[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1016/0378-1119(91)90141-W; PubMed=1902434 [NCBI, ExPASy, EBI, Israel, Japan] Messier T.L., Pittman D.D., Long G.L., Kaufman R.J., Church W.R.; "Cloning and expression in COS-1 cells of a full-length cDNA encoding human coagulation factor X."; Gene 99:291-294(1991).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1021/bi00366a018; PubMed=3768336 [NCBI, ExPASy, EBI, Israel, Japan] Leytus S.P., Foster D.C., Kurachi K., Davie E.W.; "Gene for human factor X: a blood coagulation factor whose gene organization is essentially identical with that of factor IX and protein C."; Biochemistry 25:5098-5102(1986).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-152 AND ARG-192. SeattleSNPs program for genomic applications; Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Ovary; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[5]	NUCLEOTIDE SEQUENCE [MRNA] OF 13-488. PubMed=2582420 [NCBI, ExPASy, EBI, Israel, Japan] Fung M.R., Hay C.W., McGillivray R.T.A.; "Characterization of an almost full-length cDNA coding for human blood coagulation factor X."; Proc. Natl. Acad. Sci. U.S.A. 82:3591-3595(1985).
[6]	NUCLEOTIDE SEQUENCE [MRNA] OF 19-488. TISSUE=Liver; DOI=10.1016/0378-1119(86)90112-5; PubMed=3011603 [NCBI, ExPASy, EBI, Israel, Japan] Kaul R.K., Hildebrand B., Roberts S., Jagadeeswaran P.; "Isolation and characterization of human blood-coagulation factor X cDNA."; Gene 41:311-314(1986).
[7]	PROTEIN SEQUENCE OF 41-179. DOI=10.1021/bi00281a016; PubMed=6871167 [NCBI, ExPASy, EBI, Israel, Japan] McMullen B.A., Fujikawa K., Kisiel W., Sasagawa T., Howald W.N., Kwa E.Y., Weinstein B.; "Complete amino acid sequence of the light chain of human blood coagulation factor X: evidence for identification of residue 63 as beta-hydroxyaspartic acid."; Biochemistry 22:2875-2884(1983).
[8]	NUCLEOTIDE SEQUENCE [MRNA] OF 115-488, AND TISSUE SPECIFICITY. TISSUE=Liver; PubMed=6587384 [NCBI, ExPASy, EBI, Israel, Japan] Leytus S.P., Chung D.W., Kisiel W., Kurachi K., Davie E.W.; "Characterization of a cDNA coding for human factor X."; Proc. Natl. Acad. Sci. U.S.A. 81:3699-3702(1984).
[9]	PROTEIN SEQUENCE OF 183-234, AND GLYCOSYLATION AT THR-199; THR-211; ASN-221 AND ASN-231. PubMed=8243461 [NCBI, ExPASy, EBI, Israel, Japan] Inoue K., Morita T.; "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."; Eur. J. Biochem. 218:153-163(1993).
[10]	NUCLEOTIDE SEQUENCE OF 1-23. DOI=10.1016/0378-1119(89)90529-5; PubMed=2612918 [NCBI, ExPASy, EBI, Israel, Japan] Jagadeeswaran P., Reddy S.V., Rao K.J., Hamsabhushanam K., Lyman G.; "Cloning and characterization of the 5' end (exon 1) of the gene encoding human factor X."; Gene 84:517-519(1989).
[11]	X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 86-179 AND 235-278. DOI=10.1006/jmbi.1993.1441; PubMed=8355279 [NCBI, ExPASy, EBI, Israel, Japan] Padmanabhan K., Padmanabhan K.P., Tulinsky A., Park C.H., Bode W., Huber R., Blankenship D.T., Cardin A.D., Kisiel W.; "Structure of human des(1-45) factor Xa at 2.2-A resolution."; J. Mol. Biol. 232:947-966(1993).
[12]	X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 86-179 AND 235-278. DOI=10.1073/pnas.95.12.6630; PubMed=9618463 [NCBI, ExPASy, EBI, Israel, Japan] Kamata K., Kawamoto H., Honma T., Iwama T., Kim S.H.; "Structural basis for chemical inhibition of human blood coagulation factor Xa."; Proc. Natl. Acad. Sci. U.S.A. 95:6630-6635(1998).
[13]	VARIANTS ILE-7 AND HIS-30. DOI=10.1038/10290; PubMed=10391209 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Characterization of single-nucleotide polymorphisms in coding regions of human genes."; Nat. Genet. 22:231-238(1999).
[14]	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).

