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Reviewed, UniProtKB/Swiss-Prot Q4QXT9 (FA10_TROCA)

Last modified June 16, 2009. Version 25. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
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
Synonyms: FX
OrganismTropidechis carinatus (Australian rough-scaled snake)
Taxonomic identifier100989 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Elapidae › Notechinae › Tropidechis

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Protein attributes

Sequence length483 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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 By similarity.

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 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.

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

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Propeptide21 – 4020 By similarity
PRO_0000043201
Chain41 – 483443Coagulation factor X
PRO_0000043202
Chain41 – 177137Factor X light chain By similarity
PRO_0000043203
Chain183 – 472290Factor X heavy chain By similarity
PRO_0000043204
Propeptide183 – 23856Activation peptide By similarity
PRO_0000043205
Chain239 – 483245Activated factor Xa heavy chain By similarity
PRO_0000043206

Regions

Domain41 – 8646Gla
Domain86 – 12237EGF-like 1; calcium-binding Potential
Domain125 – 16541EGF-like 2
Domain239 – 470232Peptidase S1

Sites

Active site2801Charge relay system By similarity
Active site3251Charge relay system By similarity
Active site4221Charge 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
Glycosylation921O-linked (Hex...) By similarity
Glycosylation2111N-linked (GlcNAc...) Potential
Glycosylation2231N-linked (GlcNAc...) Potential
Glycosylation2411N-linked (GlcNAc...) Potential
Glycosylation2831N-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 ↔ 345Interchain (between light and heavy chains) By similarity
Disulfide bond245 ↔ 250 By similarity
Disulfide bond265 ↔ 281 By similarity
Disulfide bond393 ↔ 407 By similarity
Disulfide bond418 ↔ 446 By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q4QXT9-1 [UniParc].

Last modified July 19, 2005. Version 1.
Checksum: F040EAC534BC960F

FASTA48353,901
        10         20         30         40         50         60 
MAPQLLLCLI LTFLWSLSEA ESNVFLKSKV ANRFLQRTKR ANSLFEEFKA GNIERECIEE 

        70         80         90        100        110        120 
RCSKEEAREA FEDNEKTETF WNVYVDGDQC SSNPCHYGGT CKDGIGSYTC TCLAGYEGKN 

       130        140        150        160        170        180 
CQYVLYQSCR VDNGNCWHFC KPVQNEIQCS CAESYLLGDD GYSCVAGGDF SCGRNIKARN 

       190        200        210        220        230        240 
KREASLPDFQ TDFSDDYDAI DENNFVETPT NFSGLVPTVQ SQNATLLKKS DNPSPDIRVV 

       250        260        270        280        290        300 
NGTDCKLGEC PWQALLINDQ GDGFCGGTIL SPIYVLTAAH CINQTKYIRV VVGEIDISRK 

       310        320        330        340        350        360 
KTGRLLSVDK IYVHQKFVPS TYDYDIALIQ MKTPIQFSEN VVPACLPTAD FANQVLMKQD 

       370        380        390        400        410        420 
FGIVSGFGRT RERGQTSNTL KVVTLPYVDR HTCMLSSNFP ITQNMFCAGY NTLPQDACQG 

       430        440        450        460        470        480 
DSGGPHITAY RDTHFITGII SWGEGCAQTG KYGAYTKVSR FILWIKRIMR LKLPSTESST 


GRL

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References

[1]"Two parallel prothrombin activator systems in Australian rough-scaled snake, Tropidechis carinatus. Structural comparison of venom prothrombin activator with blood coagulation factor X."
Reza M.A., Swarup S., Kini R.M.
Thromb. Haemost. 93:40-47(2005) [PubMed: 15630489] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.

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Cross-references

Sequence databases

AY651849 mRNA. Translation: AAV65959.1.

3D structure databases

ModBaseSearch...

Phylogenomic databases

HOVERGENQ4QXT9.

Enzyme and pathway databases

BRENDA3.4.21.6. 295067.

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.
IPR001438. EGF_2.
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. 1 hit.
PF00594. Gla. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFPIRSF001143. Factor_X. 1 hit.
PRINTSPR00722. CHYMOTRYPSIN.
PR00010. EGFBLOOD.
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. 1 hit.
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...

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Entry information

Entry nameFA10_TROCA
AccessionPrimary (citable) accession number: Q4QXT9
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: July 19, 2005
Last modified: June 16, 2009
This is version 25 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

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Relevant documents

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