Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P00742 (FA10_HUMAN)

Last modified June 16, 2009. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein namesRecommended name:
    Coagulation factor X
    EC=3.4.21.6
Alternative name(s):
    Stuart factor
    Stuart-Prower factor
Cleaved into the following 3 chains:
    1- Recommended name:
            Factor X light chain
    2- Recommended name:
            Factor X heavy chain
    3- Recommended name:
            Activated factor Xa heavy chain
Gene names
Name: F10
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Hide | Top

Protein attributes

Sequence length488 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

Hide | Top

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.

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.

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. Ref.9

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.

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.

Hide | Top

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Q169381EBI-719750,EBI-1646299From a different organism.
Q964Q01EBI-719750,EBI-1646347From a different organism.
PIIP041331EBI-719750,EBI-1646019From a different organism.

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131 Potential
Propeptide32 – 409 Ref.7
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
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

Sites

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

Amino acid modifications

Modified residue4614-carboxyglutamate
Modified residue4714-carboxyglutamate
Modified residue5414-carboxyglutamate
Modified residue5614-carboxyglutamate
Modified residue5914-carboxyglutamate
Modified residue6014-carboxyglutamate
Modified residue6514-carboxyglutamate
Modified residue6614-carboxyglutamate
Modified residue6914-carboxyglutamate
Modified residue7214-carboxyglutamate
Modified residue7914-carboxyglutamate
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: dbSNP rs5963. Ref.13
VAR_014162
Natural variant301Q → H: dbSNP rs5961. Ref.13
VAR_014163
Natural variant1521A → T: dbSNP rs3211772. Ref.3
VAR_020176
Natural variant1921G → R: dbSNP rs3211783. Ref.3
VAR_020177

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

1 ...................................................................... 488
Helix Strand Turn

Details...

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
P00742-1 [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

Hide | Top

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: 1902434] [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: 3768336] [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: 15489334] [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: 2582420] [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: 3011603] [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: 6871167] [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: 6587384] [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: 8243461] [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: 2612918] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-23.
[11]"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: 8355279] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 86-179 AND 235-278.
[12]"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: 9618463] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 86-179 AND 235-278.
[13]"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: 10391209] [Abstract]
Cited for: VARIANTS ILE-7 AND HIS-30.
[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)
+Additional computationally mapped references.

Hide | Top

Web resources

Wikipedia

Factor X entry

SeattleSNPs

Hide | Top

Cross-references

Sequence databases

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.
IPIIPI00019576.
PIREXHU. A24478.
RefSeqNP_000495.1.
UniGeneHs.361463

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1C5MX-ray1.95D235-481[»]
F84-179[»]
1EZQX-ray2.20A235-488[»]
B46-179[»]
1F0RX-ray2.10A235-488[»]
B46-179[»]
1F0SX-ray2.10A235-488[»]
B46-179[»]
1FAXX-ray3.00A235-481[»]
L84-179[»]
1FJSX-ray1.92A235-468[»]
L127-178[»]
1FXYX-ray2.15A-[»]
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[»]
1KYEX-ray2.22A235-468[»]
B128-178[»]
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[»]
B127-178[»]
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[»]
B46-179[»]
2W26X-ray2.08A235-468[»]
B127-177[»]
2W3IX-ray1.90A235-468[»]
B128-178[»]
2W3KX-ray2.05A235-468[»]
B128-178[»]
3CENX-ray1.60A235-468[»]
L127-178[»]
3CS7X-ray2.20A235-468[»]
L127-178[»]
3ENSX-ray2.30A/C85-178[»]
B/D235-472[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP00742. 6 interactions.

Protein family/group databases

MEROPSS01.216.

PTM databases

GlycoSuiteDBP00742.

Proteomic databases

PRIDEP00742.

Genome annotation databases

EnsemblENSG00000126218. Homo sapiens. [Contig view]
GeneID2159.
KEGGhsa:2159.

Organism-specific databases

GeneCardsGC13P112825.
H-InvDBHIX0026566.
HGNCHGNC:3528. F10.
MIM227600. gene+phenotype.
Orphanet328. Congenital factor X deficiency.
PharmGKBPA24967.
GenAtlasSearch...

Phylogenomic databases

HOGENOMP00742.
HOVERGENP00742.
OMAP00742. PYVDRNT.

Enzyme and pathway databases

BRENDA3.4.21.6. 247.
ReactomeREACT_1069. Post-translational protein modification.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpressP00742.
BgeeP00742.
CleanExHS_F10.
GermOnlineENSG00000126218. Homo sapiens.

Family and domain databases

InterProIPR002383. Coagulation_factor_Gla.
IPR006209. EGF.
IPR006210. EGF-like.
IPR013032. EGF-like_reg_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_CS.
IPR000742. EGF_3.
IPR001881. EGF_Ca_bd.
IPR018097. EGF_Ca_bd_CS.
IPR000294. GLA_domain.
IPR012224. Pept_S1A_FX.
IPR018114. Peptidase_S1/S6_AS.
IPR001254. Peptidase_S1_S6.
IPR001314. Peptidase_S1A.
[Graphical view]
PfamPF00008. EGF. 2 hits.
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]
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 Resources

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.
NextBio8723.
PMAP-CutDBP00742.
SOURCESearch...

Hide | Top

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: June 16, 2009
This is version 147 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Hide | Top

Relevant documents

Human chromosome 13

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents