SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

O19045

- FA10_RABIT

UniProt

O19045 - FA10_RABIT

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020 Reviewed predictionAdd
BLAST
Propeptidei21 – 4020 By 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-carboxyglutamate By similarity
Modified residuei47 – 4714-carboxyglutamate By similarity
Modified residuei54 – 5414-carboxyglutamate By similarity
Modified residuei56 – 5614-carboxyglutamate By similarity
Disulfide bondi57 ↔ 62 By similarity
Modified residuei59 – 5914-carboxyglutamate By similarity
Modified residuei60 – 6014-carboxyglutamate By similarity
Glycosylationi61 – 611N-linked (GlcNAc...) Reviewed prediction
Modified residuei65 – 6514-carboxyglutamate By similarity
Modified residuei66 – 6614-carboxyglutamate By similarity
Modified residuei69 – 6914-carboxyglutamate By similarity
Modified residuei72 – 7214-carboxyglutamate By similarity
Modified residuei75 – 7514-carboxyglutamate By similarity
Modified residuei79 – 7914-carboxyglutamate By similarity
Disulfide bondi90 ↔ 101 By similarity
Disulfide bondi95 ↔ 110 By similarity
Modified residuei103 – 1031(3R)-3-hydroxyaspartate By similarity
Disulfide bondi112 ↔ 121 By similarity
Disulfide bondi129 ↔ 140 By similarity
Disulfide bondi136 ↔ 149 By similarity
Disulfide bondi151 ↔ 164 By similarity
Disulfide bondi172 ↔ 340Interchain (between light and heavy chains) By similarity
Glycosylationi187 – 1871N-linked (GlcNAc...) Reviewed prediction
Glycosylationi205 – 2051N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi239 ↔ 244 By similarity
Disulfide bondi259 ↔ 275 By similarity
Disulfide bondi388 ↔ 402 By similarity
Disulfide bondi413 ↔ 441 By 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.

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000025032.

Structurei

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini41 – 8545GlaAdd
BLAST
Domaini86 – 12237EGF-like 1; calcium-binding Reviewed predictionAdd
BLAST
Domaini125 – 16541EGF-like 2Add
BLAST
Domaini233 – 465233Peptidase S1Add
BLAST

Sequence similaritiesi

Belongs to the peptidase S1 family.
Contains 2 EGF-like domains.

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiCOG5640.
HOGENOMiHOG000251821.
HOVERGENiHBG013304.

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

MANPLHLVLL GAALAGLLLS GSSVFISRRA ANDVLARTRR ANSFLEELKK    50
GNLERECMEE NCSYEEALEV FEDREKTNEF WNKYVDGDQC ESNPCQNQGT 100
CKDGLGMYTC SCVEGYEGQD CEPVTRKLCS LDNGGCDQFC KEEENSVLCS 150
CASGYTLGDN GKSCISTELF PCGKVTLGRW RRSPATNSSE GPPEAPGPEQ 200
QDDGNLTATE NPFNLLDSPE PPPEDDSSSL VRIVGGQDCR DGECPWQALL 250
VNEENEGFCG GTILSEYHVL TAAHCLHQAK RFKVRVGDRD TEHEEGNEET 300
HEVEVVVKHN RFVKETYDFD IAVLRLKTPI TFRRNVAPAC LPQKDWAEST 350
LMAQKTGIVS GFGRTHEMGR LSTTLKMLEV PYVDRNSCKR SSSFTITQNM 400
FCAGYDARPE DACQGDSGGP HVTRFRDTYF VTGIVSWGEG CARKGKFGVY 450
TKVSNFLKWI EKSMRARAVP VAEAAGTPGP TQPTIKGSPS 490
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.

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: May 14, 2014
This is version 117 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

Similar proteinsi