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P81428 (FAXD_TROCA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Venom prothrombin activator trocarin-D

Short name=vPA
EC=3.4.21.6
Alternative name(s):
Venom coagulation factor Xa-like protease

Cleaved into the following 2 chains:

  1. Trocarin-D light chain
  2. Trocarin-D heavy chain
OrganismTropidechis carinatus (Australian rough-scaled snake)
Taxonomic identifier100989 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaElapidaeNotechinaeTropidechis

Protein attributes

Sequence length455 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Snake prothrombin activator that attacks the hemostatic system of prey. This protein is functionally similar to blood coagulation factor Xa. Induces cyanosis and death in mice at 1 mg/kg body weight during blood clotting. Ref.3

Catalytic activity

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

Enzyme regulation

Activated by calcium and phospholipids.

Subunit structure

Heterodimer of a light chain and a heavy chain; disulfide-linked.

Subcellular location

Secreted Ref.3 Ref.5.

Tissue specificity

Expressed by the venom gland. Ref.3 Ref.5

Post-translational modification

Gamma-carboxyglutamate residues are formed by vitamin K dependent carboxylation. These residues are essential for the binding of calcium.

The O-linked saccharides at Ser-92 are a mixture of Xyl-Glc, and Glc along with smaller amounts of Xyl-GlcNAc, GlcNAc, Gal, GalNAc, Xyl-Gal, and Xyl-GalNAc, suggesting that the glycosyl transferases responsible for this modification are non-specific. The N-linked carbohydrate at Asn-254 (Asn-45 of the heavy chain) is a sialylated and diantennary oligosaccharide.

Miscellaneous

Is classified in the group D of snake venom prothrombin activators, since it requires the mammalian factor Va for maximal activity for the cleavage of prothrombin.

In contrast to blood coagulation factors that circulate as inactive zymogen in plasma, venom prothrombin activators are always found in the active form in the venom.

Sequence similarities

Belongs to the peptidase S1 family. Snake venom subfamily.

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_0000043207
Chain41 – 181141Trocarin-D light chain
PRO_0000027822
Propeptide182 – 20928Activation peptide
PRO_0000043208
Chain210 – 455246Trocarin-D heavy chain
PRO_0000027823

Regions

Domain41 – 8646Gla
Domain86 – 12237EGF-like 1; calcium-binding
Domain129 – 16436EGF-like 2
Domain210 – 453244Peptidase S1

Sites

Active site2511Charge relay system By similarity
Active site3081Charge relay system By similarity
Active site4051Charge relay system By similarity
Site1031Not modified

Amino acid modifications

Modified residue4614-carboxyglutamate Ref.3
Modified residue4714-carboxyglutamate Ref.3
Modified residue5414-carboxyglutamate Ref.3
Modified residue5614-carboxyglutamate Ref.3
Modified residue5914-carboxyglutamate Ref.3
Modified residue6014-carboxyglutamate Ref.3
Modified residue6514-carboxyglutamate Ref.3
Modified residue6614-carboxyglutamate Ref.3
Modified residue6914-carboxyglutamate Ref.3
Modified residue7214-carboxyglutamate Ref.3
Modified residue7514-carboxyglutamate Ref.3
Glycosylation921O-linked (Hex...) Ref.3 Ref.5
Glycosylation2541N-linked (GlcNAc...) Ref.3 Ref.5
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 ↔ 328Interchain (between light and heavy chains) By similarity
Disulfide bond216 ↔ 221 By similarity
Disulfide bond236 ↔ 252 By similarity
Disulfide bond376 ↔ 390 By similarity
Disulfide bond401 ↔ 429 By similarity

Experimental info

Sequence conflict260 – 27011Missing AA sequence Ref.3

Sequences

Sequence LengthMass (Da)Tools
P81428 [UniParc].

Last modified December 6, 2005. Version 2.
Checksum: 65C8571B662782DC

FASTA45551,407
        10         20         30         40         50         60 
MAPQLLLCLI LTFLWSLPEA ESNVFLKSKV ANRFLQRTKR SNSLFEEIRP GNIERECIEE 

        70         80         90        100        110        120 
KCSKEEAREV FEDNEKTETF WNVYVDGDQC SSNPCHYRGT CKDGIGSYTC TCLPNYEGKN 

       130        140        150        160        170        180 
CEKVLYQSCR VDNGNCWHFC KRVQSETQCS CAESYRLGVD GHSCVAEGDF SCGRNIKARN 

       190        200        210        220        230        240 
KREASLPDFV QSQKATLLKK SDNPSPDIRI VNGMDCKLGE CPWQAVLINE KGEVFCGGTI 

       250        260        270        280        290        300 
LSPIHVLTAA HCINQTKSVS VIVGEIDISR KETRRLLSVD KIYVHTKFVP PNYYYVHQNF 

       310        320        330        340        350        360 
DRVAYDYDIA IIRMKTPIQF SENVVPACLP TADFANEVLM KQDSGIVSGF GRIQFKQPTS 

       370        380        390        400        410        420 
NTLKVITVPY VDRHTCMLSS DFRITQNMFC AGYDTLPQDA CQGDSGGPHI TAYRDTHFIT 

       430        440        450 
GIISWGEGCA RKGKYGVYTK VSKFIPWIKK IMSLK 

« Hide

References

[1]"Comparative analysis of prothrombin activators from the venom of Australian elapids."
St Pierre L., Masci P.P., Filippovich I., Sorokina N., Marsh N., Miller D.J., Lavin M.F.
Mol. Biol. Evol. 22:1853-1864(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Venom gland.
[2]"Structure of two genes encoding parallel prothrombin activators in Tropidechis carinatus snake: gene duplication and recruitment of factor X gene to the venom gland."
Reza M.A., Swarup S., Kini R.M.
J. Thromb. Haemost. 5:117-126(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Tissue: Venom gland.
[3]"Amino acid sequence of trocarin, a prothrombin activator from Tropidechis carinatus venom: its structural similarity to coagulation factor Xa."
Joseph J.S., Chung M.C.M., Jeyaseelan K., Kini R.M.
Blood 94:621-631(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 41-181 AND 210-455, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GAMMA-CARBOXYGLUTAMATION AT GLU-46; GLU-47; GLU-54; GLU-56; GLU-59; GLU-60; GLU-65; GLU-66; GLU-69; GLU-72 AND GLU-75, GLYCOSYLATION AT SER-92 AND ASN-254.
Tissue: Venom.
[4]"Classification and nomenclature of prothrombin activators isolated from snake venoms."
Manjunatha Kini R., Morita T., Rosing J.
Thromb. Haemost. 86:710-711(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NOMENCLATURE.
[5]"Occurrence of O-linked Xyl-GlcNAc and Xyl-Glc disaccharides in trocarin, a factor Xa homolog from snake venom."
Joseph J.S., Valiyaveettil M., Gowda D.C., Kini R.M.
J. Thromb. Haemost. 1:545-550(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION AT SER-92 AND ASN-254, SIALIC ACID CONTENT, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Venom.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY769963 mRNA. Translation: AAV34695.1.
DQ017707 mRNA. Translation: AAY85309.1.
DQ533832 Genomic DNA. Translation: ABG02404.1.

3D structure databases

ProteinModelPortalP81428.
SMRP81428. Positions 42-86, 210-453.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSS01.425.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG013304.

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_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]
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. SSF50494. 2 hits.
SSF57630. SSF57630. 1 hit.
PROSITEPS00010. ASX_HYDROXYL. 1 hit.
PS00022. EGF_1. 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...

Entry information

Entry nameFAXD_TROCA
AccessionPrimary (citable) accession number: P81428
Secondary accession number(s): Q1L657, Q5UAE9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: December 6, 2005
Last modified: April 16, 2014
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries