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Protein

Venom prothrombin activator omicarin-C catalytic subunit

Gene
N/A
Organism
Oxyuranus microlepidotus (Inland taipan)
Status
Reviewed-Annotation score: -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

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.

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)DescriptionActionsGraphical viewLength
Active sitei251Charge relay systemBy similarity1
Active sitei309Charge relay systemBy similarity1
Active sitei406Charge relay systemBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionBlood coagulation cascade activating toxin, Hemostasis impairing toxin, Hydrolase, Protease, Prothrombin activator, Serine protease, Toxin
LigandCalcium

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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Sequence analysisAdd BLAST20
PropeptideiPRO_000040988921 – 40By similarityAdd BLAST20
ChainiPRO_500009534841 – 181Omicarin-C catalytic subunit light chainAdd BLAST141
PropeptideiPRO_5000095349182 – 209Activation peptideBy similarityAdd BLAST28
ChainiPRO_5000095350210 – 467Omicarin-C catalytic subunit heavy chainAdd BLAST258

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei464-carboxyglutamatePROSITE-ProRule annotation1
Modified residuei474-carboxyglutamatePROSITE-ProRule annotation1
Modified residuei544-carboxyglutamatePROSITE-ProRule annotation1
Modified residuei564-carboxyglutamatePROSITE-ProRule annotation1
Disulfide bondi57 ↔ 62By similarity
Modified residuei594-carboxyglutamatePROSITE-ProRule annotation1
Modified residuei604-carboxyglutamatePROSITE-ProRule annotation1
Modified residuei654-carboxyglutamatePROSITE-ProRule annotation1
Modified residuei664-carboxyglutamatePROSITE-ProRule annotation1
Modified residuei694-carboxyglutamatePROSITE-ProRule annotation1
Modified residuei724-carboxyglutamatePROSITE-ProRule annotation1
Modified residuei754-carboxyglutamatePROSITE-ProRule annotation1
Disulfide bondi90 ↔ 101By similarity
Glycosylationi92O-linked (Hex...) serineBy similarity1
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
Glycosylationi254N-linked (GlcNAc...) asparagineSequence analysis1
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)DescriptionActionsGraphical viewLength
Sitei209 – 210CleavageBy similarity2

Keywords - PTMi

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

Proteomic databases

PRIDEiQ58L95

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
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini41 – 86GlaPROSITE-ProRule annotationAdd BLAST46
Domaini86 – 122EGF-like 1; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini129 – 164EGF-like 2PROSITE-ProRule annotationAdd BLAST36
Domaini210 – 454Peptidase S1PROSITE-ProRule annotationAdd BLAST245

Sequence similaritiesi

Belongs to the peptidase S1 family. Snake venom subfamily.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
InterProiView protein in InterPro
IPR017857 Coagulation_fac-like_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
IPR035972 GLA-like_dom_SF
IPR000294 GLA_domain
IPR012224 Pept_S1A_FX
IPR009003 Peptidase_S1_PA
IPR001314 Peptidase_S1A
IPR001254 Trypsin_dom
IPR018114 TRYPSIN_HIS
IPR033116 TRYPSIN_SER
PfamiView protein in Pfam
PF00008 EGF, 1 hit
PF00594 Gla, 1 hit
PF00089 Trypsin, 1 hit
PIRSFiPIRSF001143 Factor_X, 1 hit
PRINTSiPR00722 CHYMOTRYPSIN
PR00001 GLABLOOD
SMARTiView protein in SMART
SM00181 EGF, 2 hits
SM00179 EGF_CA, 1 hit
SM00069 GLA, 1 hit
SM00020 Tryp_SPc, 1 hit
SUPFAMiSSF50494 SSF50494, 2 hits
SSF57630 SSF57630, 1 hit
PROSITEiView protein in PROSITE
PS00010 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

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

Similar proteinsi

Entry informationi

Entry nameiFAXC_OXYMI
AccessioniPrimary (citable) accession number: Q58L95
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 28, 2011
Last sequence update: April 26, 2005
Last modified: May 23, 2018
This is version 99 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
Annotation programAnimal Toxin Annotation Program

Miscellaneousi

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

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