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P00742

- FA10_HUMAN

UniProt

P00742 - FA10_HUMAN

Protein

Coagulation factor X

Gene

F10

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 206 (01 Oct 2014)
      Sequence version 2 (01 Oct 1989)
      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 and SERPINA10.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei276 – 2761Charge relay system
    Active sitei322 – 3221Charge relay system
    Active sitei419 – 4191Charge relay system

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. phospholipid binding Source: BHF-UCL
    3. protein binding Source: UniProtKB
    4. serine-type endopeptidase activity Source: BHF-UCL

    GO - Biological processi

    1. blood coagulation Source: BHF-UCL
    2. blood coagulation, extrinsic pathway Source: Reactome
    3. blood coagulation, intrinsic pathway Source: Reactome
    4. cellular protein metabolic process Source: Reactome
    5. peptidyl-glutamic acid carboxylation Source: Reactome
    6. positive regulation of cell migration Source: BHF-UCL
    7. positive regulation of protein kinase B signaling Source: BHF-UCL
    8. post-translational protein modification Source: Reactome
    9. proteolysis Source: Reactome

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Keywords - Biological processi

    Blood coagulation, Hemostasis

    Keywords - Ligandi

    Calcium

    Enzyme and pathway databases

    BioCyciMetaCyc:HS05000-MONOMER.
    ReactomeiREACT_1050. Gamma-carboxylation of protein precursors.
    REACT_1439. Common Pathway.
    REACT_1573. Extrinsic Pathway.
    REACT_1906. Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
    REACT_326. Intrinsic Pathway.
    REACT_733. Removal of aminoterminal propeptides from gamma-carboxylated proteins.
    SABIO-RKP00742.

    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
    Stuart-Prower factor
    Cleaved into the following 3 chains:
    Gene namesi
    Name:F10
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 13

    Organism-specific databases

    HGNCiHGNC:3528. F10.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum lumen Source: Reactome
    2. extracellular region Source: UniProtKB
    3. Golgi lumen Source: Reactome
    4. intrinsic component of external side of plasma membrane Source: BHF-UCL
    5. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Factor X deficiency (FA10D) [MIM:227600]: A hemorrhagic disease with variable presentation. Affected individuals can manifest prolonged nasal and mucosal hemorrhage, menorrhagia, hematuria, and occasionally hemarthrosis. Some patients do not have clinical bleeding diathesis.16 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti47 – 471E → G in FA10D; St. Louis II; strongly reduced activity; not activated by factor VIIa and tissue factor. 1 Publication
    VAR_065428
    Natural varianti51 – 511G → V in FA10D. 1 Publication
    VAR_065429
    Natural varianti54 – 541E → G in FA10D; Ketchikan. 1 Publication
    VAR_065430
    Natural varianti54 – 541E → K in FA10D; Vorarlberg; converts prothrombin at a normal rate but shows decreased affinity for calcium. 2 Publications
    VAR_065431
    Natural varianti72 – 721E → Q in FA10D; Tokyo. 1 Publication
    VAR_065432
    Natural varianti91 – 911E → K in FA10D; Riyadh. 1 Publication
    VAR_065433
    Natural varianti142 – 1421E → K in FA10D; uncertain pathological significance; detected in patients carrying K-54 or P-374; slightly reduced activity. 2 Publications
    Corresponds to variant rs61753266 [ dbSNP | Ensembl ].
    VAR_065434
    Natural varianti149 – 1491C → Y in FA10D. 1 Publication
    VAR_065435
    Natural varianti151 – 1511C → Y in FA10D. 1 Publication
    VAR_065436
    Natural varianti289 – 2891G → R in FA10D; may affect splicing. 1 Publication
    VAR_065437
    Natural varianti304 – 3041E → K in FA10D. 1 Publication
    VAR_065438
    Natural varianti322 – 3221D → N in FA10D; Stockton; 50% decrease in specific activity. 1 Publication
    VAR_065439
    Natural varianti327 – 3271R → W in FA10D. 1 Publication
    VAR_065440
    Natural varianti338 – 3381V → M in FA10D. 1 Publication
    VAR_065441
    Natural varianti350 – 3501E → K in FA10D. 1 Publication
    VAR_065442
    Natural varianti358 – 3581T → M in FA10D; Roma. 1 Publication
    VAR_065443
    Natural varianti363 – 3631G → S in FA10D. 1 Publication
    VAR_065444
    Natural varianti366 – 3661R → C in FA10D; San Antonio. 1 Publication
    VAR_065445
    Natural varianti374 – 3741S → P in FA10D; Marseille; decreased cleavage by factor IXa; normal catalytic efficiency for prothrombin. 3 Publications
    VAR_065446
    Natural varianti383 – 3831P → S in FA10D; Friuli. 1 Publication
    VAR_065447
    Natural varianti390 – 3901C → F in FA10D; Padua 4. 1 Publication
    Corresponds to variant rs199778916 [ dbSNP | Ensembl ].
    VAR_065448
    Natural varianti404 – 4041C → R in FA10D. 1 Publication
    VAR_065449
    Natural varianti406 – 4061G → S in FA10D; almost complete loss of activity. 1 Publication
    VAR_065450
    Natural varianti420 – 4201G → R in FA10D; Padua 3. 1 Publication
    VAR_065451
    Natural varianti448 – 4481K → N in FA10D; San Giovanni Rotondo. 1 Publication
    VAR_065452

