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Protein

Coagulation factor X

Gene

F10

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Factor Xa is a vitamin K-dependent glycoprotein that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting.

Catalytic activityi

Selective cleavage of Arg-|-Thr and then Arg-|-Ile bonds in prothrombin to form thrombin.

Enzyme regulationi

Inhibited by SERPINA5 and SERPINA10.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei276Charge relay system1
Active sitei322Charge relay system1
Active sitei419Charge relay system1

GO - Molecular functioni

  • calcium ion binding Source: InterPro
  • phospholipid binding Source: BHF-UCL
  • serine-type endopeptidase activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Blood coagulation, Hemostasis

Keywords - Ligandi

Calcium

Enzyme and pathway databases

BioCyciMetaCyc:HS05000-MONOMER.
ZFISH:HS05000-MONOMER.
BRENDAi3.4.21.6. 2681.
ReactomeiR-HSA-140834. Extrinsic Pathway of Fibrin Clot Formation.
R-HSA-140837. Intrinsic Pathway of Fibrin Clot Formation.
R-HSA-140875. Common Pathway of Fibrin Clot Formation.
R-HSA-159740. Gamma-carboxylation of protein precursors.
R-HSA-159763. Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
R-HSA-159782. Removal of aminoterminal propeptides from gamma-carboxylated proteins.
SABIO-RKP00742.
SIGNORiP00742.

Protein family/group databases

MEROPSiS01.216.

Names & Taxonomyi

Protein namesi
Recommended name:
Coagulation factor X (EC:3.4.21.6)
Alternative name(s):
Stuart factor
Stuart-Prower factor
Cleaved into the following 3 chains:
Gene namesi
Name:F10
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 13

Organism-specific databases

HGNCiHGNC:3528. F10.

