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Reviewed, UniProtKB/Swiss-Prot P00743 (FA10_BOVIN)

Last modified June 16, 2009. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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- Recommended name:
            Factor X light chain
    2- Recommended name:
            Factor X heavy chain
    3- Recommended name:
            Activated factor Xa heavy chain
Gene names
Name: F10
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

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Protein attributes

Sequence length492 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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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.

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.

Subcellular location

Secreted.

Post-translational modification

The vitamin K-dependent, enzymatic carboxylation of some glutamate residues allows the modified protein to bind calcium.

N- and O-glycosylated. Ref.4 Ref.5

The activation peptide is cleaved by factor IXa (in the intrinsic pathway), or by factor VIIa (in the extrinsic pathway). Ref.7

The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.

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.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Propeptide24 – 4017 Ref.2
PRO_0000027779
Chain41 – 492452Coagulation factor X
PRO_0000027780
Chain41 – 180140Factor X light chain
PRO_0000027781
Chain183 – 492310Factor X heavy chain
PRO_0000027782
Propeptide183 – 23351Activation peptide
PRO_0000027783
Chain234 – 492259Activated factor Xa heavy chain
PRO_0000027784
Propeptide476 – 49217May be removed but is not necessary for activation
PRO_0000027785

Regions

Domain41 – 8545Gla
Domain86 – 12237EGF-like 1; calcium-binding Potential
Domain125 – 16541EGF-like 2
Domain234 – 466233Peptidase S1

Sites

Active site2751Charge relay system Ref.6
Active site3211Charge relay system Ref.6
Active site4181Charge relay system Ref.6
Site233 – 2342Cleavage; by coagulation factor IXa and coagulation factor VIIa

Amino acid modifications

Modified residue4614-carboxyglutamate
Modified residue4714-carboxyglutamate
Modified residue5414-carboxyglutamate
Modified residue5614-carboxyglutamate
Modified residue5914-carboxyglutamate Ref.2
Modified residue6014-carboxyglutamate
Modified residue6514-carboxyglutamate
Modified residue6614-carboxyglutamate
Modified residue6914-carboxyglutamate
Modified residue7214-carboxyglutamate
Modified residue7514-carboxyglutamate
Modified residue7914-carboxyglutamate
Modified residue1031(3R)-3-hydroxyaspartate
Modified residue2001Sulfotyrosine
Glycosylation2081O-linked (GalNAc...) Ref.5
Glycosylation2181N-linked (GlcNAc...) Ref.4
CAR_000011
Glycosylation4851O-linked (GalNAc...) Ref.4
Disulfide bond57 ↔ 62 By similarity
Disulfide bond90 ↔ 101 Ref.4
Disulfide bond95 ↔ 110 Ref.4
Disulfide bond112 ↔ 121 Ref.4
Disulfide bond129 ↔ 140 By similarity
Disulfide bond136 ↔ 149 By similarity
Disulfide bond151 ↔ 164 By similarity
Disulfide bond172 ↔ 341Interchain (between light and heavy chains) Ref.4
Disulfide bond240 ↔ 245 Ref.4
Disulfide bond260 ↔ 276 Ref.4
Disulfide bond389 ↔ 403 Ref.4
Disulfide bond414 ↔ 442 Ref.4

Experimental info

Sequence conflict1031D → N AA sequence Ref.2
Sequence conflict2931Missing AA sequence Ref.4
Sequence conflict296 – 2983EGN → GDE AA sequence Ref.4
Sequence conflict3351Missing AA sequence Ref.4
Sequence conflict349 – 3502EA → AE AA sequence Ref.4
Sequence conflict3551Missing AA sequence Ref.4
Sequence conflict442 – 4454CARK → GKFG AA sequence Ref.4

Secondary structure

1 ................................................................ 492
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P00743-1 [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: D5BD911FB72F1D30

FASTA49254,510
        10         20         30         40         50         60 
MAGLLHLVLL STALGGLLRP AGSVFLPRDQ AHRVLQRARR ANSFLEEVKQ GNLERECLEE 

