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Protein

Venom prothrombin activator hopsarin-D

Gene
N/A
Organism
Hoplocephalus stephensii (Stephens' banded 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. The procoagulant activity of hopsarin-D is approximately 10-fold lower than that of trocarin-D and FXa.1 Publication

Catalytic activityi

Selective cleavage of Arg-|-Thr and then Arg-|-Ile bonds in prothrombin to form thrombin.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
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

Protein family/group databases

MEROPSiS01.426.

Names & Taxonomyi

Protein namesi
Recommended name:
Venom prothrombin activator hopsarin-D (EC:3.4.21.6)
Short name:
vPA
Alternative name(s):
Venom coagulation factor Xa-like protease
Cleaved into the following 2 chains:
OrganismiHoplocephalus stephensii (Stephens' banded snake)Curated
Taxonomic identifieri196418 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaElapidaeNotechinaeHoplocephalus

Subcellular locationi

  • Secreted 1 Publication

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 – 4020By similarityPRO_0000409722Add
BLAST
Chaini41 – 181141Hopsarin-D light chainPRO_0000027816Add
BLAST
Propeptidei182 – 20928Activation peptide1 PublicationPRO_5000095361Add
BLAST
Chaini210 – 455246Hopsarin-D heavy chainPRO_0000027817Add
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...)1 Publication
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 bondi236 ↔ 252By similarity
Glycosylationi254 – 2541N-linked (GlcNAc...)1 Publication
Disulfide bondi376 ↔ 390By similarity
Disulfide bondi401 ↔ 429By similarity

Post-translational modificationi

The vitamin K-dependent, enzymatic carboxylation of some glutamate residues allows the modified protein to bind calcium.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei103 – 1031Not modified

Keywords - PTMi

Disulfide bond, Gamma-carboxyglutamic acid, Glycoprotein

Expressioni

Tissue specificityi

Expressed by the venom gland.1 Publication

Interactioni

Subunit structurei

Heterodimer of a light chain and a heavy chain; disulfide-linked.1 Publication

Structurei

3D structure databases

ProteinModelPortaliP83370.
SMRiP83370. Positions 42-86, 210-453.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini41 – 8646GlaPROSITE-ProRule annotationAdd
BLAST
Domaini86 – 12136EGF-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.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR000294. GLA_domain.
IPR012224. Pept_S1A_FX.
IPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[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. 2 hits.
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.

P83370-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPQLLLCLI LTFLWSVPEA ESNVFLKSKV ANRFLQRTKR SNSLFEEIRP
60 70 80 90 100
GNIERECIEE KCSKEEAREV FEDNEKTETF WNVYVDGDQC SSNPCHYHGT
110 120 130 140 150
CKDGIGSYTC TCLPNYEGKN CEKVLFKSCR AFNGNCWHFC KRVQSETQCS
160 170 180 190 200
CAESYRLGVD GHSCVAEGDF SCGRNIKARN KREASLPDFV QSQKATLLKK
210 220 230 240 250
SDNPSPDIRI VNGMDSKLGE CPWQAVLINE KGEVFCGGTI LSPIHVLTAA
260 270 280 290 300
HCINQTKSVS VIVGEIDISR KETRRLLSVD KIYVHTKFVP PNYYYGHQNF
310 320 330 340 350
DRVAYDYDIA IIRMKTPIQF SENVVPACLP TADFANEVLM KQDSGIVSGF
360 370 380 390 400
GRIRFKEPTS NTLKVITVPY VDRHTCMLSS DFRITQNMFC AGYDTLPQDA
410 420 430 440 450
CEGDSGGPHI TAYGDTHFIT GIVSWGEGCA RKGKYGVYTK VSRFIPWIKK

IMSLK
Length:455
Mass (Da):51,248
Last modified:June 28, 2011 - v2
Checksum:i39B5F4442B995E4F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti78 – 781E → T AA sequence (PubMed:12403650).Curated
Sequence conflicti98 – 981H → R AA sequence (PubMed:12403650).Curated
Sequence conflicti260 – 27011Missing AA sequence (PubMed:12403650).CuratedAdd
BLAST
Sequence conflicti402 – 4021E → Q AA sequence (PubMed:12403650).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY940208 mRNA. Translation: AAX37264.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY940208 mRNA. Translation: AAX37264.1.

3D structure databases

ProteinModelPortaliP83370.
SMRiP83370. Positions 42-86, 210-453.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiS01.426.

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.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR000294. GLA_domain.
IPR012224. Pept_S1A_FX.
IPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[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. 2 hits.
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. "Group D prothrombin activators from snake venom are structural homologues of mammalian blood coagulation factor Xa."
    Rao V.S., Joseph J.S., Kini R.M.
    Biochem. J. 369:635-642(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 41-181 AND 210-455, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, 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, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Venom.
  3. "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.

Entry informationi

Entry nameiFAXD_HOPST
AccessioniPrimary (citable) accession number: P83370
Secondary accession number(s): Q58L92
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2003
Last sequence update: June 28, 2011
Last modified: May 11, 2016
This is version 96 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program
Annotation programChordata Protein 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.

Caution

Lacks the Cys residue in position 216 that is replaced by a Ser residue, resulting of a loss a disulfide bond. This may contribute to the lower procoagulant activity.Curated

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

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 one 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.