[1]	NUCLEOTIDE SEQUENCE [MRNA] OF 9-146. TISSUE=Liver; Lollar P.; Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
[2]	NUCLEOTIDE SEQUENCE [MRNA] OF 139-409. DOI=10.1016/0888-7543(90)90458-7; PubMed=2303254 [NCBI, ExPASy, EBI, Israel, Japan] Sarkar G., Koeberl D.D., Sommer S.S.; "Direct sequencing of the activation peptide and the catalytic domain of the factor IX gene in six species."; Genomics 6:133-143(1990).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 237-245. STRAIN=Meishan, and Wild boar; PubMed=8856916 [NCBI, ExPASy, EBI, Israel, Japan] Signer E.N., Armour J.A.L., Jeffreys A.J.; "Detection of an MboI RFLP at the porcine clotting factor IX locus and verification of sex linkage."; Anim. Genet. 27:130-130(1996).
[4]	PROTEIN SEQUENCE OF 1-12. DOI=10.1021/bi00398a015; PubMed=3322404 [NCBI, ExPASy, EBI, Israel, Japan] Lollar P., Parker C.G., Kajenski P.J., Litwiller R.D., Fass D.N.; "Degradation of coagulation proteins by an enzyme from Malayan pit viper (Akistrodon rhodostoma) venom."; Biochemistry 26:7627-7636(1987).
[5]	X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH INHIBITOR. PubMed=7568220 [NCBI, ExPASy, EBI, Israel, Japan] Brandstetter H., Bauer M., Huber R., Lollar P., Bode W.; "X-ray structure of clotting factor IXa: active site and module structure related to Xase activity and hemophilia B."; Proc. Natl. Acad. Sci. U.S.A. 92:9796-9800(1995).

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 Ca(2+) ions, phospholipids, and factor VIIIa.
CATALYTIC ACTIVITY: Selective cleavage of Arg-|-Ile bond in factor X to form factor Xa.
SUBUNIT: 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.
PTM: Activated by factor XIa, which excises the activation peptide (By similarity).
SIMILARITY: Belongs to the peptidase S1 family [view classification].
SIMILARITY: Contains 2 EGF-like domains.
SIMILARITY: Contains 1 Gla (gamma-carboxy-glutamate) domain.
SIMILARITY: Contains 1 peptidase S1 domain [view classification].

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

U51135; AAA96318.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M26235; AAA31031.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X92427; CAA63155.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X92593; CAA63337.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

I46580; I46580.

UniGene

Ssc.16252

3D structure databases

PDB

1PFX; X-ray; 3.00 A; C=183-409, L=8-147.	[ExPASy / RCSB / EBI]
1X7A; X-ray; 2.90 A; C=183-409, L=8-147.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1PFX; -.
1X7A; -.

ModBase

P16293.

Protein family/group databases

MEROPS

S01.214; -.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from InterPro).
GO:0005509;	Molecular function: calcium ion binding (inferred from electronic annotation from InterPro).
GO:0004252;	Molecular function: serine-type endopeptidase activity (inferred from electronic annotation from InterPro).
GO:0007596;	Biological process: blood coagulation (inferred from electronic annotation from InterPro).
GO:0006508;	Biological process: proteolysis (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR002383; Coagulation_factor_Gla.
IPR006210; EGF.
IPR000152; EGF-type_Asp/Asn_hydroxyl_CS.
IPR001438; EGF_2.
IPR000742; EGF_3.
IPR001881; EGF_Ca_bd.
IPR006209; EGF_like.
IPR013032; EGF_like_reg_CS.
IPR012224; Pept_S1A_FX.
IPR001254; Peptidase_S1_S6.
IPR001314; Peptidase_S1A.
IPR000294; VitK_dep_GLA.
Graphical view of domain structure.

Pfam

PF00008; EGF; 2.
PF00594; Gla; 1.
PF00089; Trypsin; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF001143; Factor_X; 1.

PRINTS

PR00722; CHYMOTRYPSIN.
PR00010; EGFBLOOD.
PR00001; GLABLOOD.

SMART

SM00181; EGF; 1.
SM00179; EGF_CA; 1.
SM00069; GLA; 1.
SM00020; Tryp_SPc; 1.
SMART graphical view of domain structure.

PROSITE

PS00010; ASX_HYDROXYL; 1.
PS00022; EGF_1; 1.
PS01186; EGF_2; 2.
PS50026; EGF_3; 1.
PS01187; EGF_CA; 1.
PS00011; GLA_1; 1.
PS50998; GLA_2; 1.
PS50240; TRYPSIN_DOM; 1.
PS00134; TRYPSIN_HIS; 1.
PS00135; TRYPSIN_SER; 1.
PROSITE graphical view of domain structure (profiles).

Phylogenomic databases

HOVERGEN

P16293; -.