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi227600. phenotype.
    Orphaneti328. Congenital factor X deficiency.
    PharmGKBiPA27940.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3131Sequence AnalysisAdd
    BLAST
    Propeptidei32 – 4091 PublicationPRO_0000027786
    Chaini41 – 488448Coagulation factor XPRO_0000027787Add
    BLAST
    Chaini41 – 179139Factor X light chainPRO_0000027788Add
    BLAST
    Chaini183 – 488306Factor X heavy chainPRO_0000027789Add
    BLAST
    Propeptidei183 – 23452Activation peptidePRO_0000027790Add
    BLAST
    Chaini235 – 488254Activated factor Xa heavy chainPRO_0000027791Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei46 – 4614-carboxyglutamate1 PublicationPROSITE-ProRule annotation
    Modified residuei47 – 4714-carboxyglutamate1 PublicationPROSITE-ProRule annotation
    Modified residuei54 – 5414-carboxyglutamate1 PublicationPROSITE-ProRule annotation
    Modified residuei56 – 5614-carboxyglutamate1 PublicationPROSITE-ProRule annotation
    Disulfide bondi57 ↔ 62By similarity
    Modified residuei59 – 5914-carboxyglutamate1 PublicationPROSITE-ProRule annotation
    Modified residuei60 – 6014-carboxyglutamate1 PublicationPROSITE-ProRule annotation
    Modified residuei65 – 6514-carboxyglutamate1 PublicationPROSITE-ProRule annotation
    Modified residuei66 – 6614-carboxyglutamate1 PublicationPROSITE-ProRule annotation
    Modified residuei69 – 6914-carboxyglutamate1 PublicationPROSITE-ProRule annotation
    Modified residuei72 – 7214-carboxyglutamate1 PublicationPROSITE-ProRule annotation
    Modified residuei79 – 7914-carboxyglutamate1 PublicationPROSITE-ProRule annotation
    Disulfide bondi90 ↔ 101
    Disulfide bondi95 ↔ 110
    Modified residuei103 – 1031(3R)-3-hydroxyaspartate1 Publication
    Disulfide bondi112 ↔ 121
    Disulfide bondi129 ↔ 140
    Disulfide bondi136 ↔ 149
    Disulfide bondi151 ↔ 164
    Disulfide bondi172 ↔ 342Interchain (between light and heavy chains)
    Glycosylationi199 – 1991O-linked (GalNAc...)2 Publications
    Glycosylationi211 – 2111O-linked (GalNAc...)2 Publications
    Glycosylationi221 – 2211N-linked (GlcNAc...)2 PublicationsCAR_000012
    Glycosylationi231 – 2311N-linked (GlcNAc...)2 PublicationsCAR_000013
    Disulfide bondi241 ↔ 246
    Disulfide bondi261 ↔ 277
    Disulfide bondi390 ↔ 404
    Disulfide bondi415 ↔ 443

    Post-translational modificationi

    The vitamin K-dependent, enzymatic carboxylation of some glutamate residues allows the modified protein to bind calcium.
    N- and O-glycosylated. O-glycosylated with core 1 or possibly core 8 glycans.2 Publications
    The activation peptide is cleaved by factor IXa (in the intrinsic pathway), or by factor VIIa (in the extrinsic pathway).
    The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.1 Publication

    Keywords - PTMi

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

    Proteomic databases

    MaxQBiP00742.
    PaxDbiP00742.
    PRIDEiP00742.

    PTM databases

    PhosphoSiteiP00742.
    UniCarbKBiP00742.

    Miscellaneous databases

    PMAP-CutDBP00742.

    Expressioni

    Tissue specificityi

    Plasma; synthesized in the liver.1 Publication

    Gene expression databases

    ArrayExpressiP00742.
    BgeeiP00742.
    CleanExiHS_F10.
    GenevestigatoriP00742.

    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.

    Protein-protein interaction databases

    BioGridi108457. 9 interactions.
    DIPiDIP-29896N.
    IntActiP00742. 7 interactions.
    MINTiMINT-276128.
    STRINGi9606.ENSP00000364709.

    Structurei

    Secondary structure

    1
    488
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi47 – 5711
    Helixi64 – 718
    Helixi74 – 818
    Turni89 – 924
    Beta strandi96 – 983
    Beta strandi100 – 1023
    Beta strandi105 – 1073
    Beta strandi109 – 1113
    Beta strandi116 – 1183
    Beta strandi123 – 1253
    Turni129 – 1313
    Helixi132 – 1354
    Beta strandi137 – 1437
    Beta strandi146 – 1505
    Beta strandi155 – 1573
    Beta strandi164 – 1707
    Beta strandi172 – 1743
    Beta strandi236 – 2405
    Turni243 – 2453
    Beta strandi249 – 2535
    Turni255 – 2573
    Beta strandi259 – 2657
    Beta strandi267 – 2737
    Helixi275 – 2795
    Beta strandi280 – 2834
    Beta strandi285 – 2895
    Beta strandi291 – 2955
    Beta strandi301 – 3033
    Beta strandi305 – 3106
    Turni316 – 3194
    Beta strandi324 – 3307
    Helixi346 – 3527
    Turni353 – 3553
    Beta strandi356 – 3649
    Beta strandi366 – 3683
    Beta strandi372 – 3765
    Beta strandi378 – 3858
    Helixi387 – 3937
    Beta strandi402 – 4065
    Beta strandi408 – 4114
    Turni416 – 4205
    Beta strandi422 – 4276
    Beta strandi430 – 43910
    Beta strandi441 – 4444
    Beta strandi450 – 4545
    Helixi455 – 4584
    Helixi459 – 4657
    Beta strandi471 – 4733

