenBank· DDBJ
AAH89747.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
Help