        70         80         90        100        110        120 
ACSLEEAREV FEDAEQTDEF WSKYKDGDQC EGHPCLNQGH CKDGIGDYTC TCAEGFEGKN 

       130        140        150        160        170        180 
CEFSTREICS LDNGGCDQFC REERSEVRCS CAHGYVLGDD SKSCVSTERF PCGKFTQGRS 

       190        200        210        220        230        240 
RRWAIHTSED ALDASELEHY DPADLSPTES SLDLLGLNRT EPSAGEDGSQ VVRIVGGRDC 

       250        260        270        280        290        300 
AEGECPWQAL LVNEENEGFC GGTILNEFYV LTAAHCLHQA KRFTVRVGDR NTEQEEGNEM 

       310        320        330        340        350        360 
AHEVEMTVKH SRFVKETYDF DIAVLRLKTP IRFRRNVAPA CLPEKDWAEA TLMTQKTGIV 

       370        380        390        400        410        420 
SGFGRTHEKG RLSSTLKMLE VPYVDRSTCK LSSSFTITPN MFCAGYDTQP EDACQGDSGG 

       430        440        450        460        470        480 
PHVTRFKDTY FVTGIVSWGE GCARKGKFGV YTKVSNFLKW IDKIMKARAG AAGSRGHSEA 

       490 
PATWTVPPPL PL

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References

[1]"Blood coagulation factor X mRNA encodes a single polypeptide chain containing a prepro leader sequence."
Fung M.R., Campbell R.M., McGillivray R.T.A.
Nucleic Acids Res. 12:4481-4492(1984) [PubMed: 6330671] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-487.
[2]"Amino acid sequence of the light chain of bovine factor X1 (Stuart factor)."
Enfield D.L., Ericsson L.H., Fujikawa K., Walsh K.A., Neurath H., Titani K.
Biochemistry 19:659-667(1980) [PubMed: 6766735] [Abstract]
Cited for: PROTEIN SEQUENCE OF 41-180.
[3]"The occurrence of beta-hydroxyaspartic acid in the vitamin K-dependent blood coagulation zymogens."
McMullen B.A., Fujikawa K., Kisiel W.
Biochem. Biophys. Res. Commun. 115:8-14(1983) [PubMed: 6688526] [Abstract]
Cited for: SEQUENCE REVISION TO 103.
[4]"Bovine factor X1 (Stuart factor): amino-acid sequence of heavey chain."
Titani K., Fujikawa K., Enfield D.L., Ericsson L.H., Walsh K.A., Neurath H.
Proc. Natl. Acad. Sci. U.S.A. 72:3082-3086(1975) [PubMed: 1059093] [Abstract]
Cited for: PROTEIN SEQUENCE OF 183-492, GLYCOSYLATION AT ASN-218 AND THR-485, DISULFIDE BONDS.
[5]"Identification of O-linked oligosaccharide chains in the activation peptides of blood coagulation factor X. The role of the carbohydrate moieties in the activation of factor X."
Inoue K., Morita T.
Eur. J. Biochem. 218:153-163(1993) [PubMed: 8243461] [Abstract]
Cited for: PROTEIN SEQUENCE OF 183-233, GLYCOSYLATION AT THR-208.
[6]"Bovine factor X 1a (activated Stuart factor). Evidence of homology with mammalian serine proteases."
Titani K., Hermodson M.A., Fujikawa K., Ericsson L.H., Walsh K.A., Neurath H., Davie E.W.
Biochemistry 11:4899-4903(1972) [PubMed: 4264286] [Abstract]
Cited for: ACTIVE SITE.
[7]"Activation of bovine factor X (Stuart factor): conversion of factor Xa-alpha to factor Xa-beta."
Fujikawa K., Titani K., Davie E.W.
Proc. Natl. Acad. Sci. U.S.A. 72:3359-3363(1975) [PubMed: 1059122] [Abstract]
Cited for: PROTEOLYTIC PROCESSING.
[8]"Calcium-binding properties of bovine factor X lacking the gamma-carboxyglutamic acid-containing region."
Sugo T., Bjoerk I., Holmgren A., Stenflo J.
J. Biol. Chem. 259:5705-5710(1984) [PubMed: 6546930] [Abstract]
Cited for: CALCIUM-BINDING DATA.
[9]"Localization of the structural difference between bovine blood coagulation factors X1 and X2 to tyrosine 18 in the activation peptide."
Morita T., Jackson C.M.
J. Biol. Chem. 261:4008-4014(1986) [PubMed: 3949800] [Abstract]
Cited for: SULFATION.
[10]"1H NMR assignment and secondary structure of the Ca2(+)-free form of the amino-terminal epidermal growth factor like domain in coagulation factor X."
Selander M., Persson E., Stenflo J., Drakenberg T.
Biochemistry 29:8111-8118(1990) [PubMed: 2261466] [Abstract]
Cited for: STRUCTURE BY NMR OF 85-126.
[11]"Three-dimensional structure of the apo form of the N-terminal EGF-like module of blood coagulation factor X as determined by NMR spectroscopy and simulated folding."
Ullner M., Selander M., Persson E., Stenflo J., Drakenberg T., Teleman O.
Biochemistry 31:5974-5983(1992) [PubMed: 1627540] [Abstract]
Cited for: STRUCTURE BY NMR OF 85-126.
[12]"How an epidermal growth factor (EGF)-like domain binds calcium. High resolution NMR structure of the calcium form of the NH2-terminal EGF-like domain in coagulation factor X."
Selander-Sunnerhagen M., Ullner M., Persson E., Teleman O., Stenflo J., Drakenberg T.
J. Biol. Chem. 267:19642-19649(1992) [PubMed: 1527084] [Abstract]
Cited for: STRUCTURE BY NMR OF 85-126.
[13]"The relative orientation of Gla and EGF domains in coagulation factor X is altered by Ca2+ binding to the first EGF domain. A combined NMR-small angle X-ray scattering study."
Sunnerhagen M., Olah G.A., Stenflo J., Forsen S., Drakenberg T., Trewhella J.
Biochemistry 35:11547-11559(1996) [PubMed: 8794734] [Abstract]
Cited for: STRUCTURE BY NMR OF 41-126.
+Additional computationally mapped references.