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1C5MX-ray1.95D235-488[»]
    F84-179[»]
    1EZQX-ray2.20A235-488[»]
    B46-179[»]
    1F0RX-ray2.10A235-488[»]
    B46-179[»]
    1F0SX-ray2.10A235-488[»]
    B46-179[»]
    1FAXX-ray3.00A235-488[»]
    L84-179[»]
    1FJSX-ray1.92A235-468[»]
    L127-178[»]
    1FXYX-ray2.15A235-344[»]
    1G2LX-ray1.90A235-469[»]
    B86-179[»]
    1G2MX-ray3.02A235-469[»]
    B86-179[»]
    1HCGX-ray2.20A235-475[»]
    B129-179[»]
    1IOEX-ray2.90A235-469[»]
    L84-179[»]
    1IQEX-ray2.90A235-469[»]
    L84-179[»]
    1IQFX-ray3.20A235-469[»]
    L84-179[»]
    1IQGX-ray2.60A235-469[»]
    L84-179[»]
    1IQHX-ray3.00A235-469[»]
    L84-179[»]
    1IQIX-ray2.90A235-469[»]
    L84-179[»]
    1IQJX-ray3.00A235-469[»]
    L84-179[»]
    1IQKX-ray3.20A235-469[»]
    L84-179[»]
    1IQLX-ray2.70A235-469[»]
    L84-179[»]
    1IQMX-ray2.60A235-469[»]
    L84-179[»]
    1IQNX-ray2.60A235-469[»]
    L84-179[»]
    1KSNX-ray2.10A235-488[»]
    B46-179[»]
    1LPGX-ray2.00A46-179[»]
    B235-488[»]
    1LPKX-ray2.20A46-179[»]
    B235-488[»]
    1LPZX-ray2.40A46-179[»]
    B235-488[»]
    1LQDX-ray2.70A46-179[»]
    B235-488[»]
    1MQ5X-ray2.10A235-467[»]
    L127-177[»]
    1MQ6X-ray2.10A235-467[»]
    L127-177[»]
    1MSXmodel-A235-469[»]
    1NFUX-ray2.05A235-488[»]
    B46-240[»]
    1NFWX-ray2.10A235-488[»]
    B46-179[»]
    1NFXX-ray2.15A235-488[»]
    B46-179[»]
    1NFYX-ray2.10A235-488[»]
    B46-179[»]
    1NL8model-F235-469[»]
    L41-179[»]
    1P0SX-ray2.80H235-488[»]
    L41-178[»]
    1V3XX-ray2.20A235-467[»]
    B127-178[»]
    1WU1X-ray2.30A235-467[»]
    B85-179[»]
    1XKAX-ray2.30C235-469[»]
    L85-179[»]
    1XKBX-ray2.40A/B85-179[»]
    C/D235-469[»]
    1Z6EX-ray1.80A235-468[»]
    L127-178[»]
    2BMGX-ray2.70A126-178[»]
    B235-468[»]
    2BOHX-ray2.20A46-179[»]
    B235-488[»]
    2BOKX-ray1.64A235-475[»]
    L126-180[»]
    2BQ6X-ray3.00A126-177[»]
    B220-468[»]
    2BQ7X-ray2.20A126-177[»]
    B220-468[»]
    2BQWX-ray2.95A126-177[»]
    B220-468[»]
    2CJIX-ray2.10A235-488[»]
    B46-179[»]
    2D1JX-ray2.20A235-467[»]
    B125-178[»]
    2EI6X-ray2.30A235-467[»]
    B125-178[»]
    2EI7X-ray2.30A235-467[»]
    B125-178[»]
    2EI8X-ray2.10A235-467[»]
    B125-178[»]
    2FZZX-ray2.20A235-468[»]
    L127-178[»]
    2G00X-ray2.10A235-468[»]
    L127-178[»]
    2GD4X-ray3.30A/L126-182[»]
    B/H235-475[»]
    2H9EX-ray2.20H235-467[»]
    L86-234[»]
    2J2UX-ray1.90A235-488[»]
    B46-179[»]
    2J34X-ray2.01A235-488[»]
    B46-179[»]
    2J38X-ray2.10A235-488[»]
    B46-179[»]
    2J4IX-ray1.80A235-488[»]
    B46-179[»]
    2J94X-ray2.10A235-488[»]
    B46-179[»]
    2J95X-ray2.01A235-488[»]
    B46-179[»]
    2JKHX-ray1.25A235-475[»]
    L126-180[»]
    2P16X-ray2.30A235-468[»]
    L127-178[»]
    2P3FX-ray3.10H235-469[»]
    L125-178[»]
    2P3TX-ray1.92A127-178[»]
    B235-467[»]
    2P3UX-ray1.62A127-178[»]
    B235-467[»]
    2P93X-ray1.90A235-468[»]
    L127-178[»]
    2P94X-ray1.80A235-468[»]
    L127-178[»]
    2P95X-ray2.20A235-468[»]
    L127-178[»]
    2PHBX-ray2.30A235-468[»]
    B128-178[»]
    2PR3X-ray1.50A235-468[»]
    B128-178[»]
    2Q1JX-ray1.90A235-468[»]
    B128-178[»]
    2RA0X-ray2.30A235-468[»]
    L128-178[»]
    2UWLX-ray1.90A235-488[»]
    B46-179[»]
    2UWOX-ray1.75A235-488[»]
    B46-179[»]
    2UWPX-ray1.75A235-488[»]
    B46-179[»]
    2VH0X-ray1.70A235-488[»]
    B46-179[»]
    2VH6X-ray1.95A235-488[»]
    B46-177[»]
    2VVCX-ray1.95A/B235-475[»]
    K/L126-180[»]
    2VVUX-ray2.30A235-475[»]
    L126-180[»]
    2VVVX-ray1.73A235-475[»]
    L126-180[»]
    2VWLX-ray1.80A235-475[»]
    L126-180[»]
    2VWMX-ray1.96A/B235-475[»]
    K/L126-180[»]
    2VWNX-ray1.61A235-475[»]
    L126-180[»]
    2VWOX-ray1.60A235-475[»]
    L126-180[»]
    2W26X-ray2.08A235-468[»]
    B129-177[»]
    2W3IX-ray1.90A235-468[»]
    B128-178[»]
    2W3KX-ray2.05A235-468[»]
    B128-178[»]
    2WYGX-ray1.88A235-487[»]
    B46-179[»]
    2WYJX-ray2.38A235-488[»]
    B46-179[»]
    2XBVX-ray1.66A235-475[»]
    L126-180[»]
    2XBWX-ray1.72A235-475[»]
    L126-180[»]
    2XBXX-ray1.85A235-475[»]
    L126-180[»]
    2XBYX-ray2.02A235-475[»]
    L126-180[»]
    2XC0X-ray2.05A235-475[»]
    L126-180[»]
    2XC4X-ray1.67A235-475[»]
    L126-180[»]
    2XC5X-ray1.70A235-475[»]
    L126-180[»]
    2Y5FX-ray1.29A235-468[»]
    L127-180[»]
    2Y5GX-ray1.29A235-468[»]
    L127-180[»]
    2Y5HX-ray1.33A235-468[»]
    L127-180[»]
    2Y7XX-ray1.90A235-488[»]
    B46-179[»]
    2Y7ZX-ray1.84A235-488[»]
    B46-179[»]
    2Y80X-ray1.90A235-488[»]
    B46-179[»]
    2Y81X-ray1.70A235-488[»]
    B46-179[»]
    2Y82X-ray2.20A235-488[»]
    B46-179[»]
    3CENX-ray1.60A235-468[»]
    L127-178[»]
    3CS7X-ray2.20A235-468[»]
    L127-178[»]
    3ENSX-ray2.30A/C85-178[»]
    B/D235-472[»]
    3FFGX-ray1.54A235-468[»]
    L127-178[»]
    3HPTX-ray2.19A/C85-178[»]
    B/D235-472[»]
    3IITX-ray1.80A235-467[»]
    B125-178[»]
    3K9XX-ray1.90A/C85-178[»]
    B/D235-472[»]
    3KL6X-ray1.45A235-475[»]
    B126-179[»]
    3KQBX-ray2.25A235-468[»]
    L127-178[»]
    3KQCX-ray2.20A235-468[»]
    L127-178[»]
    3KQDX-ray2.75A235-468[»]
    L127-178[»]
    3KQEX-ray2.35A235-468[»]
    L127-178[»]
    3LIWX-ray2.22A235-468[»]
    B128-178[»]
    3M36X-ray2.15A235-468[»]
    L127-178[»]
    3M37X-ray1.90A235-468[»]
    L127-178[»]
    3Q3KX-ray2.00A235-467[»]
    B125-178[»]
    3SW2X-ray2.42A85-178[»]
    B235-472[»]
    3TK5X-ray2.20A235-467[»]
    B125-178[»]
    3TK6X-ray1.80A235-467[»]
    B125-178[»]
    4A7IX-ray2.40A84-179[»]
    B235-488[»]
    4BTIX-ray2.30A/E84-179[»]
    B/F235-488[»]
    4BTTX-ray2.59A/E84-179[»]
    B/F235-488[»]
    4BTUX-ray2.37A/E84-179[»]
    B/F235-488[»]
    ProteinModelPortaliP00742.
    SMRiP00742. Positions 43-180, 235-466.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00742.

