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Protein

Venom prothrombin activator omicarin-C catalytic subunit

Gene
N/A
Organism
Oxyuranus microlepidotus (Inland taipan)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Snake prothrombin activator that attacks the hemostatic system of prey. This catalytic subunit is functionally similar to blood coagulation factor Xa. It requires a non-catalytic subunit present in the venom, which is similar to coagulation factor Va, to be fully active (By similarity).By similarity

Catalytic activityi

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

Enzyme regulationi

Activated by calcium and negatively charged phospholipids.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei251 – 2511Charge relay systemBy similarity
Active sitei309 – 3091Charge relay systemBy similarity
Active sitei406 – 4061Charge 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

MEROPSiS01.446.

Names & Taxonomyi

Protein namesi
Recommended name:
Venom prothrombin activator omicarin-C catalytic subunit (EC:3.4.21.6)
Short name:
vPA
Alternative name(s):
Venom coagulation factor Xa-like protease
Cleaved into the following 2 chains:
OrganismiOxyuranus microlepidotus (Inland taipan)
Taxonomic identifieri111177 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaElapidaeAcanthophiinaeOxyuranus

Subcellular locationi

GO - Cellular componenti

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_0000409889Add
BLAST
Chaini41 – 181141Omicarin-C catalytic subunit light chainPRO_5000095348Add
BLAST
Propeptidei182 – 20928Activation peptideBy similarityPRO_5000095349Add
BLAST
Chaini210 – 467258Omicarin-C catalytic subunit heavy chainPRO_5000095350Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei46 – 4614-carboxyglutamatePROSITE-ProRule annotation
Modified residuei47 – 4714-carboxyglutamatePROSITE-ProRule annotation
Modified residuei54 – 5414-carboxyglutamatePROSITE-ProRule annotation
Modified residuei56 – 5614-carboxyglutamatePROSITE-ProRule annotation
Disulfide bondi57 ↔ 62By similarity
Modified residuei59 – 5914-carboxyglutamatePROSITE-ProRule annotation
Modified residuei60 – 6014-carboxyglutamatePROSITE-ProRule annotation
Modified residuei65 – 6514-carboxyglutamatePROSITE-ProRule annotation
Modified residuei66 – 6614-carboxyglutamatePROSITE-ProRule annotation
Modified residuei69 – 6914-carboxyglutamatePROSITE-ProRule annotation
Modified residuei72 – 7214-carboxyglutamatePROSITE-ProRule annotation
Modified residuei75 – 7514-carboxyglutamatePROSITE-ProRule annotation
Disulfide bondi90 ↔ 101By similarity
Glycosylationi92 – 921O-linked (Hex...)By similarity
Disulfide bondi95 ↔ 110By similarity
Disulfide bondi112 ↔ 121By similarity
Disulfide bondi129 ↔ 140By similarity
Disulfide bondi136 ↔ 149By similarity
Disulfide bondi151 ↔ 164By similarity
Disulfide bondi172 ↔ 329Interchain (between light and heavy chains)PROSITE-ProRule annotation
Disulfide bondi216 ↔ 221By similarity
Disulfide bondi236 ↔ 252By similarity
Glycosylationi254 – 2541N-linked (GlcNAc...)Sequence analysis
Disulfide bondi377 ↔ 391By similarity
Disulfide bondi402 ↔ 430By similarity

Post-translational modificationi

Gamma-carboxyglutamate residues are formed by vitamin K dependent carboxylation. These residues are essential for the binding of calcium.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei209 – 2102CleavageBy similarity

Keywords - PTMi

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

Expressioni

Tissue specificityi

Expressed by the venom gland.

Interactioni

Subunit structurei

Heterodimer of a light and a heavy chains; disulfide-linked. Is associated with omicarin-C non-catalytic subunit (AC Q58L90) in a non-covalent manner (By similarity).By similarity

Structurei

3D structure databases

ProteinModelPortaliQ58L95.
SMRiQ58L95. Positions 42-86, 210-456.
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 – 454245Peptidase 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

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.
PS01186. EGF_2. 2 hits.
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.

Q58L95-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPQLLLCLI LTFLWSLPEA ESNVFLKSKV ANRFLQRTKR ANSLFEEFRS
60 70 80 90 100
GNIERECIEE RCSKEEAREV FEDDEKTETF WNVYVDGDQC SSNPCHYRGT
110 120 130 140 150
CKDGIGSYTC TCLFGYEGKN CERVLYKSCR VDNGNCWHFC KPVQNDIQCS
160 170 180 190 200
CAEGYLLGED GHSCVAGGNF SCGRNIKTRN KREASLPDFV QSQNATLLKK
210 220 230 240 250
SDNPSPDIRI VNGMDCKLGE CPWQAVLVDE KEGVFCGGTI LSPIYVLTAA
260 270 280 290 300
HCINQTEKIS VVVGEIDKSR VETGHLLSVD KIYVHKKFVP PKKGYKFYEK
310 320 330 340 350
FDLVSYDYDI AIIQMKTPIQ FSENVVPACL PTADFANQVL MKQDFGIISG
360 370 380 390 400
FGRIFEKGPK SNTLKVLKVP YVDRHTCMVS SESPITPTMF CAGYDTLPRD
410 420 430 440 450
ACQGDSGGPH ITAYRDTHFI TGIVSWGEGC AKKGKYGIYT KVSKFILWIK
460
RIMRQKLPST ESSTGRL
Length:467
Mass (Da):52,467
Last modified:April 26, 2005 - v1
Checksum:i7A2F9BD327A74DD4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY940205 mRNA. Translation: AAX37261.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY940205 mRNA. Translation: AAX37261.1.

3D structure databases

ProteinModelPortaliQ58L95.
SMRiQ58L95. Positions 42-86, 210-456.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiS01.446.

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.
PS01186. EGF_2. 2 hits.
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 nameiFAXC_OXYMI
AccessioniPrimary (citable) accession number: Q58L95
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 28, 2011
Last sequence update: April 26, 2005
Last modified: September 7, 2016
This is version 86 of the entry and version 1 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 C of snake venom prothrombin activators, since it does not require the mammalian factor Va for the cleavage of prothrombin as the venom contains its own non-catalytic factor Va-like molecule.
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. Hence, catalytic and non-catalytic subunits are found naturally in venom as stable complexes.

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.