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Protein

Coagulation factor X

Gene

F10

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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 sitei274Charge relay system1
Active sitei320Charge relay system1
Active sitei417Charge relay system1

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

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
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
Proteomesi
  • UP000001811 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL5062.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Sequence analysisAdd BLAST20
PropeptideiPRO_000002779821 – 40By similarityAdd BLAST20
ChainiPRO_000002779941 – 490Coagulation factor XAdd BLAST450
ChainiPRO_000002780041 – 180Factor X light chainAdd BLAST140
ChainiPRO_0000027801184 – 490Factor X heavy chainAdd BLAST307
PropeptideiPRO_0000027802184 – 232Activation peptideAdd BLAST49
ChainiPRO_0000027803233 – 490Activated factor Xa heavy chainAdd BLAST258

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei464-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei474-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei544-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei564-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Disulfide bondi57 ↔ 62By similarity
Modified residuei594-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei604-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Glycosylationi61N-linked (GlcNAc...)Sequence analysis1
Modified residuei654-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei664-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei694-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei724-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei754-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei794-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Disulfide bondi90 ↔ 101By similarity
Disulfide bondi95 ↔ 110By similarity
Modified residuei103(3R)-3-hydroxyaspartateBy similarity1
Disulfide bondi112 ↔ 121By similarity
Disulfide bondi129 ↔ 140By similarity
Disulfide bondi136 ↔ 149By similarity
Disulfide bondi151 ↔ 164By similarity
Disulfide bondi172 ↔ 340Interchain (between light and heavy chains)PROSITE-ProRule annotation
Glycosylationi187N-linked (GlcNAc...)Sequence analysis1
Glycosylationi205N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi239 ↔ 244By similarity
Disulfide bondi259 ↔ 275By similarity
Disulfide bondi388 ↔ 402By similarity
Disulfide bondi413 ↔ 441By similarity

Post-translational modificationi

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

Keywords - PTMi

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

Proteomic databases

PRIDEiO19045.

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

STRINGi9986.ENSOCUP00000025032.

Chemistry databases

BindingDBiO19045.

Structurei

3D structure databases

ProteinModelPortaliO19045.
ModBaseiSearch...
MobiDBiSearch...

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
Domaini233 – 465Peptidase 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.
HOGENOMiHOG000251821.
HOVERGENiHBG013304.
InParanoidiO19045.
KOiK01314.

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.

O19045-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MANPLHLVLL GAALAGLLLS GSSVFISRRA ANDVLARTRR ANSFLEELKK
60 70 80 90 100
GNLERECMEE NCSYEEALEV FEDREKTNEF WNKYVDGDQC ESNPCQNQGT
110 120 130 140 150
CKDGLGMYTC SCVEGYEGQD CEPVTRKLCS LDNGGCDQFC KEEENSVLCS
160 170 180 190 200
CASGYTLGDN GKSCISTELF PCGKVTLGRW RRSPATNSSE GPPEAPGPEQ
210 220 230 240 250
QDDGNLTATE NPFNLLDSPE PPPEDDSSSL VRIVGGQDCR DGECPWQALL
260 270 280 290 300
VNEENEGFCG GTILSEYHVL TAAHCLHQAK RFKVRVGDRD TEHEEGNEET
310 320 330 340 350
HEVEVVVKHN RFVKETYDFD IAVLRLKTPI TFRRNVAPAC LPQKDWAEST
360 370 380 390 400
LMAQKTGIVS GFGRTHEMGR LSTTLKMLEV PYVDRNSCKR SSSFTITQNM
410 420 430 440 450
FCAGYDARPE DACQGDSGGP HVTRFRDTYF VTGIVSWGEG CARKGKFGVY
460 470 480 490
TKVSNFLKWI EKSMRARAVP VAEAAGTPGP TQPTIKGSPS
Length:490
Mass (Da):53,965
Last modified:January 1, 1998 - v1
Checksum:i3A39FA85AF2A6D11
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF003200 mRNA. Translation: AAB62542.1.
RefSeqiNP_001075485.1. NM_001082016.1.
UniGeneiOcu.2157.

Genome annotation databases

GeneIDi100008647.
KEGGiocu:100008647.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF003200 mRNA. Translation: AAB62542.1.
RefSeqiNP_001075485.1. NM_001082016.1.
UniGeneiOcu.2157.

3D structure databases

ProteinModelPortaliO19045.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000025032.

Chemistry databases

BindingDBiO19045.
ChEMBLiCHEMBL5062.

Protein family/group databases

MEROPSiS01.216.

Proteomic databases

PRIDEiO19045.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100008647.
KEGGiocu:100008647.

Organism-specific databases

CTDi2159.

Phylogenomic databases

eggNOGiENOG410IGPV. Eukaryota.
COG5640. LUCA.
HOGENOMiHOG000251821.
HOVERGENiHBG013304.
InParanoidiO19045.
KOiK01314.

Miscellaneous databases

PROiO19045.

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_RABIT
AccessioniPrimary (citable) accession number: O19045
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 1, 1998
Last modified: October 5, 2016
This is version 131 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

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. 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.