Reviewed, UniProtKB/Swiss-Prot P00741 (FA9_BOVIN)

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

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	416 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein 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. The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.
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
Disease	Hemophilia
Domain	EGF-like domain
Ligand	Calcium
Molecular function	Hydrolase Protease Serine protease
PTM	Disulfide bond Gamma-carboxyglutamic acid Glycoprotein Hydroxylation Zymogen
Technical term	3D-structure Direct protein sequencing
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 – 416

416

Coagulation factor IX

PRO_0000027741

Chain

1 – 146

146

Coagulation factor IXa light chain

PRO_0000027742

Propeptide

147 – 181

35

Activation peptide

PRO_0000027743

Chain

182 – 416

235

Coagulation factor IXa heavy chain

PRO_0000027744

Regions

Domain

1 – 46

46

Gla

Domain

47 – 83

37

EGF-like 1; calcium-binding Potential

Domain

84 – 125

42

EGF-like 2

Domain

182 – 414

233

Peptidase S1

Sites

Active site

222

1

Charge relay system

Active site

270

1

Charge relay system

Active site

366

1

Charge relay system

Site

146 – 147

2

Cleavage; by factor XIa

Site

181 – 182

2

Cleavage; by factor XIa

Amino acid modifications

Modified residue

7

1

4-carboxyglutamate Ref.1

Modified residue

8

1

4-carboxyglutamate Ref.1

Modified residue

15

1

4-carboxyglutamate

Modified residue

17

1

4-carboxyglutamate Ref.1

Modified residue

20

1

4-carboxyglutamate Ref.1

Modified residue

21

1

4-carboxyglutamate Ref.1

Modified residue

26

1

4-carboxyglutamate Ref.1

Modified residue

27

1

4-carboxyglutamate Ref.1

Modified residue

30

1

4-carboxyglutamate Ref.1

Modified residue

33

1

4-carboxyglutamate Ref.1

Modified residue

36

1

4-carboxyglutamate

Modified residue

40

1

4-carboxyglutamate

Modified residue

64

1

(3R)-3-hydroxyaspartate

Glycosylation

53

1

O-linked (Glc...)

CAR_000008

Glycosylation

158

1

N-linked (GlcNAc...) Ref.1

Glycosylation

168

1

N-linked (GlcNAc...)

Glycosylation

173

1

N-linked (GlcNAc...)

Glycosylation

261

1

N-linked (GlcNAc...)

Disulfide bond

18 ↔ 23

Disulfide bond

51 ↔ 62

By similarity

Disulfide bond

56 ↔ 71

By similarity

Disulfide bond

73 ↔ 82

By similarity

Disulfide bond

88 ↔ 99

By similarity

Disulfide bond

95 ↔ 109

By similarity

Disulfide bond

111 ↔ 124

By similarity

Disulfide bond

132 ↔ 290

By similarity

Disulfide bond

207 ↔ 223

By similarity

Disulfide bond

337 ↔ 351

By similarity

Disulfide bond

362 ↔ 390

By similarity

Experimental info

Sequence conflict

64

1

D → T AA sequence Ref.1

Non-terminal residue

1

1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

416

Helix Strand Turn

Details...

