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P81428

- FAXD_TROCA

UniProt

P81428 - FAXD_TROCA

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
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 2 (06 Dec 2005)
      Previous versions | rss
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    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

    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

    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

    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-carboxyglutamate1 PublicationPROSITE-ProRule annotation
    Modified residuei47 – 4714-carboxyglutamate1 PublicationPROSITE-ProRule annotation
    Modified residuei54 – 5414-carboxyglutamate1 PublicationPROSITE-ProRule annotation
    Modified residuei56 – 5614-carboxyglutamate1 PublicationPROSITE-ProRule annotation
    Disulfide bondi57 ↔ 62By similarity
    Modified residuei59 – 5914-carboxyglutamate1 PublicationPROSITE-ProRule annotation
    Modified residuei60 – 6014-carboxyglutamate1 PublicationPROSITE-ProRule annotation
    Modified residuei65 – 6514-carboxyglutamate1 PublicationPROSITE-ProRule annotation
    Modified residuei66 – 6614-carboxyglutamate1 PublicationPROSITE-ProRule annotation
    Modified residuei69 – 6914-carboxyglutamate1 PublicationPROSITE-ProRule annotation
    Modified residuei72 – 7214-carboxyglutamate1 PublicationPROSITE-ProRule annotation
    Modified residuei75 – 7514-carboxyglutamate1 PublicationPROSITE-ProRule annotation
    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.1 PublicationPROSITE-ProRule annotation
    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

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    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

    Experimental Info

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