    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
    Domaini235 – 467233Peptidase S1PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni183 – 20321O-glycosylated at one siteAdd
    BLAST
    Regioni476 – 48510O-glycosylated at one site

    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.
    InParanoidiP00742.
    KOiK01314.
    OMAiEMAHEVE.
    PhylomeDBiP00742.
    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.

    P00742-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGRPLHLVLL SASLAGLLLL GESLFIRREQ ANNILARVTR ANSFLEEMKK    50
    GHLERECMEE TCSYEEAREV FEDSDKTNEF WNKYKDGDQC ETSPCQNQGK 100
    CKDGLGEYTC TCLEGFEGKN CELFTRKLCS LDNGDCDQFC HEEQNSVVCS 150
    CARGYTLADN GKACIPTGPY PCGKQTLERR KRSVAQATSS SGEAPDSITW 200
    KPYDAADLDP TENPFDLLDF NQTQPERGDN NLTRIVGGQE CKDGECPWQA 250
    LLINEENEGF CGGTILSEFY ILTAAHCLYQ AKRFKVRVGD RNTEQEEGGE 300
    AVHEVEVVIK HNRFTKETYD FDIAVLRLKT PITFRMNVAP ACLPERDWAE 350
    STLMTQKTGI VSGFGRTHEK GRQSTRLKML EVPYVDRNSC KLSSSFIITQ 400
    NMFCAGYDTK QEDACQGDSG GPHVTRFKDT YFVTGIVSWG EGCARKGKYG 450
    IYTKVTAFLK WIDRSMKTRG LPKAKSHAPE VITSSPLK 488
    Length:488
    Mass (Da):54,732
    Last modified:October 1, 1989 - v2
    Checksum:iF81D5746AF4797AF
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti285 – 2884KVRV → E in AAA51984. (PubMed:3011603)Curated
    Sequence conflicti285 – 2884KVRV → E in AAA52486. (PubMed:6587384)Curated
    Sequence conflicti442 – 4421G → S in AAA52490. (PubMed:2582420)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti7 – 71L → I.1 Publication
    Corresponds to variant rs5963 [ dbSNP | Ensembl ].
    VAR_014162
    Natural varianti30 – 301Q → H.1 Publication
    Corresponds to variant rs5961 [ dbSNP | Ensembl ].
    VAR_014163
    Natural varianti47 – 471E → G in FA10D; St. Louis II; strongly reduced activity; not activated by factor VIIa and tissue factor. 1 Publication
    VAR_065428
    Natural varianti51 – 511G → V in FA10D. 1 Publication
    VAR_065429
    Natural varianti54 – 541E → G in FA10D; Ketchikan. 1 Publication
    VAR_065430
    Natural varianti54 – 541E → K in FA10D; Vorarlberg; converts prothrombin at a normal rate but shows decreased affinity for calcium. 2 Publications
    VAR_065431
    Natural varianti72 – 721E → Q in FA10D; Tokyo. 1 Publication
    VAR_065432
    Natural varianti91 – 911E → K in FA10D; Riyadh. 1 Publication
    VAR_065433
    Natural varianti142 – 1421E → K in FA10D; uncertain pathological significance; detected in patients carrying K-54 or P-374; slightly reduced activity. 2 Publications
    Corresponds to variant rs61753266 [ dbSNP | Ensembl ].
    VAR_065434
    Natural varianti149 – 1491C → Y in FA10D. 1 Publication
    VAR_065435
    Natural varianti151 – 1511C → Y in FA10D. 1 Publication
    VAR_065436
    Natural varianti152 – 1521A → T.1 Publication
    Corresponds to variant rs3211772 [ dbSNP | Ensembl ].
    VAR_020176
    Natural varianti192 – 1921G → R.1 Publication
    Corresponds to variant rs3211783 [ dbSNP | Ensembl ].
    VAR_020177
    Natural varianti289 – 2891G → R in FA10D; may affect splicing. 1 Publication
    VAR_065437
    Natural varianti304 – 3041E → K in FA10D. 1 Publication
    VAR_065438
    Natural varianti322 – 3221D → N in FA10D; Stockton; 50% decrease in specific activity. 1 Publication
    VAR_065439
    Natural varianti327 – 3271R → W in FA10D. 1 Publication
    VAR_065440
    Natural varianti338 – 3381V → M in FA10D. 1 Publication
    VAR_065441
    Natural varianti350 – 3501E → K in FA10D. 1 Publication
    VAR_065442
    Natural varianti358 – 3581T → M in FA10D; Roma. 1 Publication
    VAR_065443
    Natural varianti363 – 3631G → S in FA10D. 1 Publication
    VAR_065444
    Natural varianti366 – 3661R → C in FA10D; San Antonio. 1 Publication
    VAR_065445
    Natural varianti374 – 3741S → P in FA10D; Marseille; decreased cleavage by factor IXa; normal catalytic efficiency for prothrombin. 3 Publications
    VAR_065446
    Natural varianti383 – 3831P → S in FA10D; Friuli. 1 Publication
    VAR_065447
    Natural varianti390 – 3901C → F in FA10D; Padua 4. 1 Publication
    Corresponds to variant rs199778916 [ dbSNP | Ensembl ].
    VAR_065448
    Natural varianti404 – 4041C → R in FA10D. 1 Publication
    VAR_065449
    Natural varianti406 – 4061G → S in FA10D; almost complete loss of activity. 1 Publication
    VAR_065450
    Natural varianti420 – 4201G → R in FA10D; Padua 3. 1 Publication
    VAR_065451
    Natural varianti448 – 4481K → N in FA10D; San Giovanni Rotondo. 1 Publication
    VAR_065452

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K03194 mRNA. Translation: AAA52490.1.
    M57285 mRNA. Translation: AAA52421.1.
    AF503510 Genomic DNA. Translation: AAM19347.1.
    BC046125 mRNA. Translation: AAH46125.1.
    N00045
    , L00390, L00391, L00392, L00393, L00394, L00395, L00396 Genomic DNA. Translation: AAA52764.1.
    M22613 mRNA. Translation: AAA51984.1.
    K01886 mRNA. Translation: AAA52486.1.
    M33297 Genomic DNA. Translation: AAA52636.1.
    CCDSiCCDS9530.1.
    PIRiA24478. EXHU.
    RefSeqiNP_000495.1. NM_000504.3.
    UniGeneiHs.361463.

