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UniProtKB - A6MFK7 (FAXD1_DEMVE)
Protein
Venom prothrombin activator vestarin-D1
Gene
N/A
Organism
Demansia vestigiata (Lesser black whip snake) (Demansia atra)
Status
Functioni
Snake prothrombin activator that attacks the hemostatic system of prey. This protein is functionally similar to blood coagulation factor Xa (By similarity).
By similarityMiscellaneous
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 255 that is replaced by a Gly residue, resulting of a loss a disulfide bond. This may contribute to a probable lower procoagulant activity.Curated
Catalytic activityi
- Selective cleavage of Arg-|-Thr and then Arg-|-Ile bonds in prothrombin to form thrombin. EC:3.4.21.6
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 270 | Charge relay systemBy similarity | 1 | |
Active sitei | 315 | Charge relay systemBy similarity | 1 | |
Active sitei | 412 | Charge relay systemBy similarity | 1 |
GO - Molecular functioni
- calcium ion binding Source: InterPro
- peptidase activator activity Source: UniProtKB-KW
- serine-type endopeptidase activity Source: UniProtKB
- toxin activity Source: UniProtKB-KW
GO - Biological processi
- blood coagulation Source: InterPro
- envenomation resulting in positive regulation of blood coagulation in other organism Source: UniProtKB
- positive regulation of blood coagulation in other organism Source: UniProtKB
Keywordsi
Molecular function | Blood coagulation cascade activating toxin, Hemostasis impairing toxin, Hydrolase, Protease, Prothrombin activator, Serine protease, Toxin |
Ligand | Calcium |
Protein family/group databases
MEROPSi | S01.396 |
Names & Taxonomyi
Protein namesi | Recommended name: Venom prothrombin activator vestarin-D1 (EC:3.4.21.6)Short name: vPA Alternative name(s): Venom coagulation factor Xa-like protease Cleaved into the following 2 chains: |
Organismi | Demansia vestigiata (Lesser black whip snake) (Demansia atra) |
Taxonomic identifieri | 412038 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Bifurcata › Unidentata › Episquamata › Toxicofera › Serpentes › Colubroidea › Elapidae › Notechinae › Demansia |
Subcellular locationi
Extracellular region or secreted
- Secreted 1 Publication
Extracellular region or secreted
- extracellular region Source: UniProtKB
Keywords - Cellular componenti
SecretedPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 20 | Sequence analysisAdd BLAST | 20 | |
PropeptideiPRO_0000409894 | 21 – 40 | By similarityAdd BLAST | 20 | |
ChainiPRO_5000254111 | 41 – 181 | Vestarin-D1 light chainAdd BLAST | 141 | |
PropeptideiPRO_0000409895 | 182 – 228 | Activation peptideBy similarityAdd BLAST | 47 | |
ChainiPRO_0000409896 | 229 – 473 | Vestarin-D1 heavy chainAdd BLAST | 245 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 46 | 4-carboxyglutamatePROSITE-ProRule annotation | 1 | |
Modified residuei | 47 | 4-carboxyglutamatePROSITE-ProRule annotation | 1 | |
Modified residuei | 54 | 4-carboxyglutamatePROSITE-ProRule annotation | 1 | |
Modified residuei | 56 | 4-carboxyglutamatePROSITE-ProRule annotation | 1 | |
Disulfide bondi | 57 ↔ 62 | By similarity | ||
Modified residuei | 59 | 4-carboxyglutamatePROSITE-ProRule annotation | 1 | |
Modified residuei | 60 | 4-carboxyglutamatePROSITE-ProRule annotation | 1 | |
Modified residuei | 65 | 4-carboxyglutamatePROSITE-ProRule annotation | 1 | |
Modified residuei | 66 | 4-carboxyglutamatePROSITE-ProRule annotation | 1 | |
Modified residuei | 69 | 4-carboxyglutamatePROSITE-ProRule annotation | 1 | |
Modified residuei | 72 | 4-carboxyglutamatePROSITE-ProRule annotation | 1 | |
Modified residuei | 75 | 4-carboxyglutamatePROSITE-ProRule annotation | 1 | |
Disulfide bondi | 90 ↔ 101 | By similarity | ||
Glycosylationi | 92 | O-linked (Hex...) serineBy similarity | 1 | |
Disulfide bondi | 95 ↔ 110 | By similarity | ||
Disulfide bondi | 112 ↔ 121 | By similarity | ||
Disulfide bondi | 129 ↔ 140 | By similarity | ||
Disulfide bondi | 136 ↔ 149 | By similarity | ||
Disulfide bondi | 151 ↔ 164 | By similarity | ||
Disulfide bondi | 172 ↔ 335 | Interchain (between light and heavy chains)PROSITE-ProRule annotation | ||
Disulfide bondi | 235 ↔ 240 | By similarity | ||
Glycosylationi | 273 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 383 ↔ 397 | By similarity | ||
Disulfide bondi | 408 ↔ 436 | By similarity |
Post-translational modificationi
The vitamin K-dependent, enzymatic carboxylation of some glutamate residues allows the modified protein to bind calcium.By similarity
Keywords - PTMi
Cleavage on pair of basic residues, Disulfide bond, Gamma-carboxyglutamic acid, GlycoproteinExpressioni
Tissue specificityi
Expressed by the venom gland.1 Publication
Interactioni
Subunit structurei
Heterodimer of a light chain and a heavy chain; disulfide-linked.
