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P25155 (FA10_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 110. 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
Virus-activating protease
Short name=VAP

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
Synonyms:FX
OrganismGallus gallus (Chicken)
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Protein attributes

Sequence length475 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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. VAP cleaves the fusion proteins of Sendai virus, NDV, and influenza virus a at a specific single arginine-containing site, and plays a key role in the viral spreading in the allantoic sac.

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.

Tissue specificity

Liver and chorioallantoic membrane.

Post-translational modification

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

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

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

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
PRO_0000027810
Chain41 – 475435Coagulation factor X
PRO_0000027811
Chain41 – 180140Factor X light chain
PRO_0000027812
Chain186 – 475290Factor X heavy chain
PRO_0000027813
Propeptide186 – 24055Activation peptide
PRO_0000027814
Chain241 – 475235Activated factor Xa heavy chain
PRO_0000027815

Regions

Domain41 – 8545Gla
Domain86 – 12237EGF-like 1; calcium-binding Potential
Domain125 – 16844EGF-like 2
Domain241 – 473233Peptidase S1

Sites

Active site2821Charge relay system By similarity
Active site3281Charge relay system By similarity
Active site4251Charge relay system By similarity

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 residue7914-carboxyglutamate By similarity
Modified residue1031(3R)-3-hydroxyaspartate By similarity
Glycosylation1961N-linked (GlcNAc...) Potential
Glycosylation2071N-linked (GlcNAc...) Potential
Glycosylation2281N-linked (GlcNAc...) Potential
Glycosylation2851N-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 ↔ 152 By similarity
Disulfide bond154 ↔ 167 By similarity
Disulfide bond175 ↔ 348Interchain (between light and heavy chains) By similarity
Disulfide bond247 ↔ 252 By similarity
Disulfide bond267 ↔ 283 By similarity
Disulfide bond396 ↔ 410 By similarity
Disulfide bond421 ↔ 449 By similarity

Sequences

Sequence LengthMass (Da)Tools
P25155 [UniParc].

Last modified May 1, 1992. Version 1.
Checksum: 570BF84956C5C74D

FASTA47553,142
        10         20         30         40         50         60 
MAGRLLLLLL CAALPDELRA EGGVFIKKES ADKFLERTKR ANSFLEEMKQ GNIERECNEE 

        70         80         90        100        110        120 
RCSKEEAREA FEDNEKTEEF WNIYVDGDQC SSNPCHYGGQ CKDGLGSYTC SCLDGYQGKN 

       130        140        150        160        170        180 
CEFVIPKYCK INNGDCEQFC SIKKSVQKDV VCSCTSGYEL AEDGKQCVSK VKYPCGKVLM 

       190        200        210        220        230        240 
KRIKRSVILP TNSNTNATSD QDVPSTNGSI LEEVFTTTTE SPTPPPRNGS SITDPNVDTR 

       250        260        270        280        290        300 
IVGGDECRPG ECPWQAVLIN EKGEEFCGGT ILNEDFILTA AHCINQSKEI KVVVGEVDRE 

       310        320        330        340        350        360 
KEEHSETTHT AEKIFVHSKY IAETYDNDIA LIKLKEPIQF SEYVVPACLP QADFANEVLM 

       370        380        390        400        410        420 
NQKSGMVSGF GREFEAGRLS KRLKVLEVPY VDRSTCKQST NFAITENMFC AGYETEQKDA 

       430        440        450        460        470 
CQGDSGGPHV TRYKDTYFVT GIVSWGEGCA RKGKYGVYTK LSRFLRWVRT VMRQK

« Hide

References

[1]"Primary structure of the virus activating protease from chick embryo. Its identity with the blood clotting factor Xa."
Suzuki H., Harada A., Hayashi Y., Wada K., Asaka J., Gotoh B., Ogasawara T., Nagai Y.
FEBS Lett. 283:281-285(1991) [PubMed: 2044767] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Chorioallantoic membrane.
[2]"An endoprotease homologous to the blood clotting factor X as a determinant of viral tropism in chick embryo."
Gotoh B., Ogasawara T., Toyoda T., Inocencio N.M., Hamaguchi M., Nagai Y.
EMBO J. 9:4189-4195(1990) [PubMed: 2174359] [Abstract]
Cited for: PROTEIN SEQUENCE OF 41-55 AND 241-261.
Tissue: Allantoic fluid.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D00844 mRNA. Translation: BAA00724.1.
IPIIPI00587100.
PIREXCH. S15838.
RefSeqNP_990353.1. NM_205022.1.
UniGeneGga.514.

3D structure databases

ProteinModelPortalP25155.
SMRP25155. Positions 42-86, 241-475.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID395876.
KEGGgga:395876.

Organism-specific databases

CTD2159.

Phylogenomic databases

eggNOGveNOG11189.
HOVERGENHBG013304.

Family and domain databases

InterProIPR017857. Coagulation_fac_subgr_Gla_dom.
IPR006209. EGF.
IPR006210. EGF-like.
IPR001881. EGF-like_Ca-bd.
IPR013032. EGF-like_reg_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR000742. EGF_3.
IPR018097. EGF_Ca-bd_CS.
IPR000294. GLA_domain.
IPR009003. Pept_cys/ser_Trypsin-like.
IPR012224. Pept_S1A_FX.
IPR018114. Peptidase_S1/S6_AS.
IPR001254. Peptidase_S1_S6.
IPR001314. Peptidase_S1A.
[Graphical view]
Gene3DG3DSA:4.10.740.10. Coagulation_factor_Gla. 1 hit.
KOK01314.
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...

Entry information

Entry nameFA10_CHICK
AccessionPrimary (citable) accession number: P25155
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: November 16, 2011
This is version 110 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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