Subcellular locationi

GO - Cellular componenti

  • endoplasmic reticulum lumen Source: Reactome
  • extracellular region Source: UniProtKB
  • Golgi lumen Source: Reactome
  • intrinsic component of external side of plasma membrane Source: BHF-UCL
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Factor X deficiency (FA10D)20 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:227600
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06542847E → G in FA10D; St. Louis II; strongly reduced activity; not activated by factor VIIa and tissue factor. 1 PublicationCorresponds to variant rs121964943dbSNPEnsembl.1
Natural variantiVAR_06542951G → V in FA10D. 1 PublicationCorresponds to variant rs751782758dbSNPEnsembl.1
Natural variantiVAR_06543054E → G in FA10D; Ketchikan. 1 PublicationCorresponds to variant rs121964944dbSNPEnsembl.1
Natural variantiVAR_06543154E → K in FA10D; Vorarlberg; converts prothrombin at a normal rate but shows decreased affinity for calcium. 2 PublicationsCorresponds to variant rs121964939dbSNPEnsembl.1
Natural variantiVAR_06543272E → Q in FA10D; Tokyo. 1 PublicationCorresponds to variant rs121964945dbSNPEnsembl.1
Natural variantiVAR_06543391E → K in FA10D; Riyadh. 1 Publication1
Natural variantiVAR_065434142E → K in FA10D; uncertain pathological significance; detected in patients carrying K-54 or P-374; slightly reduced activity. 3 PublicationsCorresponds to variant rs61753266dbSNPEnsembl.1
Natural variantiVAR_065435149C → Y in FA10D. 1 Publication1
Natural variantiVAR_065436151C → Y in FA10D. 1 Publication1
Natural variantiVAR_075212176 – 186Missing in FA10D; unknown pathological significance. 1 PublicationAdd BLAST11
Natural variantiVAR_075213262G → D in FA10D; unknown pathological significance. 1 Publication1
Natural variantiVAR_065437289G → R in FA10D; may affect splicing. 1 PublicationCorresponds to variant rs121964946dbSNPEnsembl.1
Natural variantiVAR_065438304E → K in FA10D. 1 PublicationCorresponds to variant rs747292771dbSNPEnsembl.1
Natural variantiVAR_065439322D → N in FA10D; Stockton; 50% decrease in specific activity. 2 PublicationsCorresponds to variant rs121964942dbSNPEnsembl.1
Natural variantiVAR_065440327R → W in FA10D. 1 PublicationCorresponds to variant rs770119164dbSNPEnsembl.1
Natural variantiVAR_065441338V → M in FA10D. 1 PublicationCorresponds to variant rs121964947dbSNPEnsembl.1
Natural variantiVAR_065442350E → K in FA10D. 1 PublicationCorresponds to variant rs372309538dbSNPEnsembl.1
Natural variantiVAR_065443358T → M in FA10D; Roma. 2 PublicationsCorresponds to variant rs768222784dbSNPEnsembl.1
Natural variantiVAR_065444363G → S in FA10D. 1 Publication1
Natural variantiVAR_065445366R → C in FA10D; San Antonio. 1 PublicationCorresponds to variant rs104894392dbSNPEnsembl.1
Natural variantiVAR_065446374S → P in FA10D; Marseille; decreased cleavage by factor IXa; normal catalytic efficiency for prothrombin. 3 PublicationsCorresponds to variant rs121964941dbSNPEnsembl.1
Natural variantiVAR_072751382V → A in FA10D; partial loss of activity. 2 Publications1
Natural variantiVAR_065447383P → S in FA10D; Friuli. 1 PublicationCorresponds to variant rs121964940dbSNPEnsembl.1
Natural variantiVAR_065448390C → F in FA10D; Padua 4. 1 PublicationCorresponds to variant rs199778916dbSNPEnsembl.1
Natural variantiVAR_065449404C → R in FA10D. 1 Publication1
Natural variantiVAR_065450406G → S in FA10D; almost complete loss of activity. 2 PublicationsCorresponds to variant rs376163818dbSNPEnsembl.1
Natural variantiVAR_065451420G → R in FA10D; Padua 3. 1 PublicationCorresponds to variant rs750759634dbSNPEnsembl.1
Natural variantiVAR_072752421G → D in FA10D; significant loss of activity. 2 PublicationsCorresponds to variant rs758726161dbSNPEnsembl.1
Natural variantiVAR_065452448K → N in FA10D; San Giovanni Rotondo. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi2159.
MalaCardsiF10.
MIMi227600. phenotype.
OpenTargetsiENSG00000126218.
Orphaneti328. Congenital factor X deficiency.
PharmGKBiPA27940.

Chemistry databases

ChEMBLiCHEMBL244.
DrugBankiDB00025. Antihemophilic Factor (Recombinant).
DB06605. Apixaban.
DB00100. Coagulation Factor IX.
DB00036. Coagulation factor VIIa.
DB09075. Edoxaban.
DB01225. Enoxaparin.
DB00569. Fondaparinux sodium.
DB01109. Heparin.
DB00170. Menadione.
DB06228. Rivaroxaban.
GuidetoPHARMACOLOGYi2359.

Polymorphism and mutation databases

BioMutaiF10.
DMDMi119761.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 31Sequence analysisAdd BLAST31
PropeptideiPRO_000002778632 – 401 Publication9
ChainiPRO_000002778741 – 488Coagulation factor XAdd BLAST448
ChainiPRO_000002778841 – 179Factor X light chainAdd BLAST139
ChainiPRO_0000027789183 – 488Factor X heavy chainAdd BLAST306
PropeptideiPRO_0000027790183 – 234Activation peptideAdd BLAST52
ChainiPRO_0000027791235 – 488Activated factor Xa heavy chainAdd BLAST254

