P00742 (FA10_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Coagulation factor X
EC=3.4.21.6

Alternative name(s):
Stuart factor
Stuart-Prower factor

Cleaved into the following 3 chains:

1. Factor X light chain
2. Factor X heavy chain
3. Activated factor Xa heavy chain

Gene names

Name:

F10

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	488 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Blood coagulation Hemostasis
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Domain	EGF-like domain Repeat Signal
Ligand	Calcium
Molecular function	Hydrolase Protease Serine protease
PTM	Cleavage on pair of basic residues Disulfide bond Gamma-carboxyglutamic acid Glycoprotein Hydroxylation Zymogen
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	blood coagulation, extrinsic pathway Traceable author statement. Source: Reactome blood coagulation, intrinsic pathway 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 cascade 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_component	Golgi 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 to external side of plasma membrane Inferred by curator PubMed 17469850. Source: BHF-UCL
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro phospholipid binding Inferred from direct assay PubMed 17469850. Source: BHF-UCL serine-type endopeptidase activity Inferred from direct assay PubMed 17469850. Source: BHF-UCL
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 31

31

Potential

Propeptide

32 – 40

9

PRO_0000027786

Chain

41 – 488

448

Coagulation factor X

PRO_0000027787

Chain

41 – 179

139

Factor X light chain

PRO_0000027788

Chain

183 – 488

306

Factor X heavy chain

PRO_0000027789

Propeptide

183 – 234

52

Activation peptide Ref.9

PRO_0000027790

Chain

235 – 488

254

Activated factor Xa heavy chain

PRO_0000027791

Regions

Domain

41 – 85

45

Gla

Domain

86 – 122

37

EGF-like 1; calcium-binding Potential

Domain

125 – 165

41

EGF-like 2

Domain

235 – 467

233

Peptidase S1

Region

183 – 203

21

O-glycosylated at one site

Region

476 – 485

10

O-glycosylated at one site

Sites

Active site

276

1

Charge relay system

Active site

322

1

Charge relay system

Active site

419

1

Charge relay system

Amino acid modifications

Modified residue

46

1

4-carboxyglutamate

Modified residue

47

1

4-carboxyglutamate

Modified residue

54

1

4-carboxyglutamate

Modified residue

56

1

4-carboxyglutamate

Modified residue

59

1

4-carboxyglutamate

Modified residue

60

1

4-carboxyglutamate

Modified residue

65

1

4-carboxyglutamate

Modified residue

66

1

4-carboxyglutamate

Modified residue

69

1

4-carboxyglutamate

Modified residue

72

1

4-carboxyglutamate

Modified residue

79

1

4-carboxyglutamate

Modified residue

103

1

(3R)-3-hydroxyaspartate

Glycosylation

199

1

O-linked (GalNAc...) Ref.9

Glycosylation

211

1

O-linked (GalNAc...) Ref.9

Glycosylation

221

1

N-linked (GlcNAc...) Ref.9

CAR_000012

Glycosylation

231

1

N-linked (GlcNAc...) Ref.9

CAR_000013

Disulfide bond

57 ↔ 62

By similarity

Disulfide bond

90 ↔ 101

Disulfide bond

95 ↔ 110

Disulfide bond

112 ↔ 121

Disulfide bond

129 ↔ 140

Disulfide bond

136 ↔ 149

Disulfide bond

151 ↔ 164

Disulfide bond

172 ↔ 342

Interchain (between light and heavy chains)

Disulfide bond

241 ↔ 246

Disulfide bond

261 ↔ 277

Disulfide bond

390 ↔ 404

Disulfide bond

415 ↔ 443

Natural variations

Natural variant

7

1

L → I. Ref.26
Corresponds to variant rs5963 [ dbSNP | Ensembl ].

VAR_014162

Natural variant

30

1

Q → H. Ref.26
Corresponds to variant rs5961 [ dbSNP | Ensembl ].

VAR_014163

Natural variant

47

1

E → G in FA10D; St. Louis II; strongly reduced activity; not activated by factor VIIa and tissue factor. Ref.24

VAR_065428

Natural variant

51

1

G → V in FA10D. Ref.35

VAR_065429

Natural variant

54

1

E → G in FA10D; Ketchikan. Ref.22

VAR_065430

Natural variant

54

1

E → K in FA10D; Vorarlberg; converts prothrombin at a normal rate but shows decreased affinity for calcium. Ref.18 Ref.28

VAR_065431

Natural variant

72

1

E → Q in FA10D; Tokyo. Ref.25

VAR_065432

Natural variant

91

1

E → K in FA10D; Riyadh. Ref.34

VAR_065433

Natural variant

142

1

E → K in FA10D; uncertain pathological significance; detected in patients carrying K-54 or P-374; slightly reduced activity. Ref.18 Ref.20 Ref.29

VAR_065434

Natural variant

149

1

C → Y in FA10D. Ref.28

VAR_065435

Natural variant

151

1

C → Y in FA10D. Ref.28

VAR_065436

Natural variant

152

1

A → T. Ref.3
Corresponds to variant rs3211772 [ dbSNP | Ensembl ].

VAR_020176

Natural variant

192

1

G → R. Ref.3
Corresponds to variant rs3211783 [ dbSNP | Ensembl ].

VAR_020177

Natural variant

289

1

G → R in FA10D; may affect splicing. Ref.28

VAR_065437

Natural variant

304

1

E → K in FA10D. Ref.28

VAR_065438

Natural variant

322

1

D → N in FA10D; Stockton; 50% decrease in specific activity. Ref.23

VAR_065439

Natural variant

327

1

R → W in FA10D. Ref.28

VAR_065440

Natural variant

338

1

V → M in FA10D. Ref.28

VAR_065441

Natural variant

350

1

E → K in FA10D. Ref.28

VAR_065442

Natural variant

358

1

T → M in FA10D; Roma. Ref.28

VAR_065443

Natural variant

363

1

G → S in FA10D. Ref.28

VAR_065444

Natural variant

366

1

R → C in FA10D; San Antonio. Ref.17

VAR_065445

Natural variant

374

1

S → P in FA10D; Marseille; decreased cleavage by factor IXa; normal catalytic efficiency for prothrombin. Ref.20 Ref.21 Ref.31

VAR_065446

Natural variant

383

1

P → S in FA10D; Friuli. Ref.19

VAR_065447

Natural variant

390

1

C → F in FA10D; Padua 4. Ref.32

VAR_065448

Natural variant

404

1

C → R in FA10D. Ref.28

VAR_065449

Natural variant

406

1

G → S in FA10D; almost complete loss of activity. Ref.33

VAR_065450

Natural variant

420

1

G → R in FA10D; Padua 3. Ref.31

VAR_065451

Natural variant

448

1

K → N in FA10D; San Giovanni Rotondo. Ref.30

VAR_065452

Experimental info

Sequence conflict

285 – 288

4

KVRV → E in AAA51984. Ref.6

Sequence conflict

285 – 288

4

KVRV → E in AAA52486. Ref.8

Sequence conflict

442

1

G → S in AAA52490. Ref.5

Secondary structure

1

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488

Helix Strand Turn

Details...

