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P00742 (FA10_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 204. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Coagulation factor X

EC=3.4.21.6
Alternative name(s):
Stuart factor
Stuart-Prower factor
Gene names
Name:F10
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length488 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 and SERPINA10. Ref.11 Ref.12

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.

Subcellular location

Secreted.

Tissue specificity

Plasma; synthesized in the liver. Ref.8

Post-translational modification

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. Ref.9 Ref.13

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.

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32 Ref.33 Ref.34 Ref.35

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.

Ontologies

Keywords
   Biological processBlood coagulation
Hemostasis
   Cellular componentSecreted
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
   DomainEGF-like domain
Repeat
Signal
   LigandCalcium
   Molecular functionHydrolase
Protease
Serine protease
   PTMCleavage on pair of basic residues
Disulfide bond
Gamma-carboxyglutamic acid
Glycoprotein
Hydroxylation
Zymogen
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processblood coagulation

Inferred by curator PubMed 17469850. Source: BHF-UCL

blood coagulation, extrinsic pathway

Traceable author statement. Source: Reactome

blood coagulation, intrinsic pathway

Traceable author statement. Source: Reactome

cellular protein metabolic process

Traceable author statement. Source: Reactome

peptidyl-glutamic acid carboxylation

Traceable author statement. Source: Reactome

positive regulation of cell migration

Traceable author statement PubMed 18612547. Source: BHF-UCL

positive regulation of protein kinase B signaling

Inferred from direct assay PubMed 18612547. Source: BHF-UCL

post-translational protein modification

Traceable author statement. Source: Reactome

proteolysis

Traceable author statement. Source: Reactome

   Cellular_componentGolgi lumen

Traceable author statement. Source: Reactome

endoplasmic reticulum lumen

Traceable author statement. Source: Reactome

extracellular region

Non-traceable author statement PubMed 14718574. Source: UniProtKB

intrinsic component of external side of plasma membrane

Inferred by curator PubMed 17469850. Source: BHF-UCL

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

phospholipid binding

Inferred from direct assay PubMed 17469850. Source: BHF-UCL

protein binding

Inferred from physical interaction Ref.11. Source: UniProtKB

serine-type endopeptidase activity

Inferred from direct assay PubMed 17469850. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131 Potential
Propeptide32 – 409
PRO_0000027786
Chain41 – 488448Coagulation factor X
PRO_0000027787
Chain41 – 179139Factor X light chain
PRO_0000027788
Chain183 – 488306Factor X heavy chain
PRO_0000027789
Propeptide183 – 23452Activation peptide Ref.9
PRO_0000027790
Chain235 – 488254Activated factor Xa heavy chain
PRO_0000027791

Regions

Domain41 – 8545Gla
Domain86 – 12237EGF-like 1; calcium-binding Potential
Domain125 – 16541EGF-like 2
Domain235 – 467233Peptidase S1
Region183 – 20321O-glycosylated at one site
Region476 – 48510O-glycosylated at one site

Sites

Active site2761Charge relay system
Active site3221Charge relay system
Active site4191Charge relay system

Amino acid modifications

Modified residue4614-carboxyglutamate Ref.7
Modified residue4714-carboxyglutamate Ref.7
Modified residue5414-carboxyglutamate Ref.7
Modified residue5614-carboxyglutamate Ref.7
Modified residue5914-carboxyglutamate Ref.7
Modified residue6014-carboxyglutamate Ref.7
Modified residue6514-carboxyglutamate Ref.7
Modified residue6614-carboxyglutamate Ref.7
Modified residue6914-carboxyglutamate Ref.7
Modified residue7214-carboxyglutamate Ref.7
Modified residue7914-carboxyglutamate Ref.7
Modified residue1031(3R)-3-hydroxyaspartate
Glycosylation1991O-linked (GalNAc...) Ref.9
Glycosylation2111O-linked (GalNAc...) Ref.9
Glycosylation2211N-linked (GlcNAc...) Ref.9
CAR_000012
Glycosylation2311N-linked (GlcNAc...) Ref.9
CAR_000013
Disulfide bond57 ↔ 62 By similarity
Disulfide bond90 ↔ 101
Disulfide bond95 ↔ 110
Disulfide bond112 ↔ 121
Disulfide bond129 ↔ 140
Disulfide bond136 ↔ 149
Disulfide bond151 ↔ 164
Disulfide bond172 ↔ 342Interchain (between light and heavy chains)
Disulfide bond241 ↔ 246
Disulfide bond261 ↔ 277
Disulfide bond390 ↔ 404
Disulfide bond415 ↔ 443

