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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)DescriptionActionsGraphical viewLength
Active sitei251Charge relay systemBy similarity1
Active sitei308Charge relay systemBy similarity1
Active sitei405Charge relay systemBy similarity1

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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Sequence analysisAdd BLAST20
PropeptideiPRO_000040972221 – 40By similarityAdd BLAST20
ChainiPRO_000002781641 – 181Hopsarin-D light chainAdd BLAST141
PropeptideiPRO_5000095361182 – 209Activation peptide1 PublicationAdd BLAST28
ChainiPRO_0000027817210 – 455Hopsarin-D heavy chainAdd BLAST246

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei464-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei474-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei544-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei564-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Disulfide bondi57 ↔ 62By similarity
Modified residuei594-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei604-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei654-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei664-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei694-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei724-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei754-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Disulfide bondi90 ↔ 101By similarity
Glycosylationi92O-linked (Hex...)1 Publication1
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
Glycosylationi254N-linked (GlcNAc...)1 Publication1
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)DescriptionActionsGraphical viewLength
Sitei103Not modified1

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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini41 – 86GlaPROSITE-ProRule annotationAdd BLAST46
Domaini86 – 121EGF-like 1; calcium-bindingPROSITE-ProRule annotationAdd BLAST36
Domaini129 – 164EGF-like 2PROSITE-ProRule annotationAdd BLAST36
Domaini210 – 453Peptidase S1PROSITE-ProRule annotationAdd BLAST244

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

CDDicd00190. Tryp_SPc. 1 hit.
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)DescriptionActionsGraphical viewLength
Sequence conflicti78E → T AA sequence (PubMed:12403650).Curated1
Sequence conflicti98H → R AA sequence (PubMed:12403650).Curated1
Sequence conflicti260 – 270Missing AA sequence (PubMed:12403650).CuratedAdd BLAST11
Sequence conflicti402E → Q AA sequence (PubMed:12403650).Curated1

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.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiS01.426.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG013304.

Family and domain databases

CDDicd00190. Tryp_SPc. 1 hit.
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...

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: October 5, 2016
This is version 98 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.