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O19045

- FA10_RABIT

UniProt

O19045 - FA10_RABIT

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Protein

Coagulation factor X

Gene

F10

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei274 – 2741Charge relay system
Active sitei320 – 3201Charge relay system
Active sitei417 – 4171Charge relay system

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. serine-type endopeptidase activity Source: InterPro

GO - Biological processi

  1. blood coagulation Source: UniProtKB-KW
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
ProteomesiUP000001811: Unplaced

Subcellular locationi

Secreted By similarity

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence AnalysisAdd
BLAST
Propeptidei21 – 4020By similarityPRO_0000027798Add
BLAST
Chaini41 – 490450Coagulation factor XPRO_0000027799Add
BLAST
Chaini41 – 180140Factor X light chainPRO_0000027800Add
BLAST
Chaini184 – 490307Factor X heavy chainPRO_0000027801Add
BLAST
Propeptidei184 – 23249Activation peptidePRO_0000027802Add
BLAST
Chaini233 – 490258Activated factor Xa heavy chainPRO_0000027803Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei46 – 4614-carboxyglutamatePROSITE-ProRule annotation
Modified residuei47 – 4714-carboxyglutamatePROSITE-ProRule annotation
Modified residuei54 – 5414-carboxyglutamatePROSITE-ProRule annotation
Modified residuei56 – 5614-carboxyglutamatePROSITE-ProRule annotation
Disulfide bondi57 ↔ 62By similarity
Modified residuei59 – 5914-carboxyglutamatePROSITE-ProRule annotation
Modified residuei60 – 6014-carboxyglutamatePROSITE-ProRule annotation
Glycosylationi61 – 611N-linked (GlcNAc...)Sequence Analysis
Modified residuei65 – 6514-carboxyglutamatePROSITE-ProRule annotation
Modified residuei66 – 6614-carboxyglutamatePROSITE-ProRule annotation
Modified residuei69 – 6914-carboxyglutamatePROSITE-ProRule annotation
Modified residuei72 – 7214-carboxyglutamatePROSITE-ProRule annotation
Modified residuei75 – 7514-carboxyglutamatePROSITE-ProRule annotation
Modified residuei79 – 7914-carboxyglutamatePROSITE-ProRule annotation
Disulfide bondi90 ↔ 101By similarity
Disulfide bondi95 ↔ 110By similarity
Modified residuei103 – 1031(3R)-3-hydroxyaspartateBy similarity
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
Glycosylationi187 – 1871N-linked (GlcNAc...)Sequence Analysis
Glycosylationi205 – 2051N-linked (GlcNAc...)Sequence Analysis
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

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.

Structurei

3D structure databases

ProteinModelPortaliO19045.
SMRiO19045. Positions 42-86, 233-473.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini41 – 8545GlaPROSITE-ProRule annotationAdd
BLAST
Domaini86 – 12237EGF-like 1; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini125 – 16541EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini233 – 465233Peptidase S1PROSITE-ProRule annotationAdd
BLAST

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

eggNOGiCOG5640.
HOGENOMiHOG000251821.
HOVERGENiHBG013304.
InParanoidiO19045.

Family and domain databases

Gene3Di4.10.740.10. 1 hit.
InterProiIPR017857. Coagulation_fac_subgr_Gla_dom.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR000294. GLA_domain.
IPR012224. Pept_S1A_FX.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[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. 1 hit.
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:
EMBL
GenBank
DDBJ
Links Updated
AF003200 mRNA. Translation: AAB62542.1.
RefSeqiNP_001075485.1. NM_001082016.1.
UniGeneiOcu.2157.

Genome annotation databases

GeneIDi100008647.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF003200 mRNA. Translation: AAB62542.1 .
RefSeqi NP_001075485.1. NM_001082016.1.
UniGenei Ocu.2157.

3D structure databases

ProteinModelPortali O19045.
SMRi O19045. Positions 42-86, 233-473.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9986.ENSOCUP00000025032.

Chemistry

BindingDBi O19045.
ChEMBLi CHEMBL5062.

Protein family/group databases

MEROPSi S01.216.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100008647.

Organism-specific databases

CTDi 2159.

Phylogenomic databases

eggNOGi COG5640.
HOGENOMi HOG000251821.
HOVERGENi HBG013304.
InParanoidi O19045.

Family and domain databases

Gene3Di 4.10.740.10. 1 hit.
InterProi IPR017857. Coagulation_fac_subgr_Gla_dom.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR000294. GLA_domain.
IPR012224. Pept_S1A_FX.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view ]
Pfami PF00008. EGF. 1 hit.
PF00594. Gla. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view ]
PIRSFi PIRSF001143. Factor_X. 1 hit.
PRINTSi PR00722. CHYMOTRYPSIN.
PR00001. GLABLOOD.
SMARTi SM00181. EGF. 1 hit.
SM00179. EGF_CA. 1 hit.
SM00069. GLA. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view ]
SUPFAMi SSF50494. SSF50494. 2 hits.
SSF57630. SSF57630. 1 hit.
PROSITEi PS00010. 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 ]
ProtoNeti Search...

Publicationsi

  1. "Characterization of a full-length cDNA for rabbit factor X."
    Pendurthi U.R., Anderson K.D., James H.L.
    Thromb. Res. 85:503-514(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

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 29, 2014
This is version 119 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

External Data

Dasty 3