Natural variations

Natural variant71L → I. Ref.26
Corresponds to variant rs5963 [ dbSNP | Ensembl ].
VAR_014162
Natural variant301Q → H. Ref.26
Corresponds to variant rs5961 [ dbSNP | Ensembl ].
VAR_014163
Natural variant471E → G in FA10D; St. Louis II; strongly reduced activity; not activated by factor VIIa and tissue factor. Ref.24
VAR_065428
Natural variant511G → V in FA10D. Ref.35
VAR_065429
Natural variant541E → G in FA10D; Ketchikan. Ref.22
VAR_065430
Natural variant541E → K in FA10D; Vorarlberg; converts prothrombin at a normal rate but shows decreased affinity for calcium. Ref.18 Ref.28
VAR_065431
Natural variant721E → Q in FA10D; Tokyo. Ref.25
VAR_065432
Natural variant911E → K in FA10D; Riyadh. Ref.34
VAR_065433
Natural variant1421E → K in FA10D; uncertain pathological significance; detected in patients carrying K-54 or P-374; slightly reduced activity. Ref.18 Ref.20 Ref.29
Corresponds to variant rs61753266 [ dbSNP | Ensembl ].
VAR_065434
Natural variant1491C → Y in FA10D. Ref.28
VAR_065435
Natural variant1511C → Y in FA10D. Ref.28
VAR_065436
Natural variant1521A → T. Ref.3
Corresponds to variant rs3211772 [ dbSNP | Ensembl ].
VAR_020176
Natural variant1921G → R. Ref.3
Corresponds to variant rs3211783 [ dbSNP | Ensembl ].
VAR_020177
Natural variant2891G → R in FA10D; may affect splicing. Ref.28
VAR_065437
Natural variant3041E → K in FA10D. Ref.28
VAR_065438
Natural variant3221D → N in FA10D; Stockton; 50% decrease in specific activity. Ref.23
VAR_065439
Natural variant3271R → W in FA10D. Ref.28
VAR_065440
Natural variant3381V → M in FA10D. Ref.28
VAR_065441
Natural variant3501E → K in FA10D. Ref.28
VAR_065442
Natural variant3581T → M in FA10D; Roma. Ref.28
VAR_065443
Natural variant3631G → S in FA10D. Ref.28
VAR_065444
Natural variant3661R → C in FA10D; San Antonio. Ref.17
VAR_065445
Natural variant3741S → P in FA10D; Marseille; decreased cleavage by factor IXa; normal catalytic efficiency for prothrombin. Ref.20 Ref.21 Ref.31
VAR_065446
Natural variant3831P → S in FA10D; Friuli. Ref.19
VAR_065447
Natural variant3901C → F in FA10D; Padua 4. Ref.32
Corresponds to variant rs199778916 [ dbSNP | Ensembl ].
VAR_065448
Natural variant4041C → R in FA10D. Ref.28
VAR_065449
Natural variant4061G → S in FA10D; almost complete loss of activity. Ref.33
VAR_065450
Natural variant4201G → R in FA10D; Padua 3. Ref.31
VAR_065451
Natural variant4481K → N in FA10D; San Giovanni Rotondo. Ref.30
VAR_065452

Experimental info

Sequence conflict285 – 2884KVRV → E in AAA51984. Ref.6
Sequence conflict285 – 2884KVRV → E in AAA52486. Ref.8
Sequence conflict4421G → S in AAA52490. Ref.5

Secondary structure

........................................................................................... 488
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00742 [UniParc].

Last modified October 1, 1989. Version 2.
Checksum: F81D5746AF4797AF

FASTA48854,732
        10         20         30         40         50         60 
MGRPLHLVLL SASLAGLLLL GESLFIRREQ ANNILARVTR ANSFLEEMKK GHLERECMEE 

        70         80         90        100        110        120 
TCSYEEAREV FEDSDKTNEF WNKYKDGDQC ETSPCQNQGK CKDGLGEYTC TCLEGFEGKN 

       130        140        150        160        170        180 
CELFTRKLCS LDNGDCDQFC HEEQNSVVCS CARGYTLADN GKACIPTGPY PCGKQTLERR 

       190        200        210        220        230        240 
KRSVAQATSS SGEAPDSITW KPYDAADLDP TENPFDLLDF NQTQPERGDN NLTRIVGGQE 

       250        260        270        280        290        300 
CKDGECPWQA LLINEENEGF CGGTILSEFY ILTAAHCLYQ AKRFKVRVGD RNTEQEEGGE 

       310        320        330        340        350        360 
AVHEVEVVIK HNRFTKETYD FDIAVLRLKT PITFRMNVAP ACLPERDWAE STLMTQKTGI 

       370        380        390        400        410        420 
VSGFGRTHEK GRQSTRLKML EVPYVDRNSC KLSSSFIITQ NMFCAGYDTK QEDACQGDSG 

       430        440        450        460        470        480 
GPHVTRFKDT YFVTGIVSWG EGCARKGKYG IYTKVTAFLK WIDRSMKTRG LPKAKSHAPE 


VITSSPLK 

« Hide

References

« Hide 'large scale' references
[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]"Characterization of a cDNA coding for human factor X."
Leytus S.P., Chung D.W., Kisiel W., Kurachi K., Davie E.W.
Proc. Natl. Acad. Sci. U.S.A. 81:3699-3702(1984) [PubMed] [Europe PMC] [Abstract]
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]"Structure of human des(1-45) factor Xa at 2.2-A resolution."
Padmanabhan K., Padmanabhan K.P., Tulinsky A., Park C.H., Bode W., Huber R., Blankenship D.T., Cardin A.D., Kisiel W.
J. Mol. Biol. 232:947-966(1993) [PubMed] [Europe PMC] [Abstract]
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]"Substituted thiophene-anthranilamides as potent inhibitors of human factor Xa."
Kochanny M.J., Adler M., Ewing J., Griedel B.D., Ho E., Karanjawala R., Lee W., Lentz D., Liang A.M., Morrissey M.M., Phillips G.B., Post J., Sacchi K.L., Sakata S.T., Subramanyam B., Vergona R., Walters J., White K.A. expand/collapse author list , Whitlow M., Ye B., Zhao Z., Shaw K.J.
Bioorg. Med. Chem. 15:2127-2146(2007) [PubMed] [Europe PMC] [Abstract]
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]"Characterization of single-nucleotide polymorphisms in coding regions of human genes."
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S.
Nat. Genet. 22:231-238(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ILE-7 AND HIS-30.
[27]Erratum
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S.
Nat. Genet. 23:373-373(1999)
[28]"Molecular analysis of the genotype-phenotype relationship in factor X deficiency."
Millar D.S., Elliston L., Deex P., Krawczak M., Wacey A.I., Reynaud J., Nieuwenhuis H.K., Bolton-Maggs P., Mannucci P.M., Reverter J.C., Cachia P., Pasi K.J., Layton D.M., Cooper D.N.
Hum. Genet. 106:249-257(2000) [PubMed] [Europe PMC] [Abstract]
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.
[29]"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.
[30]"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.
[31]"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.
[32]"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.
[33]"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.
[34]"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.
[35]"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.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
K03194 mRNA. Translation: AAA52490.1.
M57285 mRNA. Translation: AAA52421.1.
AF503510 Genomic DNA. Translation: AAM19347.1.
BC046125 mRNA. Translation: AAH46125.1.
N00045 expand/collapse EMBL AC list , 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.
CCDSCCDS9530.1.
PIREXHU. A24478.
RefSeqNP_000495.1. NM_000504.3.
UniGeneHs.361463.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP00742.
SMRP00742. Positions 43-180, 235-466.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108457. 9 interactions.
DIPDIP-29896N.
IntActP00742. 7 interactions.
MINTMINT-276128.
STRING9606.ENSP00000364709.

Chemistry

BindingDBP00742.
ChEMBLCHEMBL244.
DrugBankDB00009. Alteplase.
DB00029. Anistreplase.
DB00025. Antihemophilic Factor.
DB00100. Coagulation Factor IX.
DB00036. Coagulation factor VIIa.
DB01225. Enoxaparin.
DB01109. Heparin.
DB00170. Menadione.
DB00015. Reteplase.
DB00031. Tenecteplase.
GuidetoPHARMACOLOGY2359.

Protein family/group databases

MEROPSS01.216.

PTM databases

PhosphoSiteP00742.
UniCarbKBP00742.

Polymorphism databases

DMDM119761.

Proteomic databases

MaxQBP00742.
PaxDbP00742.
PRIDEP00742.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000375559; ENSP00000364709; ENSG00000126218.
GeneID2159.
KEGGhsa:2159.
UCSCuc001vsx.3. human.

Organism-specific databases

CTD2159.
GeneCardsGC13P113777.
HGNCHGNC:3528. F10.
MIM227600. phenotype.
613872. gene.
neXtProtNX_P00742.
Orphanet328. Congenital factor X deficiency.
PharmGKBPA27940.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5640.
HOGENOMHOG000251821.
HOVERGENHBG013304.
InParanoidP00742.
KOK01314.
OMAEMAHEVE.
PhylomeDBP00742.
TreeFamTF327329.

Enzyme and pathway databases

BioCycMetaCyc:HS05000-MONOMER.
ReactomeREACT_17015. Metabolism of proteins.
REACT_604. Hemostasis.
SABIO-RKP00742.

Gene expression databases

ArrayExpressP00742.
BgeeP00742.
CleanExHS_F10.
GenevestigatorP00742.

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_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]
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. SSF50494. 2 hits.
SSF57630. SSF57630. 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

ChiTaRSF10. human.
EvolutionaryTraceP00742.
GeneWikiFactor_X.
GenomeRNAi2159.
NextBio8723.
PMAP-CutDBP00742.
PROP00742.
SOURCESearch...

Entry information

Entry nameFA10_HUMAN
AccessionPrimary (citable) accession number: P00742
Secondary accession number(s): Q14340
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 1, 1989
Last modified: July 9, 2014
This is version 204 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 13

Human chromosome 13: entries, gene names and cross-references to MIM