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Protein

Coagulation factor X

Gene

F10

Organism
Bos taurus (Bovine)
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.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei275Charge relay system1 Publication1
Active sitei321Charge relay system1 Publication1
Active sitei418Charge relay system1 Publication1

GO - Molecular functioni

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

ReactomeiR-BTA-140834. Extrinsic Pathway of Fibrin Clot Formation.
R-BTA-140837. Intrinsic Pathway of Fibrin Clot Formation.
R-BTA-140875. Common Pathway of Fibrin Clot Formation.
R-BTA-159740. Gamma-carboxylation of protein precursors.
R-BTA-159763. Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
R-BTA-159782. Removal of aminoterminal propeptides from gamma-carboxylated proteins.
SABIO-RKP00743.

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
Cleaved into the following 3 chains:
Gene namesi
Name:F10
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 12

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3656.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 23Sequence analysisAdd BLAST23
PropeptideiPRO_000002777924 – 401 PublicationAdd BLAST17
ChainiPRO_000002778041 – 492Coagulation factor XAdd BLAST452
ChainiPRO_000002778141 – 180Factor X light chainAdd BLAST140
ChainiPRO_0000027782183 – 492Factor X heavy chainAdd BLAST310
PropeptideiPRO_0000027783183 – 233Activation peptideAdd BLAST51
ChainiPRO_0000027784234 – 492Activated factor Xa heavy chainAdd BLAST259
PropeptideiPRO_0000027785476 – 492May be removed but is not necessary for activationAdd BLAST17

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 residuei754-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei794-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Disulfide bondi90 ↔ 1011 Publication
Disulfide bondi95 ↔ 1101 Publication
Modified residuei103(3R)-3-hydroxyaspartate1 Publication1
Disulfide bondi112 ↔ 1211 Publication
Disulfide bondi129 ↔ 140By similarity
Disulfide bondi136 ↔ 149By similarity
Disulfide bondi151 ↔ 164By similarity
Disulfide bondi172 ↔ 341Interchain (between light and heavy chains)PROSITE-ProRule annotation1 Publication
Modified residuei200Sulfotyrosine1 Publication1
Glycosylationi208O-linked (GalNAc...)1 Publication1
GlycosylationiCAR_000011218N-linked (GlcNAc...)1 Publication1
Disulfide bondi240 ↔ 2451 Publication
Disulfide bondi260 ↔ 2761 Publication
Disulfide bondi389 ↔ 4031 Publication
Disulfide bondi414 ↔ 4421 Publication
Glycosylationi485O-linked (GalNAc...)1 Publication1

Post-translational modificationi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei233 – 234Cleavage; by coagulation factor IXa and coagulation factor VIIa2

Keywords - PTMi

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

Proteomic databases

PaxDbiP00743.
PRIDEiP00743.

PTM databases

UniCarbKBiP00743.

Miscellaneous databases

PMAP-CutDBP00743.

Expressioni

Gene expression databases

BgeeiENSBTAG00000016385.

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 (By similarity).By similarity

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000021789.

Chemistry databases

BindingDBiP00743.

Structurei

Secondary structure

1492
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi46 – 48Combined sources3
Helixi53 – 57Combined sources5
Beta strandi58 – 61Combined sources4
Helixi64 – 71Combined sources8
Helixi74 – 82Combined sources9
Turni86 – 90Combined sources5
Beta strandi100 – 102Combined sources3
Beta strandi105 – 107Combined sources3
Beta strandi109 – 111Combined sources3
Beta strandi116 – 118Combined sources3
Beta strandi121 – 123Combined sources3
Turni131 – 134Combined sources4
Beta strandi135 – 138Combined sources4
Beta strandi155 – 157Combined sources3
Beta strandi164 – 166Combined sources3
Beta strandi168 – 170Combined sources3
Beta strandi235 – 237Combined sources3
Turni242 – 244Combined sources3
Beta strandi248 – 252Combined sources5
Beta strandi254 – 256Combined sources3
Beta strandi258 – 264Combined sources7
Beta strandi266 – 272Combined sources7
Beta strandi304 – 309Combined sources6
Turni315 – 317Combined sources3
Beta strandi323 – 329Combined sources7
Helixi345 – 350Combined sources6
Turni351 – 354Combined sources4
Beta strandi355 – 363Combined sources9
Beta strandi365 – 367Combined sources3
Beta strandi370 – 372Combined sources3
Beta strandi377 – 383Combined sources7
Helixi386 – 392Combined sources7
Beta strandi401 – 407Combined sources7
Beta strandi421 – 426Combined sources6
Beta strandi429 – 443Combined sources15
Beta strandi447 – 454Combined sources8
Helixi455 – 457Combined sources3
Helixi458 – 464Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1APONMR-A85-126[»]
1CCFNMR-A85-126[»]
1IODX-ray2.30G41-84[»]
1KIGX-ray3.00H234-474[»]
L129-179[»]
1WHENMR-A41-126[»]
1WHFNMR-A41-126[»]
ProteinModelPortaliP00743.
SMRiP00743.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00743.

