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Protein

Venom prothrombin activator trocarin-D

Gene
N/A
Organism
Tropidechis carinatus (Australian rough-scaled snake)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

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

Enzyme regulationi

Activated by calcium and phospholipids.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei103 – 1031Not modified
Active sitei251 – 2511Charge relay systemBy similarity
Active sitei308 – 3081Charge relay systemBy similarity
Active sitei405 – 4051Charge relay systemBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Blood coagulation cascade activating toxin, Hemostasis impairing toxin, Hydrolase, Protease, Prothrombin activator, Serine protease, Toxin

Keywords - Ligandi

Calcium, Sialic acid

Protein family/group databases

MEROPSiS01.425.

Names & Taxonomyi

Protein namesi
Recommended name:
Venom prothrombin activator trocarin-D (EC:3.4.21.6)
Short name:
vPA
Alternative name(s):
Venom coagulation factor Xa-like protease
Cleaved into the following 2 chains:
OrganismiTropidechis carinatus (Australian rough-scaled snake)
Taxonomic identifieri100989 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaElapidaeNotechinaeTropidechis

Subcellular locationi

  • Secreted 2 Publications

GO - Cellular componenti

  • extracellular region Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence AnalysisAdd
BLAST
Propeptidei21 – 40201 PublicationPRO_0000043207Add
BLAST
Chaini41 – 181141Trocarin-D light chainPRO_0000027822Add
BLAST
Propeptidei182 – 20928Activation peptide1 PublicationPRO_0000043208Add
BLAST
Chaini210 – 455246Trocarin-D heavy chainPRO_0000027823Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei46 – 4614-carboxyglutamatePROSITE-ProRule annotation1 Publication
Modified residuei47 – 4714-carboxyglutamatePROSITE-ProRule annotation1 Publication
Modified residuei54 – 5414-carboxyglutamatePROSITE-ProRule annotation1 Publication
Modified residuei56 – 5614-carboxyglutamatePROSITE-ProRule annotation1 Publication
Disulfide bondi57 ↔ 62By similarity
Modified residuei59 – 5914-carboxyglutamatePROSITE-ProRule annotation1 Publication
Modified residuei60 – 6014-carboxyglutamatePROSITE-ProRule annotation1 Publication
Modified residuei65 – 6514-carboxyglutamatePROSITE-ProRule annotation1 Publication
Modified residuei66 – 6614-carboxyglutamatePROSITE-ProRule annotation1 Publication
Modified residuei69 – 6914-carboxyglutamatePROSITE-ProRule annotation1 Publication
Modified residuei72 – 7214-carboxyglutamatePROSITE-ProRule annotation1 Publication
Modified residuei75 – 7514-carboxyglutamatePROSITE-ProRule annotation1 Publication
Disulfide bondi90 ↔ 101By similarity
Glycosylationi92 – 921O-linked (Hex...)2 Publications
Disulfide bondi95 ↔ 110By similarity
Disulfide bondi112 ↔ 121By similarity
Disulfide bondi129 ↔ 140By similarity
Disulfide bondi136 ↔ 149By similarity
Disulfide bondi151 ↔ 164By similarity
Disulfide bondi172 ↔ 328Interchain (between light and heavy chains)PROSITE-ProRule annotation
Disulfide bondi216 ↔ 221By similarity
Disulfide bondi236 ↔ 252By similarity
Glycosylationi254 – 2541N-linked (GlcNAc...)2 Publications
Disulfide bondi376 ↔ 390By similarity
Disulfide bondi401 ↔ 429By similarity

Post-translational modificationi

Gamma-carboxyglutamate residues are formed by vitamin K dependent carboxylation. These residues are essential for the binding of calcium.PROSITE-ProRule annotation1 Publication
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.2 Publications

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Gamma-carboxyglutamic acid, Glycoprotein

Expressioni

Tissue specificityi

Expressed by the venom gland.2 Publications

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliP81428.
SMRiP81428. Positions 42-86, 210-453.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini41 – 8646GlaPROSITE-ProRule annotationAdd
BLAST
Domaini86 – 12237EGF-like 1; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini129 – 16436EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini210 – 453244Peptidase S1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase S1 family. Snake venom subfamily.PROSITE-ProRule annotation
Contains 2 EGF-like domains.PROSITE-ProRule annotation
Contains 1 Gla (gamma-carboxy-glutamate) domain.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

HOVERGENiHBG013304.

Family and domain databases

Gene3Di4.10.740.10. 1 hit.
InterProiIPR017857. 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]
PfamiPF00008. EGF. 1 hit.
PF00594. Gla. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFiPIRSF001143. Factor_X. 1 hit.
PRINTSiPR00722. CHYMOTRYPSIN.
PR00001. GLABLOOD.
SMARTiSM00181. EGF. 1 hit.
SM00179. EGF_CA. 1 hit.
SM00069. GLA. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 2 hits.
SSF57630. SSF57630. 1 hit.
PROSITEiPS00010. 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]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P81428-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPQLLLCLI LTFLWSLPEA ESNVFLKSKV ANRFLQRTKR SNSLFEEIRP
60 70 80 90 100
GNIERECIEE KCSKEEAREV FEDNEKTETF WNVYVDGDQC SSNPCHYRGT
110 120 130 140 150
CKDGIGSYTC TCLPNYEGKN CEKVLYQSCR VDNGNCWHFC KRVQSETQCS
160 170 180 190 200
CAESYRLGVD GHSCVAEGDF SCGRNIKARN KREASLPDFV QSQKATLLKK
210 220 230 240 250
SDNPSPDIRI VNGMDCKLGE CPWQAVLINE KGEVFCGGTI LSPIHVLTAA
260 270 280 290 300
HCINQTKSVS VIVGEIDISR KETRRLLSVD KIYVHTKFVP PNYYYVHQNF
310 320 330 340 350
DRVAYDYDIA IIRMKTPIQF SENVVPACLP TADFANEVLM KQDSGIVSGF
360 370 380 390 400
GRIQFKQPTS NTLKVITVPY VDRHTCMLSS DFRITQNMFC AGYDTLPQDA
410 420 430 440 450
CQGDSGGPHI TAYRDTHFIT GIISWGEGCA RKGKYGVYTK VSKFIPWIKK

IMSLK
Length:455
Mass (Da):51,407
Last modified:December 6, 2005 - v2
Checksum:i65C8571B662782DC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti260 – 27011Missing AA sequence (PubMed:10397729).CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY769963 mRNA. Translation: AAV34695.1.
DQ017707 mRNA. Translation: AAY85309.1.
DQ533832 Genomic DNA. Translation: ABG02404.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY769963 mRNA. Translation: AAV34695.1.
DQ017707 mRNA. Translation: AAY85309.1.
DQ533832 Genomic DNA. Translation: ABG02404.1.

3D structure databases

ProteinModelPortaliP81428.
SMRiP81428. Positions 42-86, 210-453.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiS01.425.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG013304.

Family and domain databases

Gene3Di4.10.740.10. 1 hit.
InterProiIPR017857. 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]
PfamiPF00008. EGF. 1 hit.
PF00594. Gla. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFiPIRSF001143. Factor_X. 1 hit.
PRINTSiPR00722. CHYMOTRYPSIN.
PR00001. GLABLOOD.
SMARTiSM00181. EGF. 1 hit.
SM00179. EGF_CA. 1 hit.
SM00069. GLA. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 2 hits.
SSF57630. SSF57630. 1 hit.
PROSITEiPS00010. 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]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiFAXD_TROCA
AccessioniPrimary (citable) accession number: P81428
Secondary accession number(s): Q1L657, Q5UAE9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: December 6, 2005
Last modified: October 1, 2014
This is version 107 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
Annotation programAnimal Toxin Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

Direct protein sequencing

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.