Reviewed, UniProtKB/Swiss-Prot P16296 (FA9_RAT)

Names and origin

Protein names

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

Gene names

Name:	F9
Synonyms:	Cf9

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	282 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 direct assay. Source: RGD 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 – ›282	›282	Coagulation factor IX		PRO_0000088685
Regions
	Domain	56 – ›282	›227	Peptidase S1
Sites
	Active site	96	1	Charge relay system
	Active site	144	1	Charge relay system
	Active site	240	1	Charge relay system
Amino acid modifications
	Glycosylation	25	1	N-linked (GlcNAc...) Potential
	Glycosylation	36	1	N-linked (GlcNAc...) Potential
	Glycosylation	42	1	N-linked (GlcNAc...) Potential
	Glycosylation	135	1	N-linked (GlcNAc...) Potential
	Disulfide bond	81 ↔ 97		By similarity
	Disulfide bond	211 ↔ 225		By similarity
	Disulfide bond	236 ↔ 264		By similarity
Experimental info
	Non-terminal residue	1	1
	Non-terminal residue	282	1

Sequences

	Sequence		Length	Mass (Da)
	P16296-1 [UniParc]. Last modified August 1, 1990. Version 1. Checksum: 88B37B0A4673BEC9	FASTA	282	31,447
	10 20 30 40 50 60 RVSVAYNSKK ITRAETVFSN TDYGNSTELI LDDITNSTIL DNLTENSEPI NDFTRVVGGE 70 80 90 100 110 120 NAKPGQIPWQ VILNGEIEAF CGGAIINEKW IVTAAHCLKP GDKIEVVAGE HNIDEKEDTE 130 140 150 160 170 180 QRRNVIRTIP HHQYNATINK YSHDIALLEL DKPLILNSYV TPICVANKEY TNIFLKFGSG 190 200 210 220 230 240 YVSGWGKVFN KGRQASILQY LRVPLVDRAT CLRSTKFSIY NNMFCAGYRE GGKDSCEGDS 250 260 270 280 GGPHVTEVEG TSFLTGIISW GEECAMKGKY GIYTKVSRYV NW

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	M26247 mRNA. Translation: AAA41162.1.
IPI	IPI00765267.
PIR	I84621.
UniGene	Rn.214249
3D structure databases
HSSP	HSSP built from PDB template 1RFN based on UniProtKB P00740.
SMR	P16296. Positions 56-282.
ModBase	Search...
Proteomic databases
PRIDE	P16296.
Organism-specific databases
RGD	2589. F9.
Phylogenomic databases
HOVERGEN	P16296.
Enzyme and pathway databases
BRENDA	3.4.21.22. 248.
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_RAT

Accession

Primary (citable) accession number: P16296

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	August 1, 1990
Last modified:	June 16, 2009
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)