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O19045 (FA10_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Coagulation factor X
EC=3.4.21.6
Alternative name(s):
Stuart factor

Cleaved into the following 3 chains:

  1. Factor X light chain
  2. Factor X heavy chain
  3. Activated factor Xa heavy chain
Gene names
Name:F10
OrganismOryctolagus cuniculus (Rabbit) [Reference proteome]
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

Protein attributes

Sequence length490 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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 activity

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

Enzyme regulation

Inhibited by SERPINA5 By similarity.

Subunit structure

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.

Subcellular location

Secreted By similarity.

Post-translational modification

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.

Miscellaneous

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

Sequence similarities

Belongs to the peptidase S1 family.

Contains 2 EGF-like domains.

Contains 1 Gla (gamma-carboxy-glutamate) domain.

Contains 1 peptidase S1 domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Propeptide21 – 4020 By similarity
PRO_0000027798
Chain41 – 490450Coagulation factor X
PRO_0000027799
Chain41 – 180140Factor X light chain
PRO_0000027800
Chain184 – 490307Factor X heavy chain
PRO_0000027801
Propeptide184 – 23249Activation peptide
PRO_0000027802
Chain233 – 490258Activated factor Xa heavy chain
PRO_0000027803

Regions

Domain41 – 8545Gla
Domain86 – 12237EGF-like 1; calcium-binding Potential
Domain125 – 16541EGF-like 2
Domain233 – 465233Peptidase S1

Sites

Active site2741Charge relay system
Active site3201Charge relay system
Active site4171Charge relay system

Amino acid modifications

Modified residue4614-carboxyglutamate By similarity
Modified residue4714-carboxyglutamate By similarity
Modified residue5414-carboxyglutamate By similarity
Modified residue5614-carboxyglutamate By similarity
Modified residue5914-carboxyglutamate By similarity
Modified residue6014-carboxyglutamate By similarity
Modified residue6514-carboxyglutamate By similarity
Modified residue6614-carboxyglutamate By similarity
Modified residue6914-carboxyglutamate By similarity
Modified residue7214-carboxyglutamate By similarity
Modified residue7514-carboxyglutamate By similarity
Modified residue7914-carboxyglutamate By similarity
Modified residue1031(3R)-3-hydroxyaspartate By similarity
Glycosylation611N-linked (GlcNAc...) Potential
Glycosylation1871N-linked (GlcNAc...) Potential
Glycosylation2051N-linked (GlcNAc...) Potential
Disulfide bond57 ↔ 62 By similarity
Disulfide bond90 ↔ 101 By similarity
Disulfide bond95 ↔ 110 By similarity
Disulfide bond112 ↔ 121 By similarity
Disulfide bond129 ↔ 140 By similarity
Disulfide bond136 ↔ 149 By similarity
Disulfide bond151 ↔ 164 By similarity
Disulfide bond172 ↔ 340Interchain (between light and heavy chains) By similarity
Disulfide bond239 ↔ 244 By similarity
Disulfide bond259 ↔ 275 By similarity
Disulfide bond388 ↔ 402 By similarity
Disulfide bond413 ↔ 441 By similarity

Sequences

Sequence LengthMass (Da)Tools
O19045 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 3A39FA85AF2A6D11

FASTA49053,965
        10         20         30         40         50         60 
MANPLHLVLL GAALAGLLLS GSSVFISRRA ANDVLARTRR ANSFLEELKK GNLERECMEE 

        70         80         90        100        110        120 
NCSYEEALEV FEDREKTNEF WNKYVDGDQC ESNPCQNQGT CKDGLGMYTC SCVEGYEGQD 

       130        140        150        160        170        180 
CEPVTRKLCS LDNGGCDQFC KEEENSVLCS CASGYTLGDN GKSCISTELF PCGKVTLGRW 

       190        200        210        220        230        240 
RRSPATNSSE GPPEAPGPEQ QDDGNLTATE NPFNLLDSPE PPPEDDSSSL VRIVGGQDCR 

       250        260        270        280        290        300 
DGECPWQALL VNEENEGFCG GTILSEYHVL TAAHCLHQAK RFKVRVGDRD TEHEEGNEET 

       310        320        330        340        350        360 
HEVEVVVKHN RFVKETYDFD IAVLRLKTPI TFRRNVAPAC LPQKDWAEST LMAQKTGIVS 

       370        380        390        400        410        420 
GFGRTHEMGR LSTTLKMLEV PYVDRNSCKR SSSFTITQNM FCAGYDARPE DACQGDSGGP 

       430        440        450        460        470        480 
HVTRFRDTYF VTGIVSWGEG CARKGKFGVY TKVSNFLKWI EKSMRARAVP VAEAAGTPGP 

       490 
TQPTIKGSPS

« Hide

References

[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].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF003200 mRNA. Translation: AAB62542.1.
RefSeqNP_001075485.1. NM_001082016.1.
UniGeneOcu.2157.

3D structure databases

ProteinModelPortalO19045.
SMRO19045. Positions 42-86, 233-473.
ModBaseSearch...

Protein-protein interaction databases

STRING9986.ENSOCUP00000025032.

Protein family/group databases

MEROPSS01.216.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100008647.

Organism-specific databases

CTD2159.

Phylogenomic databases

eggNOGCOG5640.
HOGENOMHOG000251821.
HOVERGENHBG013304.
OrthoDBEOG447FTB.

Family and domain databases

Gene3D4.10.740.10. 1 hit.
InterProIPR017857. Coagulation_fac_subgr_Gla_dom.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd.
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]
PfamPF00008. EGF. 1 hit.
PF00594. Gla. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFPIRSF001143. Factor_X. 1 hit.
PRINTSPR00722. CHYMOTRYPSIN.
PR00001. GLABLOOD.
SMARTSM00181. EGF. 1 hit.
SM00179. EGF_CA. 1 hit.
SM00069. GLA. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50494. Pept_Ser_Cys. 1 hit.
SSF57630. VitK_dep_GLA. 1 hit.
PROSITEPS00010. 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]
ProtoNetSearch...

Other

BindingDBO19045.
ChEMBLCHEMBL5062.

Entry information

Entry nameFA10_RABIT
AccessionPrimary (citable) accession number: O19045
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 1, 1998
Last modified: April 3, 2013
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

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