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.
SUBUNIT: 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.
INTERACTION:
Q16938:- (xeno); NbExp=1; IntAct=EBI-719750, EBI-1646299;
Q964Q0:- (xeno); NbExp=1; IntAct=EBI-719750, EBI-1646347;
P04133:PII (xeno); NbExp=1; IntAct=EBI-719750, EBI-1646019;
SUBCELLULAR LOCATION: Secreted.
TISSUE SPECIFICITY: Plasma; synthesized in the liver.
PTM: The vitamin K-dependent, enzymatic carboxylation of some glutamate residues allows the modified protein to bind calcium.
PTM: N- and O-glycosylated.
PTM: The activation peptide is cleaved by factor IXa (in the intrinsic pathway), or by factor VIIa (in the extrinsic pathway).
SIMILARITY: Belongs to the peptidase S1 family [view classification].
SIMILARITY: Contains 2 EGF-like domains.
SIMILARITY: Contains 1 Gla (gamma-carboxy-glutamate) domain.
SIMILARITY: Contains 1 peptidase S1 domain [view classification].
WEB RESOURCE: Name=Wikipedia; Note=Factor X entry; URL="http://en.wikipedia.org/wiki/Factor_X";.
WEB RESOURCE: Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/f10/";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

K03194; AAA52490.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M57285; AAA52421.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF503510; AAM19347.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC046125; AAH46125.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L29433; AAA52764.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L00390; AAA52764.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L00391; AAA52764.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L00392; AAA52764.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L00393; AAA52764.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L00394; AAA52764.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L00395; AAA52764.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L00396; AAA52764.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M22613; AAA51984.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
K01886; AAA52486.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M33297; AAA52636.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A24478; EXHU.

NP_000495.1; -.