    Genome annotation databases

    EnsembliENST00000375559; ENSP00000364709; ENSG00000126218.
    GeneIDi2159.
    KEGGihsa:2159.
    UCSCiuc001vsx.3. human.

    Polymorphism databases

    DMDMi119761.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Factor X entry

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K03194 mRNA. Translation: AAA52490.1 .
    M57285 mRNA. Translation: AAA52421.1 .
    AF503510 Genomic DNA. Translation: AAM19347.1 .
    BC046125 mRNA. Translation: AAH46125.1 .
    N00045
    , L00390 , L00391 , L00392 , L00393 , L00394 , L00395 , L00396 Genomic DNA. Translation: AAA52764.1 .
    M22613 mRNA. Translation: AAA51984.1 .
    K01886 mRNA. Translation: AAA52486.1 .
    M33297 Genomic DNA. Translation: AAA52636.1 .
    CCDSi CCDS9530.1.
    PIRi A24478. EXHU.
    RefSeqi NP_000495.1. NM_000504.3.
    UniGenei Hs.361463.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1C5M X-ray 1.95 D 235-488 [» ]
    F 84-179 [» ]
    1EZQ X-ray 2.20 A 235-488 [» ]
    B 46-179 [» ]
    1F0R X-ray 2.10 A 235-488 [» ]
    B 46-179 [» ]
    1F0S X-ray 2.10 A 235-488 [» ]
    B 46-179 [» ]
    1FAX X-ray 3.00 A 235-488 [» ]
    L 84-179 [» ]
    1FJS X-ray 1.92 A 235-468 [» ]
    L 127-178 [» ]
    1FXY X-ray 2.15 A 235-344 [» ]
    1G2L X-ray 1.90 A 235-469 [» ]
    B 86-179 [» ]
    1G2M X-ray 3.02 A 235-469 [» ]
    B 86-179 [» ]
    1HCG X-ray 2.20 A 235-475 [» ]
    B 129-179 [» ]
    1IOE X-ray 2.90 A 235-469 [» ]
    L 84-179 [» ]
    1IQE X-ray 2.90 A 235-469 [» ]
    L 84-179 [» ]
    1IQF X-ray 3.20 A 235-469 [» ]
    L 84-179 [» ]
    1IQG X-ray 2.60 A 235-469 [» ]
    L 84-179 [» ]
    1IQH X-ray 3.00 A 235-469 [» ]
    L 84-179 [» ]
    1IQI X-ray 2.90 A 235-469 [» ]
    L 84-179 [» ]
    1IQJ X-ray 3.00 A 235-469 [» ]
    L 84-179 [» ]
    1IQK X-ray 3.20 A 235-469 [» ]
    L 84-179 [» ]
    1IQL X-ray 2.70 A 235-469 [» ]
    L 84-179 [» ]
    1IQM X-ray 2.60 A 235-469 [» ]
    L 84-179 [» ]
    1IQN X-ray 2.60 A 235-469 [» ]
    L 84-179 [» ]
    1KSN X-ray 2.10 A 235-488 [» ]
    B 46-179 [» ]
    1LPG X-ray 2.00 A 46-179 [» ]
    B 235-488 [» ]
    1LPK X-ray 2.20 A 46-179 [» ]
    B 235-488 [» ]
    1LPZ X-ray 2.40 A 46-179 [» ]
    B 235-488 [» ]
    1LQD X-ray 2.70 A 46-179 [» ]
    B 235-488 [» ]
    1MQ5 X-ray 2.10 A 235-467 [» ]
    L 127-177 [» ]
    1MQ6 X-ray 2.10 A 235-467 [» ]
    L 127-177 [» ]
    1MSX model - A 235-469 [» ]
    1NFU X-ray 2.05 A 235-488 [» ]
    B 46-240 [» ]
    1NFW X-ray 2.10 A 235-488 [» ]
    B 46-179 [» ]
    1NFX X-ray 2.15 A 235-488 [» ]
    B 46-179 [» ]
    1NFY X-ray 2.10 A 235-488 [» ]
    B 46-179 [» ]
    1NL8 model - F 235-469 [» ]
    L 41-179 [» ]
    1P0S X-ray 2.80 H 235-488 [» ]
    L 41-178 [» ]
    1V3X X-ray 2.20 A 235-467 [» ]
    B 127-178 [» ]
    1WU1 X-ray 2.30 A 235-467 [» ]
    B 85-179 [» ]
    1XKA X-ray 2.30 C 235-469 [» ]
    L 85-179 [» ]
    1XKB X-ray 2.40 A/B 85-179 [» ]
    C/D 235-469 [» ]
    1Z6E X-ray 1.80 A 235-468 [» ]
    L 127-178 [» ]
    2BMG X-ray 2.70 A 126-178 [» ]
    B 235-468 [» ]
    2BOH X-ray 2.20 A 46-179 [» ]
    B 235-488 [» ]
    2BOK X-ray 1.64 A 235-475 [» ]
    L 126-180 [» ]
    2BQ6 X-ray 3.00 A 126-177 [» ]
    B 220-468 [» ]
    2BQ7 X-ray 2.20 A 126-177 [» ]
    B 220-468 [» ]
    2BQW X-ray 2.95 A 126-177 [» ]
    B 220-468 [» ]
    2CJI X-ray 2.10 A 235-488 [» ]
    B 46-179 [» ]
    2D1J X-ray 2.20 A 235-467 [» ]
    B 125-178 [» ]
    2EI6 X-ray 2.30 A 235-467 [» ]
    B 125-178 [» ]
    2EI7 X-ray 2.30 A 235-467 [» ]
    B 125-178 [» ]
    2EI8 X-ray 2.10 A 235-467 [» ]
    B 125-178 [» ]
    2FZZ X-ray 2.20 A 235-468 [» ]
    L 127-178 [» ]
    2G00 X-ray 2.10 A 235-468 [» ]
    L 127-178 [» ]
    2GD4 X-ray 3.30 A/L 126-182 [» ]
    B/H 235-475 [» ]
    2H9E X-ray 2.20 H 235-467 [» ]
    L 86-234 [» ]
    2J2U X-ray 1.90 A 235-488 [» ]
    B 46-179 [» ]
    2J34 X-ray 2.01 A 235-488 [» ]
    B 46-179 [» ]
    2J38 X-ray 2.10 A 235-488 [» ]
    B 46-179 [» ]
    2J4I X-ray 1.80 A 235-488 [» ]