Beta strand

4 – 6

3

Helix

7 – 9

3

Helix

14 – 18

5

Helix

25 – 32

8

Helix

35 – 45

11

Sequences

	Sequence		Length	Mass (Da)
	P00741-1 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 34A7DFE916330662	FASTA	416	46,785
	10 20 30 40 50 60 YNSGKLEEFV RGNLERECKE EKCSFEEARE VFENTEKTTE FWKQYVDGDQ CESNPCLNGG 70 80 90 100 110 120 MCKDDINSYE CWCQAGFEGT NCELDATCSI KNGRCKQFCK RDTDNKVVCS CTDGYRLAED 130 140 150 160 170 180 QKSCEPAVPF PCGRVSVSHI SKKLTRAETI FSNTNYENSS EAEIIWDNVT QSNQSFDEFS 190 200 210 220 230 240 RVVGGEDAER GQFPWQVLLH GEIAAFCGGS IVNEKWVVTA AHCIKPGVKI TVVAGEHNTE 250 260 270 280 290 300 KPEPTEQKRN VIRAIPYHSY NASINKYSHD IALLELDEPL ELNSYVTPIC IADRDYTNIF 310 320 330 340 350 360 SKFGYGYVSG WGKVFNRGRS ASILQYLKVP LVDRATCLRS TKFSIYSHMF CAGYHEGGKD 370 380 390 400 410 SCQGDSGGPH VTEVEGTSFL TGIISWGEEC AMKGKYGIYT KVSRYVNWIK EKTKLT

References

[1]	"Comparison of amino acid sequence of bovine coagulation Factor IX (Christmas factor) with that of other vitamin K-dependent plasma proteins." Katayama K., Ericsson L.H., Enfield D.L., Walsh K.A., Neurath H., Davie E.W., Titani K. Proc. Natl. Acad. Sci. U.S.A. 76:4990-4994(1979) [PubMed: 291916] [Abstract] Cited for: PROTEIN SEQUENCE.
[2]	"The occurrence of beta-hydroxyaspartic acid in the vitamin K-dependent blood coagulation zymogens." McMullen B.A., Fujikawa K., Kisiel W. Biochem. Biophys. Res. Commun. 115:8-14(1983) [PubMed: 6688526] [Abstract] Cited for: SEQUENCE REVISION TO 64.
[3]	"Molecular cloning of the gene for human anti-haemophilic factor IX." Choo K.H., Gould K.G., Rees D.J.G., Brownlee G.G. Nature 299:178-180(1982) [PubMed: 6287289] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 51-111.
[4]	"A new trisaccharide sugar chain linked to a serine residue in bovine blood coagulation factors VII and IX." Hase S., Kawabata S., Nishimura H., Takeya H., Sueyoshi T., Miyata T., Iwanaga S., Takao T., Shimonishi Y., Ikenaka T. J. Biochem. 104:867-868(1988) [PubMed: 3149637] [Abstract] Cited for: STRUCTURE OF CARBOHYDRATE ON SER-53.
[5]	"A new trisaccharide sugar chain linked to a serine residue in the first EGF-like domain of clotting factors VII and IX and protein Z." Iwanaga S., Nishimura H., Kawabata S., Kisiel W., Hase S., Ikenaka T. Adv. Exp. Med. Biol. 281:121-131(1990) [PubMed: 2129367] [Abstract] Cited for: STRUCTURE OF CARBOHYDRATE ON SER-53.
[6]	"The structure of (xylose)2glucose-O-serine 53 found in the first epidermal growth factor-like domain of bovine blood clotting factor IX." Hase S., Nishimura H., Kawabata S., Iwanaga S., Ikenaka T. J. Biol. Chem. 265:1858-1861(1990) [PubMed: 2105311] [Abstract] Cited for: STRUCTURE OF CARBOHYDRATE ON SER-53.

Cross-references

Sequence databases

EMBLGenBankDDBJ

J00007 mRNA. Translation: AAA30520.1.

IPI

IPI00905351.

PIR

KFBO. A14757.

UniGene

Bt.13106

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1J34	X-ray	1.55	C	1-46	[»]
1J35	X-ray	1.80	C	1-46	[»]

SMR

P00741. Positions 1-146, 182-416.

ModBase

Search...

Protein family/group databases

MEROPS

S01.214.

PTM databases

GlycoSuiteDB

P00741.

Genome annotation databases

Ensembl

ENSBTAG00000004003. Bos taurus. [Contig view]

Phylogenomic databases

HOVERGEN

P00741.

Enzyme and pathway databases

BRENDA

3.4.21.22. 251.

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...

Other Resources

PMAP-CutDB

P00741.

Entry information

Entry name

FA9_BOVIN

Accession

Primary (citable) accession number: P00741

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	June 16, 2009
This is version 111 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)