3D structure databases

PDB

1C5M; X-ray; 1.95 A; D=235-481, F=84-179.	[ExPASy / RCSB / EBI]
1EZQ; X-ray; 2.20 A; A=235-488, B=46-179.	[ExPASy / RCSB / EBI]
1F0R; X-ray; 2.10 A; A=235-488, B=46-179.	[ExPASy / RCSB / EBI]
1F0S; X-ray; 2.10 A; A=235-488, B=46-179.	[ExPASy / RCSB / EBI]
1FAX; X-ray; 3.00 A; A=235-481, L=84-179.	[ExPASy / RCSB / EBI]
1FJS; X-ray; 1.92 A; A=235-468, L=127-178.	[ExPASy / RCSB / EBI]
1FXY; X-ray; 2.15 A; A=-.	[ExPASy / RCSB / EBI]
1G2L; X-ray; 1.90 A; A=235-469, B=86-179.	[ExPASy / RCSB / EBI]
1G2M; X-ray; 3.02 A; A=235-469, B=86-179.	[ExPASy / RCSB / EBI]
1HCG; X-ray; 2.20 A; A=235-475, B=129-179.	[ExPASy / RCSB / EBI]
1IOE; X-ray; 2.90 A; A=235-469, L=84-179.	[ExPASy / RCSB / EBI]
1IQE; X-ray; 2.90 A; A=235-469, L=84-179.	[ExPASy / RCSB / EBI]
1IQF; X-ray; 3.20 A; A=235-469, L=84-179.	[ExPASy / RCSB / EBI]
1IQG; X-ray; 2.60 A; A=235-469, L=84-179.	[ExPASy / RCSB / EBI]
1IQH; X-ray; 3.00 A; A=235-469, L=84-179.	[ExPASy / RCSB / EBI]
1IQI; X-ray; 2.90 A; A=235-469, L=84-179.	[ExPASy / RCSB / EBI]
1IQJ; X-ray; 3.00 A; A=235-469, L=84-179.	[ExPASy / RCSB / EBI]
1IQK; X-ray; 3.20 A; A=235-469, L=84-179.	[ExPASy / RCSB / EBI]
1IQL; X-ray; 2.70 A; A=235-469, L=84-179.	[ExPASy / RCSB / EBI]
1IQM; X-ray; 2.60 A; A=235-469, L=84-179.	[ExPASy / RCSB / EBI]
1IQN; X-ray; 2.60 A; A=235-469, L=84-179.	[ExPASy / RCSB / EBI]
1KSN; X-ray; 2.10 A; A=235-488, B=46-179.	[ExPASy / RCSB / EBI]
1KYE; X-ray; 2.22 A; A=235-468, B=128-178.	[ExPASy / RCSB / EBI]
1LPG; X-ray; 2.00 A; A=46-179, B=235-488.	[ExPASy / RCSB / EBI]
1LPK; X-ray; 2.20 A; A=46-179, B=235-488.	[ExPASy / RCSB / EBI]
1LPZ; X-ray; 2.40 A; A=46-179, B=235-488.	[ExPASy / RCSB / EBI]
1LQD; X-ray; 2.70 A; A=46-179, B=235-488.	[ExPASy / RCSB / EBI]
1MQ5; X-ray; 2.10 A; A=235-467, L=127-177.	[ExPASy / RCSB / EBI]
1MQ6; X-ray; 2.10 A; A=235-467, L=127-177.	[ExPASy / RCSB / EBI]
1MSX; Model; -; A=235-469.	[ExPASy / RCSB / EBI]
1NFU; X-ray; 2.05 A; A=235-488, B=46-240.	[ExPASy / RCSB / EBI]
1NFW; X-ray; 2.10 A; A=235-488, B=46-179.	[ExPASy / RCSB / EBI]
1NFX; X-ray; 2.15 A; A=235-488, B=46-179.	[ExPASy / RCSB / EBI]
1NFY; X-ray; 2.10 A; A=235-488, B=46-179.	[ExPASy / RCSB / EBI]
1NL8; Model; -; F=235-469, L=41-179.	[ExPASy / RCSB / EBI]
1P0S; X-ray; 2.80 A; H=235-488, L=41-178.	[ExPASy / RCSB / EBI]
1V3X; X-ray; 2.20 A; A=235-467, B=127-178.	[ExPASy / RCSB / EBI]
1WU1; X-ray; 2.30 A; A=235-467, B=85-179.	[ExPASy / RCSB / EBI]
1XKA; X-ray; 2.30 A; C=235-469, L=85-179.	[ExPASy / RCSB / EBI]
1XKB; X-ray; 2.40 A; A/B=85-179, C/D=235-469.	[ExPASy / RCSB / EBI]
1Z6E; X-ray; 1.80 A; A=235-468, B=127-178.	[ExPASy / RCSB / EBI]
2BMG; X-ray; 2.70 A; A=126-178, B=235-468.	[ExPASy / RCSB / EBI]
2BOH; X-ray; 2.20 A; A=46-179, B=235-488.	[ExPASy / RCSB / EBI]
2BOK; X-ray; 1.64 A; A=235-475, L=126-180.	[ExPASy / RCSB / EBI]
2BQ6; X-ray; 3.00 A; A=126-177, B=220-468.	[ExPASy / RCSB / EBI]
2BQ7; X-ray; 2.20 A; A=126-177, B=220-468.	[ExPASy / RCSB / EBI]
2BQW; X-ray; 2.95 A; A=126-177, B=220-468.	[ExPASy / RCSB / EBI]
2CJI; X-ray; 2.10 A; A=235-488, B=46-179.	[ExPASy / RCSB / EBI]
2D1J; X-ray; 2.20 A; A=235-467, B=125-178.	[ExPASy / RCSB / EBI]
2EI6; X-ray; 2.30 A; A=235-467, B=125-178.	[ExPASy / RCSB / EBI]
2EI7; X-ray; 2.30 A; A=235-467, B=125-178.	[ExPASy / RCSB / EBI]
2EI8; X-ray; 2.10 A; A=235-467, B=125-178.	[ExPASy / RCSB / EBI]
2FZZ; X-ray; 2.20 A; A=235-468, L=127-178.	[ExPASy / RCSB / EBI]
2G00; X-ray; 2.10 A; A=235-468, L=127-178.	[ExPASy / RCSB / EBI]
2GD4; X-ray; 3.30 A; A/L=126-182, B/H=235-475.	[ExPASy / RCSB / EBI]
2H9E; X-ray; 2.20 A; H=235-467, L=86-234.	[ExPASy / RCSB / EBI]
2J2U; X-ray; 1.90 A; A=235-488, B=46-179.	[ExPASy / RCSB / EBI]
2J34; X-ray; 2.01 A; A=235-488, B=46-179.	[ExPASy / RCSB / EBI]
2J38; X-ray; 2.10 A; A=235-488, B=46-179.	[ExPASy / RCSB / EBI]
2J4I; X-ray; 1.80 A; A=235-488, B=46-179.	[ExPASy / RCSB / EBI]
2J94; X-ray; 2.10 A; A=235-488, B=46-179.	[ExPASy / RCSB / EBI]
2J95; X-ray; 2.01 A; A=235-488, B=46-179.	[ExPASy / RCSB / EBI]
2P16; X-ray; 2.30 A; A=235-468, L=127-178.	[ExPASy / RCSB / EBI]
2P3F; X-ray; 3.10 A; H=235-469, L=125-178.	[ExPASy / RCSB / EBI]
2P3T; X-ray; 1.92 A; A=127-178, B=235-467.	[ExPASy / RCSB / EBI]
2P3U; X-ray; 1.62 A; A=127-178, B=235-467.	[ExPASy / RCSB / EBI]
2P93; X-ray; 1.90 A; A=235-468, L=127-178.	[ExPASy / RCSB / EBI]
2P94; X-ray; 1.80 A; A=235-468, L=127-178.	[ExPASy / RCSB / EBI]
2P95; X-ray; 2.20 A; A=235-468, L=127-178.	[ExPASy / RCSB / EBI]
2PHB; X-ray; 2.30 A; A=235-468, B=128-178.	[ExPASy / RCSB / EBI]
2PR3; X-ray; 1.50 A; A=235-468, B=128-178.	[ExPASy / RCSB / EBI]
2Q1J; X-ray; 1.90 A; A=235-468, B=128-178.	[ExPASy / RCSB / EBI]
2RA0; X-ray; 2.30 A; A=235-468, L=128-178.	[ExPASy / RCSB / EBI]
2UWL; X-ray; 1.90 A; A=235-488, B=46-179.	[ExPASy / RCSB / EBI]
2UWO; X-ray; 1.75 A; A=235-488, B=46-179.	[ExPASy / RCSB / EBI]
2UWP; X-ray; 1.75 A; A=235-488, B=46-179.	[ExPASy / RCSB / EBI]
3CEN; X-ray; 1.60 A; A=235-468, L=127-178.	[ExPASy / RCSB / EBI]
3CS7; X-ray; 2.20 A; A=235-468, L=127-178.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1C5M; -.
1EZQ; -.
1F0R; -.
1F0S; -.
1FAX; -.
1FJS; -.
1FXY; -.
1G2L; -.
1G2M; -.
1HCG; -.
1IOE; -.
1IQE; -.
1IQF; -.
1IQG; -.
1IQH; -.
1IQI; -.
1IQJ; -.
1IQK; -.
1IQL; -.
1IQM; -.
1IQN; -.
1KSN; -.
1KYE; -.
1LPG; -.
1LPK; -.
1LPZ; -.
1LQD; -.
1MQ5; -.
1MQ6; -.
1MSX; -.
1NFU; -.
1NFW; -.
1NFX; -.
1NFY; -.
1NL8; -.
1P0S; -.
1V3X; -.
1WU1; -.
1XKA; -.
1XKB; -.
1Z6E; -.
2BMG; -.
2BOH; -.
2BOK; -.
2BQ6; -.
2BQ7; -.
2BQW; -.
2CJI; -.
2D1J; -.
2EI6; -.
2EI7; -.
2EI8; -.
2FZZ; -.
2G00; -.
2GD4; -.
2H9E; -.
2J2U; -.
2J34; -.
2J38; -.
2J4I; -.
2J94; -.
2J95; -.
2P16; -.
2P3F; -.
2P3T; -.
2P3U; -.
2P93; -.
2P94; -.
2P95; -.
2PHB; -.
2PR3; -.
2Q1J; -.
2RA0; -.
2UWL; -.
2UWO; -.
2UWP; -.
3CEN; -.
3CS7; -.

