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O88947

- FA10_MOUSE

UniProt

O88947 - FA10_MOUSE

Protein

Coagulation factor X

Gene

F10

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 1 (01 Nov 1998)
      Previous versions | rss
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    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. serine-type endopeptidase activity Source: InterPro

    GO - Biological processi

    1. blood coagulation Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Keywords - Biological processi

    Blood coagulation, Hemostasis

    Keywords - Ligandi

    Calcium

    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-SubCell

    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

    ArrayExpressiO88947.
    BgeeiO88947.
    CleanExiMM_F10.
    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

    MGSPVQLSLL CVVLASLLLP GKGVFINRER ANNVLARTRR ANSFFEEFKK    50
    GNLERECMEE ICSYEEVREI FEDDEKTKEY WTKYKDGDQC ESSPCQNQGA 100
    CRDGIGGYTC TCSEGFEGKN CELFVRKLCR LDNGDCDQFC REEQNSVVCS 150
    CASGYFLGND GKSCISTAPF PCGKITTGRR KRSVALNTSD SELDLEDALL 200
    DEDFLSPTEN PIELLNLNET QPERSSDDLV RIVGGRECKD GECPWQALLI 250
    NEDNEGFCGG TILNEFYILT AAHCLHQARR FKVRVGDRNT EKEEGNEMVH 300
    EVDVVIKHNK FQRDTYDYDI AVLRLKTPIT FRMNVAPACL PQKDWAESTL 350
    MTQKTGIVSG FGRTHEKGRQ SNILKMLEVP YVDRNTCKLS TSFSITQNMF 400
    CAGYEAKLED ACQGDSGGPH VTRFKNTYYV TGIVSWGEGC ARKGKYGIYT 450
    KVTTFLKWID RSMKARVGPT AETPRTAGPP N 481
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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.

    Miscellaneous databases

    NextBioi 285020.
    PROi O88947.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O88947.
    Bgeei O88947.
    CleanExi MM_F10.
    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

    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: October 1, 2014
    This is version 133 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