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O88947 (FA10_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Coagulation factor X
EC=3.4.21.6
Alternative name(s):
Stuart factor

Cleaved into the following 3 chains:

  1. Factor X light chain
  2. Factor X heavy chain
  3. Activated factor Xa heavy chain
Gene names
Name:F10
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length481 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (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.

Enzyme regulation

Inhibited by SERPINA5 By similarity.

Subunit structure

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.

Subcellular location

Secreted.

Tissue specificity

Plasma; synthesized in the liver.

Post-translational modification

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.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Propeptide21 – 4020 By similarity
PRO_0000027792
Chain41 – 481441Coagulation factor X
PRO_0000027793
Chain41 – 180140Factor X light chain By similarity
PRO_0000027794
Chain184 – 481298Factor X heavy chain By similarity
PRO_0000027795
Propeptide184 – 23148Activation peptide By similarity
PRO_0000027796
Chain232 – 481250Activated factor Xa heavy chain By similarity
PRO_0000027797

Regions

Domain41 – 8545Gla
Domain86 – 12237EGF-like 1; calcium-binding Potential
Domain125 – 16541EGF-like 2
Domain232 – 464233Peptidase S1

Sites

Active site2731Charge relay system By similarity
Active site3191Charge relay system By similarity
Active site4161Charge relay system By similarity

Amino acid modifications

Modified residue4614-carboxyglutamate By similarity
Modified residue4714-carboxyglutamate By similarity
Modified residue5414-carboxyglutamate By similarity
Modified residue5614-carboxyglutamate By similarity
Modified residue5914-carboxyglutamate By similarity
Modified residue6014-carboxyglutamate By similarity
Modified residue6514-carboxyglutamate By similarity
Modified residue6614-carboxyglutamate By similarity
Modified residue6914-carboxyglutamate By similarity
Modified residue7214-carboxyglutamate By similarity
Modified residue7514-carboxyglutamate By similarity
Modified residue7914-carboxyglutamate By similarity
Modified residue1031(3R)-3-hydroxyaspartate By similarity
Glycosylation1871N-linked (GlcNAc...) Ref.5
Glycosylation2181N-linked (GlcNAc...) Potential
Disulfide bond57 ↔ 62 By similarity
Disulfide bond90 ↔ 101 By similarity
Disulfide bond95 ↔ 110 By similarity
Disulfide bond112 ↔ 121 By similarity
Disulfide bond129 ↔ 140 By similarity
Disulfide bond136 ↔ 149 By similarity
Disulfide bond151 ↔ 164 By similarity
Disulfide bond172 ↔ 339Interchain (between light and heavy chains) By similarity
Disulfide bond238 ↔ 243 By similarity
Disulfide bond258 ↔ 274 By similarity
Disulfide bond387 ↔ 401 By similarity
Disulfide bond412 ↔ 440 By similarity

Experimental info

Sequence conflict2501I → V in AAH03877. Ref.4
Sequence conflict2941E → D in CAA10933. Ref.2
Sequence conflict2981M → L in CAA10933. Ref.2

Sequences

Sequence LengthMass (Da)Tools
O88947 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 8AC09DE5EF9D271E

FASTA48154,018
        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

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of a cDNA encoding murine coagulation factor X."
Liang Z., Cooper A., DeFord M.E., Carmeliet P., Collen D., Castellino F.J., Rosen E.D.
Thromb. Haemost. 80:87-91(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6 X CBA.
Tissue: Liver.
[2]"Cloning and recombinant expression of mouse coagulation factor X."
Heidtmann H.H., Kontermann R.E.
Thromb. Res. 92:33-41(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[3]"Cloning and characterization of the murine coagulation factor X gene."
Cooper A., Liang Z., Castellino F.J., Rosen E.D.
Thromb. Haemost. 83:732-735(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 129/SvJ.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"Proteome-wide characterization of N-glycosylation events by diagonal chromatography."
Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.
J. Proteome Res. 5:2438-2447(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-187, MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Plasma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF087644 mRNA. Translation: AAC36345.1.
AJ222677 mRNA. Translation: CAA10933.1.
AF211347 Genomic DNA. Translation: AAF22980.1.
BC003877 mRNA. Translation: AAH03877.1.
IPIIPI00331551.
RefSeqNP_031998.3. NM_007972.4.
UniGeneMm.262589.

3D structure databases

ProteinModelPortalO88947.
SMRO88947. Positions 41-176, 189-464.
ModBaseSearch...

Protein-protein interaction databases

IntActO88947. 2 interactions.

Protein family/group databases

MEROPSS01.216.

PTM databases

PhosphoSiteO88947.

Proteomic databases

PaxDbO88947.
PRIDEO88947.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000063820; ENSMUSP00000068389; ENSMUSG00000031444.
GeneID14058.
KEGGmmu:14058.

Organism-specific databases

CTD2159.
MGIMGI:103107. F10.

Phylogenomic databases

eggNOGCOG5640.
HOGENOMHOG000251821.
HOVERGENHBG013304.
InParanoidO88947.
KOK01314.

Gene expression databases

ArrayExpressO88947.
BgeeO88947.
CleanExMM_F10.
GenevestigatorO88947.
GermOnlineENSMUSG00000031444. Mus musculus.

Family and domain databases

Gene3D4.10.740.10. 1 hit.
InterProIPR017857. Coagulation_fac_subgr_Gla_dom.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR000294. GLA_domain.
IPR012224. Pept_S1A_FX.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamPF00008. EGF. 1 hit.
PF00594. Gla. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFPIRSF001143. Factor_X. 1 hit.
PRINTSPR00722. CHYMOTRYPSIN.
PR00001. GLABLOOD.
SMARTSM00181. EGF. 1 hit.
SM00179. EGF_CA. 1 hit.
SM00069. GLA. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50494. Pept_Ser_Cys. 1 hit.
SSF57630. VitK_dep_GLA. 1 hit.
PROSITEPS00010. 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]
ProtoNetSearch...

Other

NextBio285020.
SOURCESearch...

Entry information

Entry nameFA10_MOUSE
AccessionPrimary (citable) accession number: O88947
Secondary accession number(s): O54740, Q99L32
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: November 1, 1998
Last modified: May 1, 2013
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

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