    B 46-179 [» ]
    2J94 X-ray 2.10 A 235-488 [» ]
    B 46-179 [» ]
    2J95 X-ray 2.01 A 235-488 [» ]
    B 46-179 [» ]
    2JKH X-ray 1.25 A 235-475 [» ]
    L 126-180 [» ]
    2P16 X-ray 2.30 A 235-468 [» ]
    L 127-178 [» ]
    2P3F X-ray 3.10 H 235-469 [» ]
    L 125-178 [» ]
    2P3T X-ray 1.92 A 127-178 [» ]
    B 235-467 [» ]
    2P3U X-ray 1.62 A 127-178 [» ]
    B 235-467 [» ]
    2P93 X-ray 1.90 A 235-468 [» ]
    L 127-178 [» ]
    2P94 X-ray 1.80 A 235-468 [» ]
    L 127-178 [» ]
    2P95 X-ray 2.20 A 235-468 [» ]
    L 127-178 [» ]
    2PHB X-ray 2.30 A 235-468 [» ]
    B 128-178 [» ]
    2PR3 X-ray 1.50 A 235-468 [» ]
    B 128-178 [» ]
    2Q1J X-ray 1.90 A 235-468 [» ]
    B 128-178 [» ]
    2RA0 X-ray 2.30 A 235-468 [» ]
    L 128-178 [» ]
    2UWL X-ray 1.90 A 235-488 [» ]
    B 46-179 [» ]
    2UWO X-ray 1.75 A 235-488 [» ]
    B 46-179 [» ]
    2UWP X-ray 1.75 A 235-488 [» ]
    B 46-179 [» ]
    2VH0 X-ray 1.70 A 235-488 [» ]
    B 46-179 [» ]
    2VH6 X-ray 1.95 A 235-488 [» ]
    B 46-177 [» ]
    2VVC X-ray 1.95 A/B 235-475 [» ]
    K/L 126-180 [» ]
    2VVU X-ray 2.30 A 235-475 [» ]
    L 126-180 [» ]
    2VVV X-ray 1.73 A 235-475 [» ]
    L 126-180 [» ]
    2VWL X-ray 1.80 A 235-475 [» ]
    L 126-180 [» ]
    2VWM X-ray 1.96 A/B 235-475 [» ]
    K/L 126-180 [» ]
    2VWN X-ray 1.61 A 235-475 [» ]
    L 126-180 [» ]
    2VWO X-ray 1.60 A 235-475 [» ]
    L 126-180 [» ]
    2W26 X-ray 2.08 A 235-468 [» ]
    B 129-177 [» ]
    2W3I X-ray 1.90 A 235-468 [» ]
    B 128-178 [» ]
    2W3K X-ray 2.05 A 235-468 [» ]
    B 128-178 [» ]
    2WYG X-ray 1.88 A 235-487 [» ]
    B 46-179 [» ]
    2WYJ X-ray 2.38 A 235-488 [» ]
    B 46-179 [» ]
    2XBV X-ray 1.66 A 235-475 [» ]
    L 126-180 [» ]
    2XBW X-ray 1.72 A 235-475 [» ]
    L 126-180 [» ]
    2XBX X-ray 1.85 A 235-475 [» ]
    L 126-180 [» ]
    2XBY X-ray 2.02 A 235-475 [» ]
    L 126-180 [» ]
    2XC0 X-ray 2.05 A 235-475 [» ]
    L 126-180 [» ]
    2XC4 X-ray 1.67 A 235-475 [» ]
    L 126-180 [» ]
    2XC5 X-ray 1.70 A 235-475 [» ]
    L 126-180 [» ]
    2Y5F X-ray 1.29 A 235-468 [» ]
    L 127-180 [» ]
    2Y5G X-ray 1.29 A 235-468 [» ]
    L 127-180 [» ]
    2Y5H X-ray 1.33 A 235-468 [» ]
    L 127-180 [» ]
    2Y7X X-ray 1.90 A 235-488 [» ]
    B 46-179 [» ]
    2Y7Z X-ray 1.84 A 235-488 [» ]
    B 46-179 [» ]
    2Y80 X-ray 1.90 A 235-488 [» ]
    B 46-179 [» ]
    2Y81 X-ray 1.70 A 235-488 [» ]
    B 46-179 [» ]
    2Y82 X-ray 2.20 A 235-488 [» ]
    B 46-179 [» ]
    3CEN X-ray 1.60 A 235-468 [» ]
    L 127-178 [» ]
    3CS7 X-ray 2.20 A 235-468 [» ]
    L 127-178 [» ]
    3ENS X-ray 2.30 A/C 85-178 [» ]
    B/D 235-472 [» ]
    3FFG X-ray 1.54 A 235-468 [» ]
    L 127-178 [» ]
    3HPT X-ray 2.19 A/C 85-178 [» ]
    B/D 235-472 [» ]
    3IIT X-ray 1.80 A 235-467 [» ]
    B 125-178 [» ]
    3K9X X-ray 1.90 A/C 85-178 [» ]
    B/D 235-472 [» ]
    3KL6 X-ray 1.45 A 235-475 [» ]
    B 126-179 [» ]
    3KQB X-ray 2.25 A 235-468 [» ]
    L 127-178 [» ]
    3KQC X-ray 2.20 A 235-468 [» ]
    L 127-178 [» ]
    3KQD X-ray 2.75 A 235-468 [» ]
    L 127-178 [» ]
    3KQE X-ray 2.35 A 235-468 [» ]
    L 127-178 [» ]
    3LIW X-ray 2.22 A 235-468 [» ]
    B 128-178 [» ]
    3M36 X-ray 2.15 A 235-468 [» ]
    L 127-178 [» ]
    3M37 X-ray 1.90 A 235-468 [» ]
    L 127-178 [» ]
    3Q3K X-ray 2.00 A 235-467 [» ]
    B 125-178 [» ]
    3SW2 X-ray 2.42 A 85-178 [» ]
    B 235-472 [» ]
    3TK5 X-ray 2.20 A 235-467 [» ]
    B 125-178 [» ]
    3TK6 X-ray 1.80 A 235-467 [» ]
    B 125-178 [» ]
    4A7I X-ray 2.40 A 84-179 [» ]
    B 235-488 [» ]
    4BTI X-ray 2.30 A/E 84-179 [» ]
    B/F 235-488 [» ]
    4BTT X-ray 2.59 A/E 84-179 [» ]
    B/F 235-488 [» ]
    4BTU X-ray 2.37 A/E 84-179 [» ]
    B/F 235-488 [» ]
    ProteinModelPortali P00742.
    SMRi P00742. Positions 43-180, 235-466.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108457. 9 interactions.
    DIPi DIP-29896N.
    IntActi P00742. 7 interactions.
    MINTi MINT-276128.
    STRINGi 9606.ENSP00000364709.