Other

P16293; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Blood coagulation; Calcium; Direct protein sequencing; EGF-like domain; Gamma-carboxyglutamic acid; Glycoprotein; Hydrolase; Hydroxylation; Phosphoprotein; Protease; Repeat; Secreted; Serine protease; Sulfation; Zymogen.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 409`	`409`	`Coagulation factor IX.`	`PRO_0000027770`
`CHAIN`	`1 147`	`147`	`Coagulation factor IXa light chain.`	`PRO_0000027771`
`PROPEP`	`148 182`	`35`	`Activation peptide (By similarity).`	`PRO_0000027772`
`CHAIN`	`183 409`	`227`	`Coagulation factor IXa heavy chain.`	`PRO_0000027773`
`DOMAIN`	`1 47`	`47`	`Gla.`
`DOMAIN`	`48 84`	`37`	`EGF-like 1; calcium-binding (Potential).`
`DOMAIN`	`85 126`	`42`	`EGF-like 2.`
`DOMAIN`	`183 409`	`227`	`Peptidase S1.`
`ACT_SITE`	`223 223`		`Charge relay system.`
`ACT_SITE`	`271 271`		`Charge relay system.`
`ACT_SITE`	`367 367`		`Charge relay system.`
`SITE`	`147 148`	`2`	`Cleavage; by factor XIa (By similarity).`
`SITE`	`182 183`	`2`	`Cleavage; by factor XIa (By similarity).`
`MOD_RES`	`7 7`		`4-carboxyglutamate.`
`MOD_RES`	`8 8`		`4-carboxyglutamate.`
`MOD_RES`	`16 16`		`4-carboxyglutamate.`
`MOD_RES`	`18 18`		`4-carboxyglutamate.`
`MOD_RES`	`21 21`		`4-carboxyglutamate.`
`MOD_RES`	`22 22`		`4-carboxyglutamate.`
`MOD_RES`	`27 27`		`4-carboxyglutamate.`
`MOD_RES`	`28 28`		`4-carboxyglutamate.`
`MOD_RES`	`31 31`		`4-carboxyglutamate.`
`MOD_RES`	`34 34`		`4-carboxyglutamate.`
`MOD_RES`	`37 37`		`4-carboxyglutamate.`
`MOD_RES`	`41 41`		`4-carboxyglutamate.`
`MOD_RES`	`65 65`		`3-hydroxyaspartate.`
`MOD_RES`	`69 69`		`Phosphoserine (By similarity).`
`MOD_RES`	`157 157`		`Sulfotyrosine (By similarity).`
`CARBOHYD`	`161 161`		`O-linked (GalNAc...) (By similarity).`
`CARBOHYD`	`171 171`		`O-linked (GalNAc...) (By similarity).`
`CARBOHYD`	`174 174`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`262 262`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`19 24`
`DISULFID`	`52 63`
`DISULFID`	`57 72`
`DISULFID`	`74 83`
`DISULFID`	`89 100`
`DISULFID`	`96 110`
`DISULFID`	`112 125`
`DISULFID`	`133 291`
`DISULFID`	`208 224`
`DISULFID`	`338 352`
`DISULFID`	`363 391`
`NON_TER`	`1 1`
`HELIX`	`15 18`	`4`
`TURN`	`19 23`	`5`
`HELIX`	`26 33`	`8`
`HELIX`	`37 44`	`8`
`TURN`	`51 54`	`4`
`STRAND`	`62 65`	`4`
`STRAND`	`70 73`	`4`
`STRAND`	`76 79`	`4`
`TURN`	`80 83`	`4`
`HELIX`	`92 95`	`4`
`STRAND`	`97 100`	`4`
`STRAND`	`104 107`	`4`
`STRAND`	`116 118`	`3`
`STRAND`	`125 131`	`7`
`HELIX`	`137 140`	`4`
`TURN`	`141 143`	`3`
`STRAND`	`197 201`	`5`
`STRAND`	`207 214`	`8`
`STRAND`	`217 220`	`4`
`HELIX`	`222 224`	`3`
`STRAND`	`232 235`	`4`
`STRAND`	`248 257`	`10`
`STRAND`	`263 265`	`3`
`STRAND`	`273 279`	`7`
`HELIX`	`295 302`	`8`
`STRAND`	`305 313`	`9`
`STRAND`	`326 333`	`8`
`HELIX`	`335 341`	`7`
`STRAND`	`350 354`	`5`
`STRAND`	`356 359`	`4`
`STRAND`	`371 375`	`5`
`STRAND`	`378 381`	`4`
`STRAND`	`384 387`	`4`
`STRAND`	`389 392`	`4`
`STRAND`	`398 401`	`4`
`HELIX`	`403 409`	`7`

Sequence information

Length: 409 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 45516 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: 6AFEAE92E2515488 [This is a checksum on the sequence]

        10         20         30         40         50         60 
YNSGKLEESF VRGNLERECI EEKCSFEEAR EVFENTEKTN EFWKQYVDGD QCEPNPCLNG 

        70         80         90        100        110        120 
GLCKDDINSY ECWCQVGFEG KNCELDATCN IKNGRCKQFC KTGADSKVLC SCTTGYRLAP 

       130        140        150        160        170        180 
DQKSCKPAVP FPCGRVSVSH SPTTLTRAEI IFSNMDYENS TEVEPILDSL TESNQSSDDF 

       190        200        210        220        230        240 
IRIVGGENAK PGQFPWQVLL NGKIDAFCGG SIINEKWVVT AAHCIEPGVK ITVVAGEYNT 

       250        260        270        280        290        300 
EETEPTEQRR NVIRAIPHHS YNATVNKYSH DIALLELDEP LTLNSYVTPI CIADKEYTNI 

       310        320        330        340        350        360 
FLKFGSGYVS GWGRVFNRGR SATILQYLKV PLVDRATCLR STKVTIYSNM FCAGFHEGGK 

       370        380        390        400 
DSCLGDSGGP HVTEVEGTSF LTGIISWGEE CAVKGKYGIY TKVSRYVNW

P16293 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools