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Protein

Coagulation factor X

Gene

F10

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

Selective cleavage of Arg-|-Thr and then Arg-|-Ile bonds in prothrombin to form thrombin.

Enzyme regulationi

Inhibited by SERPINA5.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei273Charge relay systemBy similarity1
Active sitei319Charge relay systemBy similarity1
Active sitei416Charge relay systemBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Blood coagulation, Hemostasis

Keywords - Ligandi

Calcium

Enzyme and pathway databases

ReactomeiR-MMU-140834. Extrinsic Pathway of Fibrin Clot Formation.
R-MMU-140837. Intrinsic Pathway of Fibrin Clot Formation.
R-MMU-140875. Common Pathway of Fibrin Clot Formation.
R-MMU-159740. Gamma-carboxylation of protein precursors.
R-MMU-159763. Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
R-MMU-159782. Removal of aminoterminal propeptides from gamma-carboxylated proteins.

Protein family/group databases

MEROPSiS01.216.

Names & Taxonomyi

Protein namesi
Recommended name:
Coagulation factor X (EC:3.4.21.6)
Alternative name(s):
Stuart factor
Cleaved into the following 3 chains:
Gene namesi
Name:F10
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:103107. F10.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Sequence analysisAdd BLAST20
PropeptideiPRO_000002779221 – 40By similarityAdd BLAST20
ChainiPRO_000002779341 – 481Coagulation factor XAdd BLAST441
ChainiPRO_000002779441 – 180Factor X light chainBy similarityAdd BLAST140
ChainiPRO_0000027795184 – 481Factor X heavy chainBy similarityAdd BLAST298
PropeptideiPRO_0000027796184 – 231Activation peptideBy similarityAdd BLAST48
ChainiPRO_0000027797232 – 481Activated factor Xa heavy chainBy similarityAdd BLAST250

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei464-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei474-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei544-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei564-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Disulfide bondi57 ↔ 62By similarity
Modified residuei594-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei604-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei654-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei664-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei694-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei724-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei754-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei794-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Disulfide bondi90 ↔ 101By similarity
Disulfide bondi95 ↔ 110By similarity
Modified residuei103(3R)-3-hydroxyaspartateBy similarity1
Disulfide bondi112 ↔ 121By similarity
Disulfide bondi129 ↔ 140By similarity
Disulfide bondi136 ↔ 149By similarity
Disulfide bondi151 ↔ 164By similarity
Disulfide bondi172 ↔ 339Interchain (between light and heavy chains)PROSITE-ProRule annotation
Glycosylationi187N-linked (GlcNAc...)1 Publication1
Glycosylationi218N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi238 ↔ 243By similarity
Disulfide bondi258 ↔ 274By similarity
Disulfide bondi387 ↔ 401By similarity
Disulfide bondi412 ↔ 440By similarity

Post-translational modificationi

The vitamin K-dependent, enzymatic carboxylation of some glutamate residues allows the modified protein to bind calcium.
N- and O-glycosylated.By similarity
The activation peptide is cleaved by factor IXa (in the intrinsic pathway), or by factor VIIa (in the extrinsic pathway).By similarity

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Gamma-carboxyglutamic acid, Glycoprotein, Hydroxylation, Zymogen

Proteomic databases

PaxDbiO88947.
PeptideAtlasiO88947.
PRIDEiO88947.

PTM databases

iPTMnetiO88947.
PhosphoSitePlusiO88947.

Expressioni

Tissue specificityi

Plasma; synthesized in the liver.

Gene expression databases

BgeeiENSMUSG00000031444.
CleanExiMM_F10.
ExpressionAtlasiO88947. baseline and differential.
GenevisibleiO88947. MM.

Interactioni

Subunit structurei

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. Forms a heterodimer with SERPINA5 (By similarity).By similarity

Protein-protein interaction databases

IntActiO88947. 2 interactors.
MINTiMINT-6597397.
STRINGi10090.ENSMUSP00000033821.

Structurei

3D structure databases

ProteinModelPortaliO88947.
SMRiO88947.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini41 – 85GlaPROSITE-ProRule annotationAdd BLAST45
Domaini86 – 122EGF-like 1; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini125 – 165EGF-like 2PROSITE-ProRule annotationAdd BLAST41
Domaini232 – 464Peptidase S1PROSITE-ProRule annotationAdd BLAST233

Sequence similaritiesi

Belongs to the peptidase S1 family.PROSITE-ProRule annotation
Contains 2 EGF-like domains.PROSITE-ProRule annotation
Contains 1 Gla (gamma-carboxy-glutamate) domain.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IGPV. Eukaryota.
COG5640. LUCA.
GeneTreeiENSGT00760000118890.
HOGENOMiHOG000251821.
HOVERGENiHBG013304.
InParanoidiO88947.
KOiK01314.
TreeFamiTF327329.

Family and domain databases

CDDicd00190. Tryp_SPc. 1 hit.
Gene3Di4.10.740.10. 1 hit.
InterProiIPR017857. Coagulation_fac_subgr_Gla_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR000294. GLA_domain.
IPR012224. Pept_S1A_FX.
IPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[Graphical view]
PfamiPF00008. EGF. 1 hit.
PF00594. Gla. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFiPIRSF001143. Factor_X. 1 hit.
PRINTSiPR00722. CHYMOTRYPSIN.
PR00001. GLABLOOD.
SMARTiSM00181. EGF. 2 hits.
SM00179. EGF_CA. 1 hit.
SM00069. GLA. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 2 hits.
SSF57630. SSF57630. 1 hit.
PROSITEiPS00010. 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]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O88947-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSPVQLSLL CVVLASLLLP GKGVFINRER ANNVLARTRR ANSFFEEFKK
60 70 80 90 100
GNLERECMEE ICSYEEVREI FEDDEKTKEY WTKYKDGDQC ESSPCQNQGA
110 120 130 140 150
CRDGIGGYTC TCSEGFEGKN CELFVRKLCR LDNGDCDQFC REEQNSVVCS
160 170 180 190 200
CASGYFLGND GKSCISTAPF PCGKITTGRR KRSVALNTSD SELDLEDALL
210 220 230 240 250
DEDFLSPTEN PIELLNLNET QPERSSDDLV RIVGGRECKD GECPWQALLI
260 270 280 290 300
NEDNEGFCGG TILNEFYILT AAHCLHQARR FKVRVGDRNT EKEEGNEMVH
310 320 330 340 350
EVDVVIKHNK FQRDTYDYDI AVLRLKTPIT FRMNVAPACL PQKDWAESTL
360 370 380 390 400
MTQKTGIVSG FGRTHEKGRQ SNILKMLEVP YVDRNTCKLS TSFSITQNMF
410 420 430 440 450
CAGYEAKLED ACQGDSGGPH VTRFKNTYYV TGIVSWGEGC ARKGKYGIYT
460 470 480
KVTTFLKWID RSMKARVGPT AETPRTAGPP N
Length:481
Mass (Da):54,018
Last modified:November 1, 1998 - v1
Checksum:i8AC09DE5EF9D271E
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti250I → V in AAH03877 (PubMed:15489334).Curated1
Sequence conflicti294E → D in CAA10933 (PubMed:9783672).Curated1
Sequence conflicti298M → L in CAA10933 (PubMed:9783672).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF087644 mRNA. Translation: AAC36345.1.
AJ222677 mRNA. Translation: CAA10933.1.
AF211347 Genomic DNA. Translation: AAF22980.1.
BC003877 mRNA. Translation: AAH03877.1.
CCDSiCCDS40226.1.
RefSeqiNP_031998.3. NM_007972.4.
UniGeneiMm.262589.

Genome annotation databases

EnsembliENSMUST00000063820; ENSMUSP00000068389; ENSMUSG00000031444.
GeneIDi14058.
KEGGimmu:14058.
UCSCiuc009kws.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF087644 mRNA. Translation: AAC36345.1.
AJ222677 mRNA. Translation: CAA10933.1.
AF211347 Genomic DNA. Translation: AAF22980.1.
BC003877 mRNA. Translation: AAH03877.1.
CCDSiCCDS40226.1.
RefSeqiNP_031998.3. NM_007972.4.
UniGeneiMm.262589.

3D structure databases

ProteinModelPortaliO88947.
SMRiO88947.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO88947. 2 interactors.
MINTiMINT-6597397.
STRINGi10090.ENSMUSP00000033821.

Protein family/group databases

MEROPSiS01.216.

PTM databases

iPTMnetiO88947.
PhosphoSitePlusiO88947.

Proteomic databases

PaxDbiO88947.
PeptideAtlasiO88947.
PRIDEiO88947.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000063820; ENSMUSP00000068389; ENSMUSG00000031444.
GeneIDi14058.
KEGGimmu:14058.
UCSCiuc009kws.2. mouse.

Organism-specific databases

CTDi2159.
MGIiMGI:103107. F10.

Phylogenomic databases

eggNOGiENOG410IGPV. Eukaryota.
COG5640. LUCA.
GeneTreeiENSGT00760000118890.
HOGENOMiHOG000251821.
HOVERGENiHBG013304.
InParanoidiO88947.
KOiK01314.
TreeFamiTF327329.

Enzyme and pathway databases

ReactomeiR-MMU-140834. Extrinsic Pathway of Fibrin Clot Formation.
R-MMU-140837. Intrinsic Pathway of Fibrin Clot Formation.
R-MMU-140875. Common Pathway of Fibrin Clot Formation.
R-MMU-159740. Gamma-carboxylation of protein precursors.
R-MMU-159763. Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
R-MMU-159782. Removal of aminoterminal propeptides from gamma-carboxylated proteins.

Miscellaneous databases

PROiO88947.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000031444.
CleanExiMM_F10.
ExpressionAtlasiO88947. baseline and differential.
GenevisibleiO88947. MM.

Family and domain databases

CDDicd00190. Tryp_SPc. 1 hit.
Gene3Di4.10.740.10. 1 hit.
InterProiIPR017857. Coagulation_fac_subgr_Gla_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR000294. GLA_domain.
IPR012224. Pept_S1A_FX.
IPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[Graphical view]
PfamiPF00008. EGF. 1 hit.
PF00594. Gla. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFiPIRSF001143. Factor_X. 1 hit.
PRINTSiPR00722. CHYMOTRYPSIN.
PR00001. GLABLOOD.
SMARTiSM00181. EGF. 2 hits.
SM00179. EGF_CA. 1 hit.
SM00069. GLA. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 2 hits.
SSF57630. SSF57630. 1 hit.
PROSITEiPS00010. 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]
ProtoNetiSearch...

Entry informationi

Entry nameiFA10_MOUSE
AccessioniPrimary (citable) accession number: O88947
Secondary accession number(s): O54740, Q99L32
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: November 1, 1998
Last modified: November 2, 2016
This is version 155 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.