    Chemistry

    BindingDBi P00742.
    ChEMBLi CHEMBL244.
    DrugBanki DB00009. Alteplase.
    DB00029. Anistreplase.
    DB00025. Antihemophilic Factor.
    DB00100. Coagulation Factor IX.
    DB00036. Coagulation factor VIIa.
    DB01225. Enoxaparin.
    DB01109. Heparin.
    DB00170. Menadione.
    DB00015. Reteplase.
    DB00031. Tenecteplase.
    GuidetoPHARMACOLOGYi 2359.

    Protein family/group databases

    MEROPSi S01.216.

    PTM databases

    PhosphoSitei P00742.
    UniCarbKBi P00742.

    Polymorphism databases

    DMDMi 119761.

    Proteomic databases

    MaxQBi P00742.
    PaxDbi P00742.
    PRIDEi P00742.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000375559 ; ENSP00000364709 ; ENSG00000126218 .
    GeneIDi 2159.
    KEGGi hsa:2159.
    UCSCi uc001vsx.3. human.

    Organism-specific databases

    CTDi 2159.
    GeneCardsi GC13P113777.
    HGNCi HGNC:3528. F10.
    MIMi 227600. phenotype.
    613872. gene.
    neXtProti NX_P00742.
    Orphaneti 328. Congenital factor X deficiency.
    PharmGKBi PA27940.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5640.
    HOGENOMi HOG000251821.
    HOVERGENi HBG013304.
    InParanoidi P00742.
    KOi K01314.
    OMAi EMAHEVE.
    PhylomeDBi P00742.
    TreeFami TF327329.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS05000-MONOMER.
    Reactomei REACT_1050. Gamma-carboxylation of protein precursors.
    REACT_1439. Common Pathway.
    REACT_1573. Extrinsic Pathway.
    REACT_1906. Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
    REACT_326. Intrinsic Pathway.
    REACT_733. Removal of aminoterminal propeptides from gamma-carboxylated proteins.
    SABIO-RK P00742.

    Miscellaneous databases

    ChiTaRSi F10. human.
    EvolutionaryTracei P00742.
    GeneWikii Factor_X.
    GenomeRNAii 2159.
    NextBioi 8723.
    PMAP-CutDB P00742.
    PROi P00742.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P00742.
    Bgeei P00742.
    CleanExi HS_F10.
    Genevestigatori P00742.