By similarityFamily & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 41 – 86 | GlaPROSITE-ProRule annotationAdd BLAST | 46 | |
Domaini | 86 – 122 | EGF-like 1; calcium-bindingPROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 129 – 164 | EGF-like 2PROSITE-ProRule annotationAdd BLAST | 36 | |
Domaini | 229 – 460 | Peptidase S1PROSITE-ProRule annotationAdd BLAST | 232 |
Sequence similaritiesi
Keywords - Domaini
EGF-like domain, Repeat, SignalFamily and domain databases
CDDi | cd00190, Tryp_SPc, 1 hit |
Gene3Di | 2.40.10.10, 2 hits 4.10.740.10, 1 hit |
InterProi | View protein in InterPro IPR017857, Coagulation_fac-like_Gla_dom IPR001881, EGF-like_Ca-bd_dom 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 IPR043504, Peptidase_S1_PA_chymotrypsin IPR001314, Peptidase_S1A IPR001254, Trypsin_dom IPR018114, TRYPSIN_HIS IPR033116, TRYPSIN_SER |
Pfami | View protein in Pfam PF00008, EGF, 1 hit PF00594, Gla, 1 hit PF00089, Trypsin, 1 hit |
PIRSFi | PIRSF001143, Factor_X, 1 hit |
PRINTSi | PR00722, CHYMOTRYPSIN PR00001, GLABLOOD |
SMARTi | View protein in SMART SM00181, EGF, 2 hits SM00179, EGF_CA, 1 hit SM00069, GLA, 1 hit SM00020, Tryp_SPc, 1 hit |
SUPFAMi | SSF50494, SSF50494, 1 hit SSF57630, SSF57630, 1 hit |
PROSITEi | View 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 |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
A6MFK7-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MAPQLLLCLI QTFLWSLPEA ESNVFLKSNV ANRFLQRTKR ANSGFEEIYP
60 70 80 90 100
ANFERECVEE RCSKEEAREV FEDDEKTEAF WTVYVDGDQC LSNPCHYGGT
110 120 130 140 150
CKDGIGSYTC TCLAGYEGKN CEHDLLKSCR VDNGNCWHFC KPVQNDTQCS
160 170 180 190 200
CAEGYRLGDN GFSCIAEGEF SCGRNIKSRN KREASLPDFQ TDFSDDYDAI
210 220 230 240 250
DENNLIETVQ SQSATLLKKS DNPNPDIRIV NGLDCKLGEC PWQAVLIDEK
260 270 280 290 300
GTAFGGGTIL SPYFVLTAAH CINKTKSIAV VVGQVDISRK ETRRLLSVDK
310 320 330 340 350
VYTHPKYVHV TNDYDIAIIQ LKTPIQFSEN VVPACLPTAD FANHVLMKQD
360 370 380 390 400
FGIVSGFGRI EEKGPTSNIL KVVMVPYVDR HTCILSTKIP ITRNMFCAGY
410 420 430 440 450
GNQPEDACEG DSGGPHITAY KDTHFLTGIV SWGEGCGRDG KYGIYTKVSN
460 470
FLPWIKTIMR RKQPSTESST GRL
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | DQ917518 mRNA Translation: ABK63547.1 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | DQ917518 mRNA Translation: ABK63547.1 |
3D structure databases
SMRi | A6MFK7 |
ModBasei | Search... |
Protein family/group databases
MEROPSi | S01.396 |
Family and domain databases
CDDi | cd00190, Tryp_SPc, 1 hit |
Gene3Di | 2.40.10.10, 2 hits 4.10.740.10, 1 hit |
InterProi | View protein in InterPro IPR017857, Coagulation_fac-like_Gla_dom IPR001881, EGF-like_Ca-bd_dom 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 IPR043504, Peptidase_S1_PA_chymotrypsin IPR001314, Peptidase_S1A IPR001254, Trypsin_dom IPR018114, TRYPSIN_HIS IPR033116, TRYPSIN_SER |
Pfami | View protein in Pfam PF00008, EGF, 1 hit PF00594, Gla, 1 hit PF00089, Trypsin, 1 hit |
PIRSFi | PIRSF001143, Factor_X, 1 hit |
PRINTSi | PR00722, CHYMOTRYPSIN PR00001, GLABLOOD |
SMARTi | View protein in SMART SM00181, EGF, 2 hits SM00179, EGF_CA, 1 hit SM00069, GLA, 1 hit SM00020, Tryp_SPc, 1 hit |
SUPFAMi | SSF50494, SSF50494, 1 hit SSF57630, SSF57630, 1 hit |
PROSITEi | View 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 |
MobiDBi | Search... |
Entry informationi
Entry namei | FAXD1_DEMVE | |
Accessioni | A6MFK7Primary (citable) accession number: A6MFK7 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | June 28, 2011 |
Last sequence update: | July 24, 2007 | |
Last modified: | February 23, 2022 | |
This is version 84 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Animal Toxin Annotation Program | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Direct protein sequencingDocuments
- Peptidase families
Classification of peptidase families and list of entries - SIMILARITY comments
Index of protein domains and families