ModBase

P00742.

Protein-protein interaction databases

IntAct

P00742; 6.

Protein family/group databases

MEROPS

S01.216; -.

PTM databases

GlycoSuiteDB

P00742; -.

Enzyme and pathway databases

Reactome

REACT_1069; Post-translational protein modification.
REACT_604; Hemostasis.

Organism-specific databases

GC13P112825; -.

HIX0026566; -.

HGNC:3528; F10.

F10.

227600; gene+phenotype. [NCBI / EBI]

Orphanet

328; Factor X deficiency, congenital.

PharmGKB

PA24967; -.

GeneCards

P00742.

Gene expression databases

ArrayExpress

P00742; -.

CleanEx

HS_F10; -.

GermOnline

ENSG00000126218; Homo sapiens.

Ontologies

GO:0005576;	Cellular component: extracellular region (non-traceable author statement from UniProtKB).
GO:0005886;	Cellular component: plasma membrane (inferred from experiment from Reactome).
GO:0005509;	Molecular function: calcium ion binding (inferred from electronic annotation from InterPro).
GO:0003804;	Molecular function: coagulation factor Xa activity (inferred from experiment from Reactome).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0004252;	Molecular function: serine-type endopeptidase activity (traceable author statement from ProtInc).
GO:0007598;	Biological process: blood coagulation, extrinsic pathway (inferred from experiment from Reactome).
GO:0006508;	Biological process: proteolysis (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR002383; Coagulation_factor_Gla.
IPR006210; EGF.
IPR000152; EGF-type_Asp/Asn_hydroxyl_CS.
IPR001438; EGF_2.
IPR000742; EGF_3.
IPR001881; EGF_Ca_bd.
IPR006209; EGF_like.
IPR013032; EGF_like_reg_CS.
IPR012224; Pept_S1A_FX.
IPR001254; Peptidase_S1_S6.
IPR001314; Peptidase_S1A.
IPR000294; VitK_dep_GLA.
Graphical view of domain structure.

Pfam

PF00008; EGF; 2.
PF00594; Gla; 1.
PF00089; Trypsin; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF001143; Factor_X; 1.

PRINTS

PR00722; CHYMOTRYPSIN.
PR00010; EGFBLOOD.
PR00001; GLABLOOD.

SMART

SM00181; EGF; 1.
SM00179; EGF_CA; 1.
SM00069; GLA; 1.
SM00020; Tryp_SPc; 1.
SMART graphical view of domain structure.

PROSITE

PS00010; ASX_HYDROXYL; 1.
PS00022; EGF_1; 1.
PS01186; EGF_2; 2.
PS50026; EGF_3; 1.
PS01187; EGF_CA; 1.
PS00011; GLA_1; 1.
PS50998; GLA_2; 1.
PS50240; TRYPSIN_DOM; 1.
PS00134; TRYPSIN_HIS; 1.
PS00135; TRYPSIN_SER; 1.
PROSITE graphical view of domain structure (profiles).

Proteomics databases

PRIDE

P00742; -.

Genome annotation databases

Ensembl

ENSG00000126218; Homo sapiens. [Contig view]

GeneID

2159; -.

KEGG

hsa:2159; -.

Phylogenomic databases

HOGENOM

P00742; -.

HOVERGEN

P00742; -.

Other

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.

P00742; -.

8723; -.

F10; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Blood coagulation; Calcium; Cleavage on pair of basic residues; Direct protein sequencing; EGF-like domain; Gamma-carboxyglutamic acid; Glycoprotein; Hydrolase; Hydroxylation; Polymorphism; Protease; Repeat; Secreted; Serine protease; Signal; Zymogen.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 31`	`31`	`Potential.`
`PROPEP`	`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`
`PROPEP`	`183 234`	`52`	`Activation peptide.`	`PRO_0000027790`
`CHAIN`	`235 488`	`254`	`Activated factor Xa heavy chain.`	`PRO_0000027791`
`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.`
`ACT_SITE`	`276 276`		`Charge relay system.`
`ACT_SITE`	`322 322`		`Charge relay system.`
`ACT_SITE`	`419 419`		`Charge relay system.`
`MOD_RES`	`46 46`		`4-carboxyglutamate.`
`MOD_RES`	`47 47`		`4-carboxyglutamate.`
`MOD_RES`	`54 54`		`4-carboxyglutamate.`
`MOD_RES`	`56 56`		`4-carboxyglutamate.`
`MOD_RES`	`59 59`		`4-carboxyglutamate.`
`MOD_RES`	`60 60`		`4-carboxyglutamate.`
`MOD_RES`	`65 65`		`4-carboxyglutamate.`
`MOD_RES`	`66 66`		`4-carboxyglutamate.`
`MOD_RES`	`69 69`		`4-carboxyglutamate.`
`MOD_RES`	`72 72`		`4-carboxyglutamate.`
`MOD_RES`	`79 79`		`4-carboxyglutamate.`
`MOD_RES`	`103 103`		`3-hydroxyaspartate.`
`CARBOHYD`	`199 199`		`O-linked (GalNAc...).`
`CARBOHYD`	`211 211`		`O-linked (GalNAc...).`
`CARBOHYD`	`221 221`		`N-linked (GlcNAc...) [GlycoSuiteDB].`	`CAR_000012`
`CARBOHYD`	`231 231`		`N-linked (GlcNAc...) [GlycoSuiteDB].`	`CAR_000013`
`DISULFID`	`57 62`		`By similarity.`
`DISULFID`	`90 101`
`DISULFID`	`95 110`
`DISULFID`	`112 121`
`DISULFID`	`129 140`
`DISULFID`	`136 149`
`DISULFID`	`151 164`
`DISULFID`	`172 342`		`Interchain (between light and heavy chains).`
`DISULFID`	`241 246`
`DISULFID`	`261 277`
`DISULFID`	`390 404`
`DISULFID`	`415 443`
`VARIANT`	`7 7`	`1`	`L -> I (in dbSNP:rs5963 [NCBI]).`	`VAR_014162`
`VARIANT`	`30 30`