[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=C57BL/6 X CBA; TISSUE=Liver; PubMed=9684791 [NCBI, ExPASy, EBI, Israel, Japan] Liang Z., Cooper A., DeFord M.E., Carmeliet P., Collen D., Castellino F.J., Rosen E.D.; "Cloning and characterization of a cDNA encoding murine coagulation factor X."; Thromb. Haemost. 80:87-91(1998).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Liver; DOI=10.1016/S0049-3848(98)00110-8; PubMed=9783672 [NCBI, ExPASy, EBI, Israel, Japan] Heidtmann H.H., Kontermann R.E.; "Cloning and recombinant expression of mouse coagulation factor X."; Thromb. Res. 92:33-41(1998).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=129/SvJ; PubMed=10823271 [NCBI, ExPASy, EBI, Israel, Japan] Cooper A., Liang Z., Castellino F.J., Rosen E.D.; "Cloning and characterization of the murine coagulation factor X gene."; Thromb. Haemost. 83:732-735(2000).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[5]	GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-187, AND MASS SPECTROMETRY. TISSUE=Plasma; DOI=10.1021/pr060186m; PubMed=16944957 [NCBI, ExPASy, EBI, Israel, Japan] Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.; "Proteome-wide characterization of N-glycosylation events by diagonal chromatography."; J. Proteome Res. 5:2438-2447(2006).

Comments

FUNCTION: Factor Xa is a vitamin K-dependent glycoprotein that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting.
CATALYTIC ACTIVITY: Selective cleavage of Arg-|-Thr and then Arg-|-Ile bonds in prothrombin to form thrombin.
SUBUNIT: The two chains are formed from a single-chain precursor by the excision of two Arg residues and are held together by 1 or more disulfide bonds (By similarity).
INTERACTION:
Q16938:- (xeno); NbExp=1; IntAct=EBI-1646313, EBI-1646299;
Q964Q0:- (xeno); NbExp=1; IntAct=EBI-1646313, EBI-1646347;
SUBCELLULAR LOCATION: Secreted.
TISSUE SPECIFICITY: Plasma; synthesized in the liver.
PTM: The vitamin K-dependent, enzymatic carboxylation of some glutamate residues allows the modified protein to bind calcium.
PTM: N- and O-glycosylated (By similarity).
PTM: The activation peptide is cleaved by factor IXa (in the intrinsic pathway), or by factor VIIa (in the extrinsic pathway) (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

AF087644; AAC36345.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ222677; CAA10933.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF211347; AAF22980.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC003877; AAH03877.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_031998.3; -.

UniGene

Mm.262589

3D structure databases

HSSP

P00742; 1G2L. [HSSP ENTRY / PDB]

SMR

O88947; 232-472.

ModBase

O88947.

Protein-protein interaction databases

IntAct

O88947; 2.

Protein family/group databases

MEROPS

S01.216; -.

Organism-specific databases

MGI

MGI:103107; F10.

Gene expression databases

ArrayExpress

O88947; -.

CleanEx

MM_F10; -.

GermOnline

ENSMUSG00000031444; Mus musculus.

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:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
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).

Genome annotation databases

Ensembl

ENSMUSG00000031444; Mus musculus. [Contig view]

GeneID

14058; -.

KEGG

mmu:14058; -.

Phylogenomic databases

HOVERGEN

O88947; -.

Other

285020; -.

F10; Mus musculus.

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

Keywords

Blood coagulation; Calcium; Cleavage on pair of basic residues; EGF-like domain; Gamma-carboxyglutamic acid; Glycoprotein; Hydrolase; Hydroxylation; Protease; Repeat; Secreted; Serine protease; Signal; Zymogen.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 20`	`20`	`Potential.`
`PROPEP`	`21 40`	`20`	`By similarity.`	`PRO_0000027792`
`CHAIN`	`41 481`	`441`	`Coagulation factor X.`	`PRO_0000027793`
`CHAIN`	`41 180`	`140`	`Factor X light chain (By similarity).`	`PRO_0000027794`
`CHAIN`	`184 481`	`298`	`Factor X heavy chain (By similarity).`	`PRO_0000027795`
`PROPEP`	`184 231`	`48`	`Activation peptide (By similarity).`	`PRO_0000027796`
`CHAIN`	`232 481`	`250`	`Activated factor Xa heavy chain (By similarity).`	`PRO_0000027797`
`DOMAIN`	`41 85`	`45`	`Gla.`
`DOMAIN`	`86 122`	`37`	`EGF-like 1; calcium-binding (Potential).`
`DOMAIN`	`125 165`	`41`	`EGF-like 2.`
`DOMAIN`	`232 464`	`233`	`Peptidase S1.`
`ACT_SITE`	`273 273`		`Charge relay system (By similarity).`
`ACT_SITE`	`319 319`		`Charge relay system (By similarity).`
`ACT_SITE`	`416 416`		`Charge relay system (By similarity).`
`MOD_RES`	`46 46`		`4-carboxyglutamate (By similarity).`
`MOD_RES`	`47 47`		`4-carboxyglutamate (By similarity).`
`MOD_RES`	`54 54`		`4-carboxyglutamate (By similarity).`
`MOD_RES`	`56 56`		`4-carboxyglutamate (By similarity).`
`MOD_RES`	`59 59`		`4-carboxyglutamate (By similarity).`
`MOD_RES`	`60 60`		`4-carboxyglutamate (By similarity).`
`MOD_RES`	`65 65`		`4-carboxyglutamate (By similarity).`
`MOD_RES`	`66 66`		`4-carboxyglutamate (By similarity).`
`MOD_RES`	`69 69`		`4-carboxyglutamate (By similarity).`
`MOD_RES`	`72 72`		`4-carboxyglutamate (By similarity).`
`MOD_RES`	`75 75`		`4-carboxyglutamate (By similarity).`
`MOD_RES`	`79 79`		`4-carboxyglutamate (By similarity).`
`MOD_RES`	`103 103`		`3-hydroxyaspartate (By similarity).`
`CARBOHYD`	`187 187`		`N-linked (GlcNAc...).`
`CARBOHYD`	`218 218`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`57 62`		`By similarity.`
`DISULFID`	`90 101`		`By similarity.`
`DISULFID`	`95 110`		`By similarity.`
`DISULFID`	`112 121`		`By similarity.`
`DISULFID`	`129 140`		`By similarity.`
`DISULFID`	`136 149`		`By similarity.`
`DISULFID`	`151 164`		`By similarity.`
`DISULFID`	`172 339`		`Interchain (between light and heavy chains) (By similarity).`
`DISULFID`	`238 243`		`By similarity.`
`DISULFID`	`258 274`		`By similarity.`
`DISULFID`	`387 401`		`By similarity.`
`DISULFID`	`412 440`		`By similarity.`
`CONFLICT`	`250 250`		`I -> V (in Ref. 4; AAH03877).`
`CONFLICT`	`294 294`		`E -> D (in Ref. 2; CAA10933).`
`CONFLICT`	`298 298`		`M -> L (in Ref. 2; CAA10933).`

Sequence information

Length: 481 AA [This is the length of the unprocessed precursor]

Molecular weight: 54018 Da [This is the MW of the unprocessed precursor]

CRC64: 8AC09DE5EF9D271E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MGSPVQLSLL CVVLASLLLP GKGVFINRER ANNVLARTRR ANSFFEEFKK GNLERECMEE 

        70         80         90        100        110        120 
ICSYEEVREI FEDDEKTKEY WTKYKDGDQC ESSPCQNQGA CRDGIGGYTC TCSEGFEGKN 

       130        140        150        160        170        180 
CELFVRKLCR LDNGDCDQFC REEQNSVVCS CASGYFLGND GKSCISTAPF PCGKITTGRR 

       190        200        210        220        230        240 
KRSVALNTSD SELDLEDALL DEDFLSPTEN PIELLNLNET QPERSSDDLV RIVGGRECKD 

       250        260        270        280        290        300 
GECPWQALLI NEDNEGFCGG TILNEFYILT AAHCLHQARR FKVRVGDRNT EKEEGNEMVH 

       310        320        330        340        350        360 
EVDVVIKHNK FQRDTYDYDI AVLRLKTPIT FRMNVAPACL PQKDWAESTL MTQKTGIVSG 

       370        380        390        400        410        420 
FGRTHEKGRQ SNILKMLEVP YVDRNTCKLS TSFSITQNMF CAGYEAKLED ACQGDSGGPH 

       430        440        450        460        470        480 
VTRFKNTYYV TGIVSWGEGC ARKGKYGIYT KVTTFLKWID RSMKARVGPT AETPRTAGPP 


N

O88947 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