Helix

47 – 57

11

Helix

64 – 71

8

Helix

74 – 81

8

Beta strand

96 – 98

3

Beta strand

100 – 103

4

Beta strand

108 – 111

4

Beta strand

116 – 118

3

Helix

130 – 135

6

Beta strand

140 – 143

4

Beta strand

146 – 149

4

Beta strand

155 – 157

3

Beta strand

164 – 170

7

Beta strand

172 – 174

3

Turn

243 – 245

3

Beta strand

249 – 254

6

Turn

255 – 257

3

Beta strand

258 – 265

8

Beta strand

267 – 273

7

Helix

275 – 279

5

Beta strand

282 – 289

8

Beta strand

301 – 303

3

Beta strand

305 – 310

6

Turn

316 – 318

3

Beta strand

324 – 330

7

Helix

346 – 352

7

Turn

353 – 355

3

Beta strand

356 – 365

10

Beta strand

372 – 376

5

Beta strand

378 – 384

7

Helix

387 – 391

5

Beta strand

408 – 410

3

Beta strand

422 – 427

6

Beta strand

430 – 439

10

Beta strand

441 – 444

4

Beta strand

450 – 454

5

Helix

455 – 457

3

Helix

459 – 465

7

Sequences

	Sequence		Length	Mass (Da)
	P00742 [UniParc]. Last modified October 1, 1989. Version 2. Checksum: F81D5746AF4797AF	FASTA	488	54,732
	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

References

	« Hide 'large scale' referencesShow '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.
[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, 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. , 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

Wikipedia

Factor X entry

SeattleSNPs

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 , 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.

IPI

IPI00019576.

PIR

EXHU. A24478.

RefSeq

NP_000495.1. NM_000504.3.

UniGene

Hs.361463.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1C5M	X-ray	1.95	D	235-481	[»]
			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	235-481	[»]
			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	129-178	[»]
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	127-177	[»]
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	47-179	[»]
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	[»]

ProteinModelPortal

P00742.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29896N.

IntAct

P00742. 6 interactions.

MINT

MINT-276128.

STRING

9606.ENSP00000364709.

Protein family/group databases

MEROPS

S01.216.

PTM databases

GlycoSuiteDB

P00742.

PhosphoSite

P00742.

Polymorphism databases

DMDM

119761.

Proteomic databases

PaxDb

P00742.

PRIDE

P00742.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000375559; ENSP00000364709; ENSG00000126218.

GeneID

2159.

KEGG

hsa:2159.

UCSC

uc001vsx.3. human.

Organism-specific databases

CTD

2159.

GeneCards

GC13P113777.

HGNC

HGNC:3528. F10.

MIM

227600. phenotype.
613872. gene.

neXtProt

NX_P00742.

Orphanet

328. Congenital factor X deficiency.

PharmGKB

PA27940.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5640.

HOGENOM

HOG000251821.

HOVERGEN

HBG013304.

InParanoid

P00742.

KO

K01314.

OMA

PACLPQK.

OrthoDB

EOG447FTB.

PhylomeDB

P00742.

Enzyme and pathway databases

BioCyc

MetaCyc:HS05000-MONOMER.

Reactome

REACT_17015. Metabolism of proteins.
REACT_604. Hemostasis.

SABIO-RK

P00742.

Gene expression databases

ArrayExpress

P00742.

Bgee

P00742.

CleanEx

HS_F10.

Genevestigator

P00742.

GermOnline

ENSG00000126218. Homo sapiens.

Family and domain databases

Gene3D

4.10.740.10. 1 hit.

InterPro

IPR017857. Coagulation_fac_subgr_Gla_dom.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR000294. GLA_domain.
IPR012224. Pept_S1A_FX.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]

Pfam

PF00008. EGF. 1 hit.
PF00594. Gla. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]

PIRSF

PIRSF001143. Factor_X. 1 hit.

PRINTS

PR00722. CHYMOTRYPSIN.
PR00001. GLABLOOD.

SMART

SM00181. EGF. 1 hit.
SM00179. EGF_CA. 1 hit.
SM00069. GLA. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]

SUPFAM

SSF50494. Pept_Ser_Cys. 1 hit.
SSF57630. VitK_dep_GLA. 1 hit.

PROSITE

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]

ProtoNet

Search...

Other

BindingDB

P00742.

ChEMBL

CHEMBL244.

ChiTaRS

F10. human.

DrugBank

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.

EvolutionaryTrace

P00742.

GenomeRNAi

2159.

NextBio

8723.

PMAP-CutDB

P00742.

SOURCE

Search...

Entry information

Entry name

FA10_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 191 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.