Reviewed, UniProtKB/Swiss-Prot P16292 (FA9_RABIT)

Names and origin

Protein names

Recommended name:
    Coagulation factor IX
    EC=3.4.21.22
Alternative name(s):
    Christmas factor

Gene names

Name:

F9

Organism

Oryctolagus cuniculus (Rabbit)

Taxonomic identifier

9986 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

Protein attributes

Sequence length	275 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

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 Ca2+ 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.
Sequence similarities	Belongs to the peptidase S1 family. Contains 1 peptidase S1 domain.

Ontologies

Keywords
Biological process	Blood coagulation
Cellular component	Secreted
Ligand	Calcium
Molecular function	Hydrolase Protease Serine protease
PTM	Disulfide bond Glycoprotein
Gene Ontology (GO)
Biological process	blood coagulation Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	‹1 – ›275	›275	Coagulation factor IX		PRO_0000088684
Regions
	Domain	49 – ›275	›227	Peptidase S1
Sites
	Active site	89	1	Charge relay system
	Active site	137	1	Charge relay system
	Active site	233	1	Charge relay system
Amino acid modifications
	Glycosylation	25	1	N-linked (GlcNAc...) Potential
	Glycosylation	35	1	N-linked (GlcNAc...) Potential
	Glycosylation	96	1	N-linked (GlcNAc...) Potential
	Glycosylation	128	1	N-linked (GlcNAc...) Potential
	Disulfide bond	74 ↔ 90		By similarity
	Disulfide bond	204 ↔ 218		By similarity
	Disulfide bond	229 ↔ 257		By similarity
Experimental info
	Non-terminal residue	1	1
	Non-terminal residue	275	1

Sequences

	Sequence		Length	Mass (Da)
	P16292-1 [UniParc]. Last modified August 1, 1990. Version 1. Checksum: FE364489AC76BE87	FASTA	275	30,777
	10 20 30 40 50 60 GVSVSHASKK ITRATTIFSN TEYENFTEAE TIRGNVTQRS QSSDDFTRIV GGENAKPGQF 70 80 90 100 110 120 PWQVLLNGKV EAFCGGSIIN EKWVVTAAHC IKPDDNITVV AGEYNIQETE NTEQKRNVIR 130 140 150 160 170 180 IIPYHKYNAT INKYNHDIAL LELDKPLTLN SYVTPICIAN REYTNIFLNF GSGYVSGWGR 190 200 210 220 230 240 VFNRGRQASI LQYLRVPFVD RATCLRSTKF TIYNNMFCAG FDVGGKDSCE GDSGGPHVTE 250 260 270 VEGTSFLTGI ISWGEECAIK GKYGVYTRVS WYVNW

References

[1]	"Direct sequencing of the activation peptide and the catalytic domain of the factor IX gene in six species." Sarkar G., Koeberl D.D., Sommer S.S. Genomics 6:133-143(1990) [PubMed: 2303254] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	M26234 mRNA. Translation: AAA31251.1.
PIR	I46712.
UniGene	Ocu.1877
3D structure databases
HSSP	HSSP built from PDB template 1PFX based on UniProtKB P16293.
SMR	P16292. Positions 49-275.
ModBase	Search...
Protein family/group databases
MEROPS	S01.214.
Phylogenomic databases
HOVERGEN	P16292.
Enzyme and pathway databases
BRENDA	3.4.21.22. 255.
Family and domain databases
InterPro	IPR018114. Peptidase_S1/S6_AS. IPR001254. Peptidase_S1_S6. IPR001314. Peptidase_S1A. [Graphical view]
Pfam	PF00089. Trypsin. 1 hit. [Graphical view]
PRINTS	PR00722. CHYMOTRYPSIN.
SMART	SM00020. Tryp_SPc. 1 hit. [Graphical view]
PROSITE	PS50240. TRYPSIN_DOM. 1 hit. PS00134. TRYPSIN_HIS. 1 hit. PS00135. TRYPSIN_SER. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FA9_RABIT

Accession

Primary (citable) accession number: P16292

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	August 1, 1990
Last modified:	June 16, 2009
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)