    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 expression in COS-1 cells of a full-length cDNA encoding human coagulation factor X."
      Messier T.L., Pittman D.D., Long G.L., Kaufman R.J., Church W.R.
      Gene 99:291-294(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Gene for human factor X: a blood coagulation factor whose gene organization is essentially identical with that of factor IX and protein C."
      Leytus S.P., Foster D.C., Kurachi K., Davie E.W.
      Biochemistry 25:5098-5102(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. SeattleSNPs variation discovery resource
      Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS THR-152 AND ARG-192.
    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].
      Tissue: Ovary.
    5. "Characterization of an almost full-length cDNA coding for human blood coagulation factor X."
      Fung M.R., Hay C.W., McGillivray R.T.A.
      Proc. Natl. Acad. Sci. U.S.A. 82:3591-3595(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 13-488.
    6. "Isolation and characterization of human blood-coagulation factor X cDNA."
      Kaul R.K., Hildebrand B., Roberts S., Jagadeeswaran P.
      Gene 41:311-314(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 19-488.
      Tissue: Liver.
    7. "Complete amino acid sequence of the light chain of human blood coagulation factor X: evidence for identification of residue 63 as beta-hydroxyaspartic acid."
      McMullen B.A., Fujikawa K., Kisiel W., Sasagawa T., Howald W.N., Kwa E.Y., Weinstein B.
      Biochemistry 22:2875-2884(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 41-179, HYDROXYLATION AT ASP-103, GAMMA-CARBOXYGLUTAMATION AT GLU-46; GLU-47; GLU-54; GLU-56; GLU-59; GLU-60; GLU-65; GLU-66; GLU-69; GLU-72 AND GLU-79.
    8. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 115-488, TISSUE SPECIFICITY.
      Tissue: Liver.
    9. "Identification of O-linked oligosaccharide chains in the activation peptides of blood coagulation factor X. The role of the carbohydrate moieties in the activation of factor X."
      Inoue K., Morita T.
      Eur. J. Biochem. 218:153-163(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 183-234, GLYCOSYLATION AT THR-199; THR-211; ASN-221 AND ASN-231.
    10. "Cloning and characterization of the 5' end (exon 1) of the gene encoding human factor X."
      Jagadeeswaran P., Reddy S.V., Rao K.J., Hamsabhushanam K., Lyman G.
      Gene 84:517-519(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-23.
    11. "Mechanism of inhibition of activated protein C by protein C inhibitor."
      Suzuki K., Nishioka J., Kusumoto H., Hashimoto S.
      J. Biochem. 95:187-195(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION, HETERODIMER WITH SERPINA5.
    12. "Basis for the specificity and activation of the serpin protein Z-dependent proteinase inhibitor (ZPI) as an inhibitor of membrane-associated factor Xa."
      Huang X., Dementiev A., Olson S.T., Gettins P.G.
      J. Biol. Chem. 285:20399-20409(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    13. "Human urinary glycoproteomics; attachment site specific analysis of N-and O-linked glycosylations by CID and ECD."
      Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.
      Mol. Cell. Proteomics 0:0-0(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION, STRUCTURE OF CARBOHYDRATES, IDENTIFICATION BY MASS SPECTROMETRY.
    14. Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 86-179 AND 235-278.
    15. "Structural basis for chemical inhibition of human blood coagulation factor Xa."
      Kamata K., Kawamoto H., Honma T., Iwama T., Kim S.H.
      Proc. Natl. Acad. Sci. U.S.A. 95:6630-6635(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 86-179 AND 235-278.
    16. Cited for: X-RAY CRYSTALLOGRAPHY (1.62 ANGSTROMS) OF 127-467.
    17. "Molecular characterization of human factor XSan Antonio."
      Reddy S.V., Zhou Z.Q., Rao K.J., Scott J.P., Watzke H., High K.A., Jagadeeswaran P.
      Blood 74:1486-1490(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT FA10D CYS-366.
    18. "Molecular defect (Gla+14TO: hereditary factor X deficiency (factor X 'Vorarlberg')."
      Watzke H.H., Lechner K., Roberts H.R., Reddy S.V., Welsch D.J., Friedman P., Mahr G., Jagadeeswaran P., Monroe D.M., High K.A.
      J. Biol. Chem. 265:11982-11989(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS FA10D LYS-54 AND LYS-142, CHARACTERIZATION OF VARIANT FA10D LYS-54.
    19. "Molecular defect in coagulation factor XFriuli results from a substitution of serine for proline at position 343."
      James H.L., Girolami A., Fair D.S.
      Blood 77:317-323(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT FA10D SER-383.
    20. "Molecular bases of CRM+ factor X deficiency: a frequent mutation (Ser334Pro) in the catalytic domain and a substitution (Glu102Lys) in the second EGF-like domain."
      Marchetti G., Castaman G., Pinotti M., Lunghi B., Di Iasio M.G., Ruggieri M., Rodeghiero F., Bernardi F.
      Br. J. Haematol. 90:910-915(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS FA10D LYS-142 AND PRO-374.
    21. "Functional consequences of the Ser334-->Pro mutation in a human factor X variant (factor XMarseille)."
      Bezeaud A., Miyata T., Helley D., Zeng Y.Z., Kato H., Aillaud M.F., Juhan-Vague I., Guillin M.C.
      Eur. J. Biochem. 234:140-147(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT FA10D PRO-374, CHARACTERIZATION OF VARIANT FA10D PRO-374.
    22. "Factor XKetchikan: a variant molecule in which Gly replaces a Gla residue at position 14 in the light chain."
      Kim D.J., Thompson A.R., James H.L.
      Hum. Genet. 95:212-214(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT FA10D GLY-54.
    23. "Factor X Stockton: a mild bleeding diathesis associated with an active site mutation in factor X."
      Messier T.L., Wong C.Y., Bovill E.G., Long G.L., Church W.R.
      Blood Coagul. Fibrinolysis 7:5-14(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT FA10D ASN-322, CHARACTERIZATION OF VARIANT FA10D ASN-322.
    24. "Factor XSt. Louis II. Identification of a glycine substitution at residue 7 and characterization of the recombinant protein."
      Rudolph A.E., Mullane M.P., Porche-Sorbet R., Tsuda S., Miletich J.P.
      J. Biol. Chem. 271:28601-28606(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT FA10D GLY-47.
    25. "A family with hereditary factor X deficiency with a point mutation Gla32 to Gln in the Gla domain (factor X Tokyo)."
      Zama T., Murata M., Watanabe R., Yokoyama K., Moriki T., Ambo H., Murakami H., Kikuchi M., Ikeda Y.
      Br. J. Haematol. 106:809-811(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT FA10D GLN-72.
    26. Cited for: VARIANTS ILE-7 AND HIS-30.
    27. Cited for: VARIANTS FA10D LYS-54; TYR-149; TYR-151; ARG-289; LYS-304; TRP-327; MET-338; LYS-350; MET-358; SER-363 AND ARG-404.
    28. "The impact of Glu102Lys on the factor X function in a patient with a doubly homozygous factor X deficiency (Gla14Lys and Glu102Lys)."
      Forberg E., Huhmann I., Jimenez-Boj E., Watzke H.H.
      Thromb. Haemost. 83:234-238(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF VARIANT FA10D LYS-142.
    29. "A dysfunctional factor X (factor X San Giovanni Rotondo) present at homozygous and double heterozygous level: identification of a novel microdeletion (delC556) and missense mutation (Lys(408)-->Asn) in the factor X gene. A study of an Italian family."
      Simioni P., Vianello F., Kalafatis M., Barzon L., Ladogana S., Paolucci P., Carotenuto M., Dal Bello F., Palu G., Girolami A.
      Thromb. Res. 101:219-230(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT FA10D ASN-448.
    30. "A new factor X defect (factor X Padua 3): a compound heterozygous between true deficiency (Gly(380)-->Arg) and an abnormality (Ser(334)-->Pro)."
      Vianello F., Lombardi A.M., Boldrin C., Luni S., Girolami A.
      Thromb. Res. 104:257-264(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS FA10D PRO-374 AND ARG-420.
    31. "A novel type I factor X variant (factor X Cys350Phe) due to loss of a disulfide bond in the catalytic domain."
      Vianello F., Lombardi A.M., Bello F.D., Palu G., Zanon E., Girolami A.
      Blood Coagul. Fibrinolysis 14:401-405(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT FA10D PHE-390.
    32. "Genetic analysis of hereditary factor X deficiency in a French patient of Sri Lankan ancestry: in vitro expression study identified Gly366Ser substitution as the molecular basis of the dysfunctional factor X."
      Isshiki I., Favier R., Moriki T., Uchida T., Ishihara H., Van Dreden P., Murata M., Ikeda Y.
      Blood Coagul. Fibrinolysis 16:9-16(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT FA10D SER-406, CHARACTERIZATION OF VARIANT FA10D SER-406.
    33. "Analysis of the novel factor X gene mutation Glu51Lys in two families with factor X-Riyadh anomaly."
      Al-Hilali A., Wulff K., Abdel-Razeq H., Saud K.A., Al-Gaili F., Herrmann F.H.
      Thromb. Haemost. 97:542-545(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT FA10D LYS-91.
    34. "Characterization of a homozygous Gly11Val mutation in the Gla domain of coagulation factor X."
      Chafa O., Tagzirt M., Tapon-Bretaudiere J., Reghis A., Fischer A.M., LeBonniec B.F.
      Thromb. Res. 124:144-148(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT FA10D VAL-51.

    Entry informationi

    Entry nameiFA10_HUMAN
    AccessioniPrimary (citable) accession number: P00742
    Secondary accession number(s): Q14340
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: October 1, 1989
    Last modified: October 1, 2014
    This is version 206 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 13
      Human chromosome 13: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Peptidase families
      Classification of peptidase families and list of entries
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3