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Cross-references

Sequence databases

X00673 mRNA. Translation: CAA25286.1.
IPIIPI00685993.
PIREXBO. A22867.
RefSeqXP_613822.3.
UniGeneBt.13151

3D structure databases

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[»]
ModBaseSearch...

Protein family/group databases

MEROPSS01.216.

PTM databases

GlycoSuiteDBP00743.

Genome annotation databases

EnsemblENSBTAG00000016385. Bos taurus. [Contig view]
GeneID280787.
KEGGbta:280787.

Phylogenomic databases

HOVERGENP00743.
OMAP00743. PYVDRNT.

Enzyme and pathway databases

BRENDA3.4.21.6. 251.

Family and domain databases

InterProIPR002383. Coagulation_factor_Gla.
IPR006209. EGF.
IPR006210. EGF-like.
IPR013032. EGF-like_reg_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_CS.
IPR000742. EGF_3.
IPR001881. EGF_Ca_bd.
IPR018097. EGF_Ca_bd_CS.
IPR000294. GLA_domain.
IPR012224. Pept_S1A_FX.
IPR018114. Peptidase_S1/S6_AS.
IPR001254. Peptidase_S1_S6.
IPR001314. Peptidase_S1A.
[Graphical view]
PfamPF00008. EGF. 2 hits.
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]
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 Resources

PMAP-CutDBP00743.

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Entry information

Entry nameFA10_BOVIN
AccessionPrimary (citable) accession number: P00743
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: August 13, 1987
Last modified: June 16, 2009
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents