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P81428

- FAXD_TROCA

UniProt

P81428 - FAXD_TROCA

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Protein

Venom prothrombin activator trocarin-D

Gene
N/A
Organism
Tropidechis carinatus (Australian rough-scaled snake)
Status
Reviewed - 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 system By similarity
Active sitei308 – 3081Charge relay system By similarity
Active sitei405 – 4051Charge relay system By similarity

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. peptidase activator activity Source: UniProtKB-KW
  3. serine-type endopeptidase activity Source: UniProtKB

GO - Biological processi

  1. blood coagulation Source: InterPro
  2. envenomation resulting in positive regulation of blood coagulation in other organism Source: UniProtKB
  3. positive regulation of blood coagulation in other organism Source: UniProtKB
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

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

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020 Reviewed predictionAdd
BLAST
Propeptidei21 – 4020PRO_0000043207Add
BLAST
Chaini41 – 181141Trocarin-D light chainPRO_0000027822Add
BLAST
Propeptidei182 – 20928Activation peptidePRO_0000043208Add
BLAST
Chaini210 – 455246Trocarin-D heavy chainPRO_0000027823Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei46 – 4614-carboxyglutamate1 Publication
Modified residuei47 – 4714-carboxyglutamate1 Publication
Modified residuei54 – 5414-carboxyglutamate1 Publication
Modified residuei56 – 5614-carboxyglutamate1 Publication
Disulfide bondi57 ↔ 62 By similarity
Modified residuei59 – 5914-carboxyglutamate1 Publication
Modified residuei60 – 6014-carboxyglutamate1 Publication
Modified residuei65 – 6514-carboxyglutamate1 Publication
Modified residuei66 – 6614-carboxyglutamate1 Publication
Modified residuei69 – 6914-carboxyglutamate1 Publication
Modified residuei72 – 7214-carboxyglutamate1 Publication
Modified residuei75 – 7514-carboxyglutamate1 Publication
Disulfide bondi90 ↔ 101 By similarity
Glycosylationi92 – 921O-linked (Hex...)2 Publications
Disulfide bondi95 ↔ 110 By similarity
Disulfide bondi112 ↔ 121 By similarity
Disulfide bondi129 ↔ 140 By similarity
Disulfide bondi136 ↔ 149 By similarity
Disulfide bondi151 ↔ 164 By similarity
Disulfide bondi172 ↔ 328Interchain (between light and heavy chains) By similarity
Disulfide bondi216 ↔ 221 By similarity
Disulfide bondi236 ↔ 252 By similarity
Glycosylationi254 – 2541N-linked (GlcNAc...)2 Publications
Disulfide bondi376 ↔ 390 By similarity
Disulfide bondi401 ↔ 429 By similarity

Post-translational modificationi

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.

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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini41 – 8646GlaAdd
BLAST
Domaini86 – 12237EGF-like 1; calcium-bindingAdd
BLAST
Domaini129 – 16436EGF-like 2Add
BLAST
Domaini210 – 453244Peptidase S1Add
BLAST

Sequence similaritiesi

Contains 2 EGF-like domains.

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

MAPQLLLCLI LTFLWSLPEA ESNVFLKSKV ANRFLQRTKR SNSLFEEIRP    50
GNIERECIEE KCSKEEAREV FEDNEKTETF WNVYVDGDQC SSNPCHYRGT 100
CKDGIGSYTC TCLPNYEGKN CEKVLYQSCR VDNGNCWHFC KRVQSETQCS 150
CAESYRLGVD GHSCVAEGDF SCGRNIKARN KREASLPDFV QSQKATLLKK 200
SDNPSPDIRI VNGMDCKLGE CPWQAVLINE KGEVFCGGTI LSPIHVLTAA 250
HCINQTKSVS VIVGEIDISR KETRRLLSVD KIYVHTKFVP PNYYYVHQNF 300
DRVAYDYDIA IIRMKTPIQF SENVVPACLP TADFANEVLM KQDSGIVSGF 350
GRIQFKQPTS NTLKVITVPY VDRHTCMLSS DFRITQNMFC AGYDTLPQDA 400
CQGDSGGPHI TAYRDTHFIT GIISWGEGCA RKGKYGVYTK VSKFIPWIKK 450
IMSLK 455
Length:455
Mass (Da):51,407
Last modified:December 6, 2005 - v2
Checksum:i65C8571B662782DC
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti260 – 27011Missing AA sequence 1 PublicationAdd
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AY769963 mRNA. Translation: AAV34695.1 .
DQ017707 mRNA. Translation: AAY85309.1 .
DQ533832 Genomic DNA. Translation: ABG02404.1 .

3D structure databases

ProteinModelPortali P81428.
SMRi P81428. Positions 42-86, 210-453.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi S01.425.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOVERGENi HBG013304.

Family and domain databases

Gene3Di 4.10.740.10. 1 hit.
InterProi IPR017857. 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 ]
Pfami PF00008. EGF. 1 hit.
PF00594. Gla. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view ]
PIRSFi PIRSF001143. Factor_X. 1 hit.
PRINTSi PR00722. CHYMOTRYPSIN.
PR00001. GLABLOOD.
SMARTi SM00181. EGF. 1 hit.
SM00179. EGF_CA. 1 hit.
SM00069. GLA. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view ]
SUPFAMi SSF50494. SSF50494. 2 hits.
SSF57630. SSF57630. 1 hit.
PROSITEi PS00010. 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 ]
ProtoNeti Search...

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: May 14, 2014
This is version 106 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

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