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei464-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei474-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei544-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei564-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Disulfide bondi57 ↔ 62By similarity
Modified residuei594-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei604-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei654-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei664-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei694-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei724-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei794-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Disulfide bondi90 ↔ 101
Disulfide bondi95 ↔ 110
Modified residuei103(3R)-3-hydroxyaspartate1 Publication1
Disulfide bondi112 ↔ 121
Disulfide bondi129 ↔ 140
Disulfide bondi136 ↔ 149
Disulfide bondi151 ↔ 164
Disulfide bondi172 ↔ 342Interchain (between light and heavy chains)
Glycosylationi199O-linked (GalNAc...)1 Publication1
Glycosylationi211O-linked (GalNAc...)1 Publication1
GlycosylationiCAR_000012221N-linked (GlcNAc...)1 Publication1
GlycosylationiCAR_000013231N-linked (GlcNAc...)1 Publication1
Disulfide bondi241 ↔ 246
Disulfide bondi261 ↔ 277
Disulfide bondi390 ↔ 404
Disulfide bondi415 ↔ 443

Post-translational modificationi

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

Keywords - PTMi

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

Proteomic databases

EPDiP00742.
PaxDbiP00742.
PeptideAtlasiP00742.
PRIDEiP00742.

PTM databases

iPTMnetiP00742.
PhosphoSitePlusiP00742.
UniCarbKBiP00742.

Miscellaneous databases

PMAP-CutDBP00742.

Expressioni

Tissue specificityi

Plasma; synthesized in the liver.1 Publication

Gene expression databases

BgeeiENSG00000126218.
CleanExiHS_F10.
ExpressionAtlasiP00742. baseline and differential.
GenevisibleiP00742. HS.

Interactioni

Subunit structurei

The two chains are formed from a single-chain precursor by the excision of two Arg residues and are held together by 1 or more disulfide bonds. Forms a heterodimer with SERPINA5.

Protein-protein interaction databases

BioGridi108457. 8 interactors.
DIPiDIP-29896N.
IntActiP00742. 9 interactors.
MINTiMINT-276128.
STRINGi9606.ENSP00000364709.

Chemistry databases

BindingDBiP00742.

Structurei

Secondary structure

1488
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi47 – 57Combined sources11
Helixi64 – 71Combined sources8
Helixi74 – 81Combined sources8
Turni89 – 92Combined sources4
Beta strandi96 – 98Combined sources3
Beta strandi100 – 102Combined sources3
Beta strandi105 – 107Combined sources3
Beta strandi109 – 111Combined sources3
Beta strandi116 – 118Combined sources3
Beta strandi123 – 125Combined sources3
Turni129 – 131Combined sources3
Helixi132 – 135Combined sources4
Beta strandi137 – 143Combined sources7
Beta strandi146 – 150Combined sources5
Beta strandi155 – 157Combined sources3
Beta strandi164 – 170Combined sources7
Beta strandi172 – 174Combined sources3
Beta strandi236 – 240Combined sources5
Turni243 – 245Combined sources3
Beta strandi249 – 253Combined sources5
Turni255 – 257Combined sources3
Beta strandi259 – 265Combined sources7
Beta strandi267 – 273Combined sources7
Helixi275 – 279Combined sources5
Beta strandi280 – 283Combined sources4
Beta strandi285 – 289Combined sources5
Beta strandi291 – 295Combined sources5
Beta strandi301 – 303Combined sources3
Beta strandi305 – 310Combined sources6
Turni316 – 319Combined sources4
Beta strandi324 – 330Combined sources7
Helixi346 – 352Combined sources7
Turni353 – 355Combined sources3
Beta strandi356 – 364Combined sources9
Beta strandi366 – 368Combined sources3
Beta strandi372 – 376Combined sources5
Beta strandi378 – 385Combined sources8
Helixi387 – 393Combined sources7
Beta strandi402 – 406Combined sources5
Beta strandi408 – 411Combined sources4
Turni416 – 420Combined sources5
Beta strandi422 – 427Combined sources6
Beta strandi430 – 439Combined sources10
Beta strandi441 – 444Combined sources4
Beta strandi450 – 454Combined sources5
Helixi455 – 458Combined sources4
Helixi459 – 465Combined sources7
Beta strandi471 – 473Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4Y6DX-ray1.55A235-488[»]
B46-179[»]
4Y71X-ray1.80A235-488[»]
B46-179[»]
4Y76X-ray2.00A235-488[»]
B46-179[»]
4Y79X-ray2.10A235-488[»]
B46-179[»]
4Y7AX-ray1.99A235-488[»]
B46-179[»]
4Y7BX-ray1.79A235-488[»]
B46-179[»]
4ZH8X-ray1.80A235-488[»]
B46-179[»]
4ZHAX-ray1.86A235-488[»]
B46-179[»]
5K0HX-ray2.20A235-468[»]
B128-178[»]
ProteinModelPortaliP00742.
SMRiP00742.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00742.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini41 – 85GlaPROSITE-ProRule annotationAdd BLAST45
Domaini86 – 122EGF-like 1; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini125 – 165EGF-like 2PROSITE-ProRule annotationAdd BLAST41
Domaini235 – 467Peptidase S1PROSITE-ProRule annotationAdd BLAST233

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni183 – 203O-glycosylated at one siteAdd BLAST21
Regioni476 – 485O-glycosylated at one site10

Sequence similaritiesi

Belongs to the peptidase S1 family.PROSITE-ProRule annotation
Contains 2 EGF-like domains.PROSITE-ProRule annotation
Contains 1 Gla (gamma-carboxy-glutamate) domain.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IGPV. Eukaryota.
COG5640. LUCA.
GeneTreeiENSGT00760000118890.
HOGENOMiHOG000251821.
HOVERGENiHBG013304.
InParanoidiP00742.
KOiK01314.
OMAiEMAHEVE.
OrthoDBiEOG091G0AH5.
PhylomeDBiP00742.
TreeFamiTF327329.

Family and domain databases

CDDicd00190. Tryp_SPc. 1 hit.
Gene3Di4.10.740.10. 1 hit.
InterProiIPR017857. Coagulation_fac_subgr_Gla_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR000294. GLA_domain.
IPR012224. Pept_S1A_FX.
IPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[Graphical view]
PfamiPF00008. EGF. 1 hit.
PF00594. Gla. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFiPIRSF001143. Factor_X. 1 hit.
PRINTSiPR00722. CHYMOTRYPSIN.
PR00001. GLABLOOD.
SMARTiSM00181. EGF. 2 hits.
SM00179. EGF_CA. 1 hit.
SM00069. GLA. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 2 hits.
SSF57630. SSF57630. 1 hit.
PROSITEiPS00010. ASX_HYDROXYL. 1 hit.
PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 2 hits.
PS50026. EGF_3. 1 hit.
PS01187. EGF_CA. 1 hit.
PS00011. GLA_1. 1 hit.
PS50998. GLA_2. 1 hit.
PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00742-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGRPLHLVLL SASLAGLLLL GESLFIRREQ ANNILARVTR ANSFLEEMKK
60 70 80 90 100
GHLERECMEE TCSYEEAREV FEDSDKTNEF WNKYKDGDQC ETSPCQNQGK
110 120 130 140 150
CKDGLGEYTC TCLEGFEGKN CELFTRKLCS LDNGDCDQFC HEEQNSVVCS
160 170 180 190 200
CARGYTLADN GKACIPTGPY PCGKQTLERR KRSVAQATSS SGEAPDSITW
210 220 230 240 250
KPYDAADLDP TENPFDLLDF NQTQPERGDN NLTRIVGGQE CKDGECPWQA
260 270 280 290 300
LLINEENEGF CGGTILSEFY ILTAAHCLYQ AKRFKVRVGD RNTEQEEGGE
310 320 330 340 350
AVHEVEVVIK HNRFTKETYD FDIAVLRLKT PITFRMNVAP ACLPERDWAE
360 370 380 390 400
STLMTQKTGI VSGFGRTHEK GRQSTRLKML EVPYVDRNSC KLSSSFIITQ
410 420 430 440 450
NMFCAGYDTK QEDACQGDSG GPHVTRFKDT YFVTGIVSWG EGCARKGKYG
460 470 480
IYTKVTAFLK WIDRSMKTRG LPKAKSHAPE VITSSPLK
Length:488
Mass (Da):54,732
Last modified:October 1, 1989 - v2
Checksum:iF81D5746AF4797AF
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti285 – 288KVRV → E in AAA51984 (PubMed:3011603).Curated4
Sequence conflicti285 – 288KVRV → E in AAA52486 (PubMed:6587384).Curated4
Sequence conflicti442G → S in AAA52490 (PubMed:2582420).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0141627L → I.1 PublicationCorresponds to variant rs5963dbSNPEnsembl.1
Natural variantiVAR_01416330Q → H.1 PublicationCorresponds to variant rs5961dbSNPEnsembl.1
Natural variantiVAR_06542847E → G in FA10D; St. Louis II; strongly reduced activity; not activated by factor VIIa and tissue factor. 1 PublicationCorresponds to variant rs121964943dbSNPEnsembl.1
Natural variantiVAR_06542951G → V in FA10D. 1 PublicationCorresponds to variant rs751782758dbSNPEnsembl.1
Natural variantiVAR_06543054E → G in FA10D; Ketchikan. 1 PublicationCorresponds to variant rs121964944dbSNPEnsembl.1
Natural variantiVAR_06543154E → K in FA10D; Vorarlberg; converts prothrombin at a normal rate but shows decreased affinity for calcium. 2 PublicationsCorresponds to variant rs121964939dbSNPEnsembl.1
Natural variantiVAR_06543272E → Q in FA10D; Tokyo. 1 PublicationCorresponds to variant rs121964945dbSNPEnsembl.1
Natural variantiVAR_06543391E → K in FA10D; Riyadh. 1 Publication1
Natural variantiVAR_065434142E → K in FA10D; uncertain pathological significance; detected in patients carrying K-54 or P-374; slightly reduced activity. 3 PublicationsCorresponds to variant rs61753266dbSNPEnsembl.1
Natural variantiVAR_065435149C → Y in FA10D. 1 Publication1
Natural variantiVAR_065436151C → Y in FA10D. 1 Publication1
Natural variantiVAR_020176152A → T.1 PublicationCorresponds to variant rs3211772dbSNPEnsembl.1
Natural variantiVAR_075212176 – 186Missing in FA10D; unknown pathological significance. 1 PublicationAdd BLAST11
Natural variantiVAR_020177192G → R.1 PublicationCorresponds to variant rs3211783dbSNPEnsembl.1
Natural variantiVAR_075213262G → D in FA10D; unknown pathological significance. 1 Publication1
Natural variantiVAR_065437289G → R in FA10D; may affect splicing. 1 PublicationCorresponds to variant rs121964946dbSNPEnsembl.1
Natural variantiVAR_065438304E → K in FA10D. 1 PublicationCorresponds to variant rs747292771dbSNPEnsembl.1
Natural variantiVAR_065439322D → N in FA10D; Stockton; 50% decrease in specific activity. 2 PublicationsCorresponds to variant rs121964942dbSNPEnsembl.1
Natural variantiVAR_065440327R → W in FA10D. 1 PublicationCorresponds to variant rs770119164dbSNPEnsembl.1
Natural variantiVAR_065441338V → M in FA10D. 1 PublicationCorresponds to variant rs121964947dbSNPEnsembl.1
Natural variantiVAR_065442350E → K in FA10D. 1 PublicationCorresponds to variant rs372309538dbSNPEnsembl.1
Natural variantiVAR_065443358T → M in FA10D; Roma. 2 PublicationsCorresponds to variant rs768222784dbSNPEnsembl.1
Natural variantiVAR_065444363G → S in FA10D. 1 Publication1
Natural variantiVAR_065445366R → C in FA10D; San Antonio. 1 PublicationCorresponds to variant rs104894392dbSNPEnsembl.1
Natural variantiVAR_065446374S → P in FA10D; Marseille; decreased cleavage by factor IXa; normal catalytic efficiency for prothrombin. 3 PublicationsCorresponds to variant rs121964941dbSNPEnsembl.1
Natural variantiVAR_072751382V → A in FA10D; partial loss of activity. 2 Publications1
Natural variantiVAR_065447383P → S in FA10D; Friuli. 1 PublicationCorresponds to variant rs121964940dbSNPEnsembl.1
Natural variantiVAR_065448390C → F in FA10D; Padua 4. 1 PublicationCorresponds to variant rs199778916dbSNPEnsembl.1
Natural variantiVAR_065449404C → R in FA10D. 1 Publication1
Natural variantiVAR_065450406G → S in FA10D; almost complete loss of activity. 2 PublicationsCorresponds to variant rs376163818dbSNPEnsembl.1
Natural variantiVAR_065451420G → R in FA10D; Padua 3. 1 PublicationCorresponds to variant rs750759634dbSNPEnsembl.1
Natural variantiVAR_072752421G → D in FA10D; significant loss of activity. 2 PublicationsCorresponds to variant rs758726161dbSNPEnsembl.1
Natural variantiVAR_065452448K → N in FA10D; San Giovanni Rotondo. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K03194 mRNA. Translation: AAA52490.1.
M57285 mRNA. Translation: AAA52421.1.
AF503510 Genomic DNA. Translation: AAM19347.1.
BC046125 mRNA. Translation: AAH46125.1.
N00045
, L00390, L00391, L00392, L00393, L00394, L00395, L00396 Genomic DNA. Translation: AAA52764.1.
M22613 mRNA. Translation: AAA51984.1.
K01886 mRNA. Translation: AAA52486.1.
M33297 Genomic DNA. Translation: AAA52636.1.
CCDSiCCDS9530.1.
PIRiA24478. EXHU.
RefSeqiNP_000495.1. NM_000504.3.
NP_001299603.1. NM_001312674.1.
NP_001299604.1. NM_001312675.1.
UniGeneiHs.361463.

Genome annotation databases

EnsembliENST00000375559; ENSP00000364709; ENSG00000126218.
GeneIDi2159.
KEGGihsa:2159.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Factor X entry

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K03194 mRNA. Translation: AAA52490.1.
M57285 mRNA. Translation: AAA52421.1.
AF503510 Genomic DNA. Translation: AAM19347.1.
BC046125 mRNA. Translation: AAH46125.1.
N00045
, L00390, L00391, L00392, L00393, L00394, L00395, L00396 Genomic DNA. Translation: AAA52764.1.
M22613 mRNA. Translation: AAA51984.1.
K01886 mRNA. Translation: AAA52486.1.
M33297 Genomic DNA. Translation: AAA52636.1.
CCDSiCCDS9530.1.
PIRiA24478. EXHU.
RefSeqiNP_000495.1. NM_000504.3.
NP_001299603.1. NM_001312674.1.
NP_001299604.1. NM_001312675.1.
UniGeneiHs.361463.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4Y6DX-ray1.55A235-488[»]
B46-179[»]
4Y71X-ray1.80A235-488[»]
B46-179[»]
4Y76X-ray2.00A235-488[»]
B46-179[»]
4Y79X-ray2.10A235-488[»]
B46-179[»]
4Y7AX-ray1.99A235-488[»]
B46-179[»]
4Y7BX-ray1.79A235-488[»]
B46-179[»]
4ZH8X-ray1.80A235-488[»]
B46-179[»]
4ZHAX-ray1.86A235-488[»]
B46-179[»]
5K0HX-ray2.20A235-468[»]
B128-178[»]
ProteinModelPortaliP00742.
SMRiP00742.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108457. 8 interactors.
DIPiDIP-29896N.
IntActiP00742. 9 interactors.
MINTiMINT-276128.
STRINGi9606.ENSP00000364709.

Chemistry databases

BindingDBiP00742.
ChEMBLiCHEMBL244.
DrugBankiDB00025. Antihemophilic Factor (Recombinant).
DB06605. Apixaban.
DB00100. Coagulation Factor IX.
DB00036. Coagulation factor VIIa.
DB09075. Edoxaban.
DB01225. Enoxaparin.
DB00569. Fondaparinux sodium.
DB01109. Heparin.
DB00170. Menadione.
DB06228. Rivaroxaban.
GuidetoPHARMACOLOGYi2359.

Protein family/group databases

MEROPSiS01.216.

PTM databases

iPTMnetiP00742.
PhosphoSitePlusiP00742.
UniCarbKBiP00742.

Polymorphism and mutation databases

BioMutaiF10.
DMDMi119761.

Proteomic databases

EPDiP00742.
PaxDbiP00742.
PeptideAtlasiP00742.
PRIDEiP00742.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000375559; ENSP00000364709; ENSG00000126218.
GeneIDi2159.
KEGGihsa:2159.

Organism-specific databases

CTDi2159.
DisGeNETi2159.
GeneCardsiF10.
HGNCiHGNC:3528. F10.
MalaCardsiF10.
MIMi227600. phenotype.
613872. gene.
neXtProtiNX_P00742.
OpenTargetsiENSG00000126218.
Orphaneti328. Congenital factor X deficiency.
PharmGKBiPA27940.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IGPV. Eukaryota.
COG5640. LUCA.
GeneTreeiENSGT00760000118890.
HOGENOMiHOG000251821.
HOVERGENiHBG013304.
InParanoidiP00742.
KOiK01314.
OMAiEMAHEVE.
OrthoDBiEOG091G0AH5.
PhylomeDBiP00742.
TreeFamiTF327329.

Enzyme and pathway databases

BioCyciMetaCyc:HS05000-MONOMER.
ZFISH:HS05000-MONOMER.
BRENDAi3.4.21.6. 2681.
ReactomeiR-HSA-140834. Extrinsic Pathway of Fibrin Clot Formation.
R-HSA-140837. Intrinsic Pathway of Fibrin Clot Formation.
R-HSA-140875. Common Pathway of Fibrin Clot Formation.
R-HSA-159740. Gamma-carboxylation of protein precursors.
R-HSA-159763. Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
R-HSA-159782. Removal of aminoterminal propeptides from gamma-carboxylated proteins.
SABIO-RKP00742.
SIGNORiP00742.

Miscellaneous databases

ChiTaRSiF10. human.
EvolutionaryTraceiP00742.
GeneWikiiFactor_X.
GenomeRNAii2159.
PMAP-CutDBP00742.
PROiP00742.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000126218.
CleanExiHS_F10.
ExpressionAtlasiP00742. baseline and differential.
GenevisibleiP00742. HS.

Family and domain databases

CDDicd00190. Tryp_SPc. 1 hit.
Gene3Di4.10.740.10. 1 hit.
InterProiIPR017857. Coagulation_fac_subgr_Gla_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR000294. GLA_domain.
IPR012224. Pept_S1A_FX.
IPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[Graphical view]
PfamiPF00008. EGF. 1 hit.
PF00594. Gla. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFiPIRSF001143. Factor_X. 1 hit.
PRINTSiPR00722. CHYMOTRYPSIN.
PR00001. GLABLOOD.
SMARTiSM00181. EGF. 2 hits.
SM00179. EGF_CA. 1 hit.
SM00069. GLA. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 2 hits.
SSF57630. SSF57630. 1 hit.
PROSITEiPS00010. ASX_HYDROXYL. 1 hit.
PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 2 hits.
PS50026. EGF_3. 1 hit.
PS01187. EGF_CA. 1 hit.
PS00011. GLA_1. 1 hit.
PS50998. GLA_2. 1 hit.
PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFA10_HUMAN
AccessioniPrimary (citable) accession number: P00742
Secondary accession number(s): Q14340
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 1, 1989
Last modified: November 30, 2016
This is version 230 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

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

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.