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
Domaini234 – 466Peptidase S1PROSITE-ProRule annotationAdd BLAST233

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.
InParanoidiP00743.
KOiK01314.
OMAiEMAHEVE.
OrthoDBiEOG091G0AH5.
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. 1 hit.
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.

P00743-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGLLHLVLL STALGGLLRP AGSVFLPRDQ AHRVLQRARR ANSFLEEVKQ
60 70 80 90 100
GNLERECLEE ACSLEEAREV FEDAEQTDEF WSKYKDGDQC EGHPCLNQGH
110 120 130 140 150
CKDGIGDYTC TCAEGFEGKN CEFSTREICS LDNGGCDQFC REERSEVRCS
160 170 180 190 200
CAHGYVLGDD SKSCVSTERF PCGKFTQGRS RRWAIHTSED ALDASELEHY
210 220 230 240 250
DPADLSPTES SLDLLGLNRT EPSAGEDGSQ VVRIVGGRDC AEGECPWQAL
260 270 280 290 300
LVNEENEGFC GGTILNEFYV LTAAHCLHQA KRFTVRVGDR NTEQEEGNEM
310 320 330 340 350
AHEVEMTVKH SRFVKETYDF DIAVLRLKTP IRFRRNVAPA CLPEKDWAEA
360 370 380 390 400
TLMTQKTGIV SGFGRTHEKG RLSSTLKMLE VPYVDRSTCK LSSSFTITPN
410 420 430 440 450
MFCAGYDTQP EDACQGDSGG PHVTRFKDTY FVTGIVSWGE GCARKGKFGV
460 470 480 490
YTKVSNFLKW IDKIMKARAG AAGSRGHSEA PATWTVPPPL PL
Length:492
Mass (Da):54,510
Last modified:August 13, 1987 - v1
Checksum:iD5BD911FB72F1D30
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti103D → N AA sequence (PubMed:6766735).Curated1
Sequence conflicti293Missing AA sequence (PubMed:1059093).Curated1
Sequence conflicti296 – 298EGN → GDE AA sequence (PubMed:1059093).Curated3
Sequence conflicti335Missing AA sequence (PubMed:1059093).Curated1
Sequence conflicti349 – 350EA → AE AA sequence (PubMed:1059093).Curated2
Sequence conflicti355Missing AA sequence (PubMed:1059093).Curated1
Sequence conflicti442 – 445CARK → GKFG AA sequence (PubMed:1059093).Curated4

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00673 mRNA. Translation: CAA25286.1.
PIRiA22867. EXBO.
RefSeqiNP_001073682.1. NM_001080213.1.
UniGeneiBt.13151.

Genome annotation databases

EnsembliENSBTAT00000021789; ENSBTAP00000021789; ENSBTAG00000016385.
GeneIDi280787.
KEGGibta:280787.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00673 mRNA. Translation: CAA25286.1.
PIRiA22867. EXBO.
RefSeqiNP_001073682.1. NM_001080213.1.
UniGeneiBt.13151.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1APONMR-A85-126[»]
1CCFNMR-A85-126[»]
1IODX-ray2.30G41-84[»]
1KIGX-ray3.00H234-474[»]
L129-179[»]
1WHENMR-A41-126[»]
1WHFNMR-A41-126[»]
ProteinModelPortaliP00743.
SMRiP00743.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000021789.

Chemistry databases

BindingDBiP00743.
ChEMBLiCHEMBL3656.

Protein family/group databases

MEROPSiS01.216.

PTM databases

UniCarbKBiP00743.

Proteomic databases

PaxDbiP00743.
PRIDEiP00743.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000021789; ENSBTAP00000021789; ENSBTAG00000016385.
GeneIDi280787.
KEGGibta:280787.

Organism-specific databases

CTDi2159.

Phylogenomic databases

eggNOGiENOG410IGPV. Eukaryota.
COG5640. LUCA.
GeneTreeiENSGT00760000118890.
HOGENOMiHOG000251821.
HOVERGENiHBG013304.
InParanoidiP00743.
KOiK01314.
OMAiEMAHEVE.
OrthoDBiEOG091G0AH5.
TreeFamiTF327329.

Enzyme and pathway databases

ReactomeiR-BTA-140834. Extrinsic Pathway of Fibrin Clot Formation.
R-BTA-140837. Intrinsic Pathway of Fibrin Clot Formation.
R-BTA-140875. Common Pathway of Fibrin Clot Formation.
R-BTA-159740. Gamma-carboxylation of protein precursors.
R-BTA-159763. Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
R-BTA-159782. Removal of aminoterminal propeptides from gamma-carboxylated proteins.
SABIO-RKP00743.

Miscellaneous databases

EvolutionaryTraceiP00743.
PMAP-CutDBP00743.
PROiP00743.

Gene expression databases

BgeeiENSBTAG00000016385.

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. 1 hit.
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_BOVIN
AccessioniPrimary (citable) accession number: P00743
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: August 13, 1987
Last modified: November 2, 2016
This is version 196 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Calcium also binds, with stronger affinity to another site, beyond the GLA domain.

Keywords - Technical termi

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

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. 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.