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O88947

- FA10_MOUSE

UniProt

O88947 - FA10_MOUSE

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Protein

Coagulation factor X

Gene

F10

Organism
Mus musculus (Mouse)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei273 – 2731Charge relay systemBy similarity
Active sitei319 – 3191Charge relay systemBy similarity
Active sitei416 – 4161Charge relay systemBy similarity

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. phospholipid binding Source: Ensembl
  3. serine-type endopeptidase activity Source: Ensembl

GO - Biological processi

  1. blood coagulation Source: UniProtKB-KW
  2. positive regulation of protein kinase B signaling Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Blood coagulation, Hemostasis

Keywords - Ligandi

Calcium

Enzyme and pathway databases

ReactomeiREACT_239392. Intrinsic Pathway.
REACT_240293. Extrinsic Pathway.
REACT_245393. Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
REACT_254191. Gamma-carboxylation of protein precursors.
REACT_255710. Removal of aminoterminal propeptides from gamma-carboxylated proteins.
REACT_259461. Common Pathway.

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
ProteomesiUP000000589: Chromosome 8

Organism-specific databases

MGIiMGI:103107. F10.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
  2. intracellular membrane-bounded organelle Source: Ensembl
  3. membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence AnalysisAdd
BLAST
Propeptidei21 – 4020By similarityPRO_0000027792Add
BLAST
Chaini41 – 481441Coagulation factor XPRO_0000027793Add
BLAST
Chaini41 – 180140Factor X light chainBy similarityPRO_0000027794Add
BLAST
Chaini184 – 481298Factor X heavy chainBy similarityPRO_0000027795Add
BLAST
Propeptidei184 – 23148Activation peptideBy similarityPRO_0000027796Add
BLAST
Chaini232 – 481250Activated factor Xa heavy chainBy similarityPRO_0000027797Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei46 – 4614-carboxyglutamatePROSITE-ProRule annotation
Modified residuei47 – 4714-carboxyglutamatePROSITE-ProRule annotation
Modified residuei54 – 5414-carboxyglutamatePROSITE-ProRule annotation
Modified residuei56 – 5614-carboxyglutamatePROSITE-ProRule annotation
Disulfide bondi57 ↔ 62By similarity
Modified residuei59 – 5914-carboxyglutamatePROSITE-ProRule annotation
Modified residuei60 – 6014-carboxyglutamatePROSITE-ProRule annotation
Modified residuei65 – 6514-carboxyglutamatePROSITE-ProRule annotation
Modified residuei66 – 6614-carboxyglutamatePROSITE-ProRule annotation
Modified residuei69 – 6914-carboxyglutamatePROSITE-ProRule annotation
Modified residuei72 – 7214-carboxyglutamatePROSITE-ProRule annotation
Modified residuei75 – 7514-carboxyglutamatePROSITE-ProRule annotation
Modified residuei79 – 7914-carboxyglutamatePROSITE-ProRule annotation
Disulfide bondi90 ↔ 101By similarity
Disulfide bondi95 ↔ 110By similarity
Modified residuei103 – 1031(3R)-3-hydroxyaspartateBy similarity
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
Glycosylationi187 – 1871N-linked (GlcNAc...)1 Publication
Glycosylationi218 – 2181N-linked (GlcNAc...)Sequence Analysis
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

MaxQBiO88947.
PaxDbiO88947.
PRIDEiO88947.

PTM databases

PhosphoSiteiO88947.

Expressioni

Tissue specificityi

Plasma; synthesized in the liver.

Gene expression databases

BgeeiO88947.
CleanExiMM_F10.
ExpressionAtlasiO88947. baseline and differential.
GenevestigatoriO88947.

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 interactions.
MINTiMINT-6597397.

Structurei

3D structure databases

ProteinModelPortaliO88947.
SMRiO88947. Positions 41-464.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini41 – 8545GlaPROSITE-ProRule annotationAdd
BLAST
Domaini86 – 12237EGF-like 1; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini125 – 16541EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini232 – 464233Peptidase S1PROSITE-ProRule annotationAdd
BLAST

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

eggNOGiCOG5640.
HOGENOMiHOG000251821.
HOVERGENiHBG013304.
InParanoidiO88947.
KOiK01314.
OrthoDBiEOG75B84T.
TreeFamiTF327329.

Family and domain databases

Gene3Di4.10.740.10. 1 hit.
InterProiIPR017857. Coagulation_fac_subgr_Gla_dom.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
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]
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. 1 hit.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti250 – 2501I → V in AAH03877. (PubMed:15489334)Curated
Sequence conflicti294 – 2941E → D in CAA10933. (PubMed:9783672)Curated
Sequence conflicti298 – 2981M → L in CAA10933. (PubMed:9783672)Curated

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 .
CCDSi CCDS40226.1.
RefSeqi NP_031998.3. NM_007972.4.
UniGenei Mm.262589.

3D structure databases

ProteinModelPortali O88947.
SMRi O88947. Positions 41-464.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi O88947. 2 interactions.
MINTi MINT-6597397.

Protein family/group databases

MEROPSi S01.216.

PTM databases

PhosphoSitei O88947.

Proteomic databases

MaxQBi O88947.
PaxDbi O88947.
PRIDEi O88947.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000063820 ; ENSMUSP00000068389 ; ENSMUSG00000031444 .
GeneIDi 14058.
KEGGi mmu:14058.
UCSCi uc009kws.2. mouse.

Organism-specific databases

CTDi 2159.
MGIi MGI:103107. F10.

Phylogenomic databases

eggNOGi COG5640.
HOGENOMi HOG000251821.
HOVERGENi HBG013304.
InParanoidi O88947.
KOi K01314.
OrthoDBi EOG75B84T.
TreeFami TF327329.

Enzyme and pathway databases

Reactomei REACT_239392. Intrinsic Pathway.
REACT_240293. Extrinsic Pathway.
REACT_245393. Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
REACT_254191. Gamma-carboxylation of protein precursors.
REACT_255710. Removal of aminoterminal propeptides from gamma-carboxylated proteins.
REACT_259461. Common Pathway.

Miscellaneous databases

NextBioi 285020.
PROi O88947.
SOURCEi Search...

Gene expression databases

Bgeei O88947.
CleanExi MM_F10.
ExpressionAtlasi O88947. baseline and differential.
Genevestigatori O88947.

Family and domain databases

Gene3Di 4.10.740.10. 1 hit.
InterProi IPR017857. Coagulation_fac_subgr_Gla_dom.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
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 ]
Pfami PF00008. EGF. 1 hit.
PF00594. Gla. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view ]
PIRSFi PIRSF001143. Factor_X. 1 hit.
PRINTSi PR00722. CHYMOTRYPSIN.
PR00001. GLABLOOD.
SMARTi SM00181. EGF. 1 hit.
SM00179. EGF_CA. 1 hit.
SM00069. GLA. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view ]
SUPFAMi SSF50494. SSF50494. 2 hits.
SSF57630. SSF57630. 1 hit.
PROSITEi 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    Strain: C57BL/6.
    Tissue: Plasma.

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 26, 2014
This is version 135 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

External Data

Dasty 3