Coagulation factor IX precursor - Homo sapiens (Human)

Sequence

>sp|P00740|FA9_HUMAN Coagulation factor IX OS=Homo sapiens GN=F9 PE=1 SV=2 MQRVNMIMAESPGLITICLLGYLLSAECTVFLDHENANKILNRPKRYNSGKLEEFVQGNL ERECMEEKCSFEEAREVFENTERTTEFWKQYVDGDQCESNPCLNGGSCKDDINSYECWCP FGFEGKNCELDVTCNIKNGRCEQFCKNSADNKVVCSCTEGYRLAENQKSCEPAVPFPCGR VSVSQTSKLTRAETVFPDVDYVNSTEAETILDNITQSTQSFNDFTRVVGGEDAKPGQFPW QVVLNGKVDAFCGGSIVNEKWIVTAAHCVETGVKITVVAGEHNIEETEHTEQKRNVIRII PHHNYNAAINKYNHDIALLELDEPLVLNSYVTPICIADKEYTNIFLKFGSGYVSGWGRVF HKGRSALVLQYLRVPLVDRATCLRSTKFTIYNNMFCAGFHEGGRDSCQGDSGGPHVTEVE GTSFLTGIISWGEECAMKGKYGIYTKVSRYVNWIKEKTKLT

Options »

Blast tips

You can enter:
• a protein or nucleotide sequence
• a valid UniProt identifier, for example:
P00750 or A4_HUMAN or UPI0000000001
More...

Identifiers

P00740

From

To

or

Database identifier mapping tips

To map identifiers to or from UniProtKB:
• enter identifiers, e.g.: 1TTA 1FNS
• select a source database, e.g.: PDB
• or select a target database, e.g.: UniProtKB
More...

Sequence length	461 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

Function	Factor IX is a vitamin K-dependent plasma protein that participates in the intrinsic pathway of blood coagulation by converting factor X to its active form in the presence of Ca(2+) ions, phospholipids, and factor VIIIa.
Catalytic activity	Selective cleavage of Arg-\|-Ile bond in factor X to form factor Xa.
Subunit structure	Heterodimer of a light chain and a heavy chain; disulfide-linked.
Subcellular location	Secreted.
Tissue specificity	Synthesized primarily in the liver and secreted in plasma.
Domain	Calcium binds to the gamma-carboxyglutamic acid (Gla) residues and, with stronger affinity, to another site, beyond the Gla domain.
Post-translational modification	Activated by factor XIa, which excises the activation peptide.
Involvement in disease	Defects in F9 are the cause of recessive X-linked hemophilia B (HEMB) [MIM:306900]; also known as Christmas disease. Mutations in position 43 (Oxford-3, San Dimas) and 46 (Cambridge) prevents cleavage of the propeptide, mutation in position 93 (Alabama) probably fails to bind to cell membranes, mutation in position 191 (Chapel-Hill) or in position 226 (Nagoya OR Hilo) prevent cleavage of the activation peptide.
Pharmaceutical use	Available under the names BeneFix (Baxter and American Home Products). Used to treat hemophilia B.
Miscellaneous	In 1952, one of the earliest researchers of the disease, Dr. R.G. Macfarlane used the patient's surname, Christmas, to refer to the disease and also to refer to the clotting factor which he called the 'Christmas Factor' At the time Stephen Christmas was a 5-year-old boy. He died in 1993 at the age of 46 from acquired immunodeficiency syndrome contracted through treatment with blood products.
Sequence similarities	Belongs to the peptidase S1 family. Contains 2 EGF-like domains. Contains 1 Gla (gamma-carboxy-glutamate) domain. Contains 1 peptidase S1 domain.

Keywords
Biological process	Blood coagulation
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Disease	Disease mutation Hemophilia
Domain	EGF-like domain Repeat Signal
Ligand	Calcium
Molecular function	Hydrolase Protease Serine protease
PTM	Cleavage on pair of basic residues Gamma-carboxyglutamic acid Glycoprotein Hydroxylation Phosphoprotein Sulfation Zymogen
Technical term	3D-structure Direct protein sequencing Pharmaceutical
Gene Ontology (GO)
Biological process	blood coagulation, extrinsic pathway Inferred from Experiment. Source: Reactome proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from direct assay. Source: HPA extracellular region Non-traceable author statement. Source: UniProtKB nucleus Inferred from direct assay. Source: HPA plasma membrane Inferred from Experiment. Source: Reactome
Molecular function	calcium ion binding Inferred from electronic annotation. Source: InterPro serine-type endopeptidase activity Ref.46 Traceable author statement. Source: ProtInc
Complete GO annotation...

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Keywords

Gene Ontology (GO)

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations