Reviewed, UniProtKB/Swiss-Prot Q804X6 (FA9_CHICK)

Names and origin

Protein names

Recommended name:
    Coagulation factor IX
    EC=3.4.21.22
Alternative name(s):
    Christmas factor
Cleaved into the following 2 chains:
    1- Recommended name:
            Coagulation factor IXa light chain
    2- Recommended name:
            Coagulation factor IXa heavy chain

Gene names

Name:

F9

Organism

Gallus gallus (Chicken)

Taxonomic identifier

9031 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Protein attributes

Sequence length	471 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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 By similarity.
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 By similarity.
Subcellular location	Secreted By similarity.
Domain	Calcium binds to the gamma-carboxyglutamic acid (Gla) residues and, with stronger affinity, to another site, beyond the Gla domain By similarity.
Post-translational modification	Activated by factor XIa, which excises the activation peptide By similarity. The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains By similarity.
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.

Ontologies

Keywords
Biological process	Blood coagulation
Cellular component	Secreted
Domain	EGF-like domain Repeat Signal
Ligand	Calcium
Molecular function	Hydrolase Protease Serine protease
PTM	Cleavage on pair of basic residues Disulfide bond Gamma-carboxyglutamic acid Glycoprotein Hydroxylation Phosphoprotein Zymogen
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
	Signal peptide	1 – 19	19	Potential
	Propeptide	20 – 39	20	By similarity		PRO_0000027774
	Chain	40 – 471	432	Coagulation factor IX		PRO_0000027775
	Chain	40 – 185	146	Coagulation factor IXa light chain		PRO_0000027776
	Propeptide	186 – 235	50	Activation peptide By similarity		PRO_0000027777
	Chain	236 – 471	236	Coagulation factor IXa heavy chain		PRO_0000027778
Regions
	Domain	40 – 85	46	Gla
	Domain	86 – 122	37	EGF-like 1; calcium-binding Potential
	Domain	123 – 164	42	EGF-like 2
	Domain	236 – 469	234	Peptidase S1
Sites
	Active site	277	1	Charge relay system By similarity
	Active site	325	1	Charge relay system By similarity
	Active site	421	1	Charge relay system By similarity
	Site	185 – 186	2	Cleavage; by factor XIa By similarity
	Site	235 – 236	2	Cleavage; by factor XIa By similarity
Amino acid modifications
	Modified residue	46	1	4-carboxyglutamate By similarity
	Modified residue	47	1	4-carboxyglutamate By similarity
	Modified residue	54	1	4-carboxyglutamate By similarity
	Modified residue	56	1	4-carboxyglutamate By similarity
	Modified residue	59	1	4-carboxyglutamate By similarity
	Modified residue	60	1	4-carboxyglutamate By similarity
	Modified residue	65	1	4-carboxyglutamate By similarity
	Modified residue	66	1	4-carboxyglutamate By similarity
	Modified residue	69	1	4-carboxyglutamate By similarity
	Modified residue	72	1	4-carboxyglutamate By similarity
	Modified residue	75	1	4-carboxyglutamate By similarity
	Modified residue	79	1	4-carboxyglutamate By similarity
	Modified residue	103	1	(3R)-3-hydroxyaspartate By similarity
	Modified residue	107	1	Phosphoserine By similarity
	Glycosylation	92	1	O-linked (Glc...) By similarity
	Disulfide bond	57 ↔ 62		By similarity
	Disulfide bond	90 ↔ 101		By similarity
	Disulfide bond	95 ↔ 110		By similarity
	Disulfide bond	112 ↔ 121		By similarity
	Disulfide bond	127 ↔ 138		By similarity
	Disulfide bond	134 ↔ 148		By similarity
	Disulfide bond	150 ↔ 163		By similarity
	Disulfide bond	171 ↔ 345		By similarity
	Disulfide bond	262 ↔ 278		By similarity
	Disulfide bond	392 ↔ 406		By similarity
	Disulfide bond	417 ↔ 445		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q804X6-1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 3C133356BBF7C02A	FASTA	471	51,804
	10 20 30 40 50 60 MAKIPLILSF CLLEAFLGAE STVFIENKEA STVLSRTRRG NSNRLEELIP GNLERECIEE 70 80 90 100 110 120 KCSFEEAREV FENTEKTMEF WKIYIDGDQC NSNPCKNGAV CKDGVSSYEC MCPPGYGGRN 130 140 150 160 170 180 CEIDSTCATK NGGCEHFCRH DTPQKAVCSC ASGYKLHEDG KSCKPAVPYP CGRITAPEMR 190 200 210 220 230 240 GKVTRTENTI ERWNITAHDE GDAHDEALDI TEPPPPPTTS AAPAKIVPIT KNDTRVVGGY 250 260 270 280 290 300 DSVKGQLPWQ VHLVDSRGLG FCGGSIINEK WVVTAAHCLE PGDNVTAVAG EYNTKEDDHT 310 320 330 340 350 360 EQRRQVVKIL PYPTYNRTRN KHHNDIALLE LDQPLTFNSY VTPICIGSRD FTNNLLSNGP 370 380 390 400 410 420 GTVSGWGSML YRGRSAIVLQ VLTVPFVDRV TCLKSTSTTI LHSMFCAGYT AGGKDTCGGD 430 440 450 460 470 SGGPYTNSIG ETWFLTGVTS WGEECAKPGK YGIYTKVAKY VKWIRETTRL T

References

[1]	"Molecular evolution of the vertebrate blood coagulation network." Davidson C.J., Hirt R.P., Lal K., Snell P., Elgar G., Tuddenham E.G., McVey J.H. Thromb. Haemost. 89:420-428(2003) [PubMed: 12624623] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF465269 mRNA. Translation: AAO33364.1.
IPI	IPI00574534.
RefSeq	NP_989674.1.
UniGene	Gga.5169
3D structure databases
HSSP	HSSP built from PDB template 1CFH based on UniProtKB P00740.
ModBase	Search...
Protein family/group databases
MEROPS	S01.214.
Genome annotation databases
Ensembl	ENSGALG00000006513. Gallus gallus. [Contig view]
GeneID	374258.
KEGG	gga:374258.
Phylogenomic databases
HOVERGEN	Q804X6.
Enzyme and pathway databases
BRENDA	3.4.21.22. 4.
Family and domain databases
InterPro	IPR002383. Coagulation_factor_Gla. IPR006209. EGF. IPR006210. EGF-like. IPR013032. EGF-like_reg_CS. IPR000152. EGF-type_Asp/Asn_hydroxyl_CS. IPR001438. EGF_2. IPR000742. EGF_3. IPR001881. EGF_Ca_bd. IPR018097. EGF_Ca_bd_CS. IPR000294. GLA_domain. IPR012224. Pept_S1A_FX. IPR018114. Peptidase_S1/S6_AS. IPR001254. Peptidase_S1_S6. IPR001314. Peptidase_S1A. [Graphical view]
Pfam	PF00008. EGF. 2 hits. PF00594. Gla. 1 hit. PF00089. Trypsin. 1 hit. [Graphical view]
PIRSF	PIRSF001143. Factor_X. 1 hit.
PRINTS	PR00722. CHYMOTRYPSIN. PR00010. EGFBLOOD. PR00001. GLABLOOD.
SMART	SM00181. EGF. 1 hit. SM00179. EGF_CA. 1 hit. SM00069. GLA. 1 hit. SM00020. Tryp_SPc. 1 hit. [Graphical view]
PROSITE	PS00010. ASX_HYDROXYL. 1 hit. PS00022. EGF_1. 1 hit. PS01186. EGF_2. 2 hits. PS50026. EGF_3. 1 hit. PS01187. EGF_CA. 1 hit. PS00011. GLA_1. 1 hit. PS50998. GLA_2. 1 hit. PS50240. TRYPSIN_DOM. 1 hit. PS00134. TRYPSIN_HIS. 1 hit. PS00135. TRYPSIN_SER. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FA9_CHICK

Accession

Primary (citable) accession number: Q804X6

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 2005
Last sequence update:	June 1, 2003
Last modified:	June 16, 2009
This is version 51 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)