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Protein

Venom prothrombin activator omicarin-C non-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 non-catalytic subunit is functionally similar to blood coagulation factor V. It serves as a critical cofactor for the prothrombinase activity of the catalytic subunit, which is similar to the blood coagulation factor X (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi142CalciumBy similarity1
Metal bindingi143CalciumBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Blood coagulation cascade activating toxin, Hemostasis impairing toxin, Prothrombin activator, Toxin

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Venom prothrombin activator omicarin-C non-catalytic subunit
Short name:
vPA
Alternative name(s):
Venom coagulation factor Va-like protein
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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 30By similarityAdd BLAST30
ChainiPRO_000040990431 – 771Omicarin-C non-catalytic subunit heavy chainAdd BLAST741
PropeptideiPRO_0000409905772 – 817Activation peptide (connecting region)By similarityAdd BLAST46
ChainiPRO_0000409906818 – 1460Omicarin-C non-catalytic subunit light chainAdd BLAST643

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi156N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi170 ↔ 196PROSITE-ProRule annotation
Glycosylationi242N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi251 ↔ 332PROSITE-ProRule annotation
Glycosylationi300N-linked (GlcNAc...)Sequence analysis1
Glycosylationi385N-linked (GlcNAc...)Sequence analysis1
Glycosylationi406N-linked (GlcNAc...)Sequence analysis1
Glycosylationi471N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi503 ↔ 529PROSITE-ProRule annotation
Glycosylationi557N-linked (GlcNAc...)Sequence analysis1
Glycosylationi943N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi965 ↔ 991PROSITE-ProRule annotation
Glycosylationi1000N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1147 ↔ 1298PROSITE-ProRule annotation
Glycosylationi1180N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1303 ↔ 1457PROSITE-ProRule annotation
Glycosylationi1397N-linked (GlcNAc...)Sequence analysis1

Post-translational modificationi

In physiological conditions, blood coagulation factor V and factor Va are inactivated by activated protein C (APC) through proteolytic degradation of the heavy chain. However, omicarin-C non-catalytic subunit (factor V-like protein) retains its full activity even at high concentration of APC. This has two explanations: this protein has only one of the three cleavage sites present in factor V that are targeted by the APC for inactivation, and the binding with the catalytic subunit protect the cleavage site from inactivation (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei537 – 538Cleavage; by activated protein CBy similarity2
Sitei771 – 772Cleavage; by thrombinBy similarity2
Sitei817 – 818Cleavage; by thrombinBy similarity2

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Expressioni

Tissue specificityi

Expressed by the venom gland.

Interactioni

Subunit structurei

Heterodimer of a light and a heavy chains; non-disulfide-linked. The interaction between the two chains is calcium-dependent. Found in its active form associated with omicarin-C catalytic subunit (AC Q58L95) (By similarity).By similarity

Structurei

3D structure databases

ProteinModelPortaliQ58L90.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini32 – 330F5/8 type A 1Add BLAST299
Domaini32 – 196Plastocyanin-like 1Add BLAST165
Domaini206 – 330Plastocyanin-like 2Add BLAST125
Domaini350 – 685F5/8 type A 2Add BLAST336
Domaini351 – 529Plastocyanin-like 3Add BLAST179
Domaini539 – 685Plastocyanin-like 4Add BLAST147
Domaini823 – 1143F5/8 type A 3Add BLAST321
Domaini823 – 991Plastocyanin-like 5Add BLAST169
Domaini1000 – 1143Plastocyanin-like 6Add BLAST144
Domaini1147 – 1298F5/8 type C 1PROSITE-ProRule annotationAdd BLAST152
Domaini1303 – 1457F5/8 type C 2PROSITE-ProRule annotationAdd BLAST155

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni693 – 817BAdd BLAST125

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi695 – 699Poly-Glu5

Sequence similaritiesi

Belongs to the multicopper oxidase family.Curated
Contains 3 F5/8 type A domains.Curated
Contains 2 F5/8 type C domains.PROSITE-ProRule annotation
Contains 6 plastocyanin-like domains.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

HOVERGENiHBG005631.

Family and domain databases

Gene3Di2.60.120.260. 2 hits.
2.60.40.420. 6 hits.
InterProiIPR011707. Cu-oxidase_3.
IPR033138. Cu_oxidase_CS.
IPR008972. Cupredoxin.
IPR000421. FA58C.
IPR029821. Factor_V.
IPR008979. Galactose-bd-like.
[Graphical view]
PANTHERiPTHR10127:SF597. PTHR10127:SF597. 3 hits.
PfamiPF07732. Cu-oxidase_3. 3 hits.
PF00754. F5_F8_type_C. 2 hits.
[Graphical view]
SMARTiSM00231. FA58C. 2 hits.
[Graphical view]
SUPFAMiSSF49503. SSF49503. 6 hits.
SSF49785. SSF49785. 2 hits.
PROSITEiPS01285. FA58C_1. 2 hits.
PS01286. FA58C_2. 1 hit.
PS50022. FA58C_3. 2 hits.
PS00079. MULTICOPPER_OXIDASE1. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q58L90-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGRYSVSPVP KCLLLMFLGW SGLKYYQVNA AQLREYRIAA QLEDWDYNPQ
60 70 80 90 100
PEELSRLSES ELTFKKIVYR EYELDFKQEK PRDELSGLLG PTLRGEVGDI
110 120 130 140 150
LIIYFKNFAT QPVSIHPQSA VYNKWSEGSS YSDGTSDVER LDDAVPPGQS
160 170 180 190 200
FKYVWNITAE IGPKKADPPC LTYAYYSHVN MVRDFNSGLI GALLICKEGS
210 220 230 240 250
LNANGAQKFF NREYVLMFSV FDESKNWYRK PSLQYTINGF ANGTLPDVQA
260 270 280 290 300
CAYDHISWHL IGMSSSPEIF SVHFNGQTLE QNHYKVSTIN LVGGASVTAN
310 320 330 340 350
MSVSRTGKWL ISSLVAKHLQ AGMYGYLNIK DCGHPNTLTR KLSFRELRRI
360 370 380 390 400
MNWEYFIAAE EITWDYAPEI PSSVDRRYKA QYLDNFSNFI GKKYKKAVFR
410 420 430 440 450
QYEDGNFTKP TYAIWPKERG ILGPVIKAKV RDTVTIVFKN LASRPYSIYV
460 470 480 490 500
HGVSVSKDAE GAIYPSDPKE NITHGKAVEP GQVYTYKWTV LDTDEPTVKD
510 520 530 540 550
SECITKLYHS AVDMTRDIAS GLIGPLLVCK LKALSVKGVQ NKADVEQHAV
560 570 580 590 600
FAVFDENKSW YLEDNIKKYC SNPSSVKKDD PKFYKSNVMY TLNGYASDRT
610 620 630 640 650
EVLGFHQSEV VQWHLTSVGT VDEIVPVHLS GHTFLSKGKH QDILNLFPMS
660 670 680 690 700
GESATVTMDN LGTWLLSSWG SCEMSNGMRL RFLDANYDDE DEGNEEEEED
710 720 730 740 750
DGDIFADIFS PPEVVKKKEE VPVNFVPDPE SDALAKELGL LDDEDNPEQS
760 770 780 790 800
RSEQTEDDEE QLMIASVLGL RSFKGSVAEE ELKHTALALE EDAHASDPRI
810 820 830 840 850
DSNSARNSDD IAGRYLRTIN RRNKRRYYIA AEEVLWDYSP IGKSQVRSLP
860 870 880 890 900
AKTTFKKAIF RSYLDDTFQT PSTGGEYEKH LGILGPIIRA EVDDVIEVQF
910 920 930 940 950
RNLASRPYSL HAHGLLYEKS SEGRSYDDNS PELFKKDDAI MPNGTYTYVW
960 970 980 990 1000
QVPPRSGPTD NTEKCKSWAY YSGVNPEKDI HSGLIGPILI CQKGMIDKYN
1010 1020 1030 1040 1050
RTIDIREFVL FFMVFDEEKS WYFPKSDKST CEEKLIGVQS SHHTFPAING
1060 1070 1080 1090 1100
IPYQLQGLMM YKDENVHWHL LNMGGPKDIH VVNFHGQTFT EEGREDNQLG
1110 1120 1130 1140 1150
VLPLLPGTFA SIKMKPSKIG TWLLETEVGE NQERGMQALF TVIDKDCKLP
1160 1170 1180 1190 1200
MGLASGIIQD SQISASGHVE YWEPKLARLN NTGMFNAWSI IKKEHEHPWI
1210 1220 1230 1240 1250
QIDLQRQVVI TGIQTQGTVQ LLKHSYTVEY FVTYSKDGQN WITFKGRHSE
1260 1270 1280 1290 1300
TQMHFEGNSD GTTVKENHID PPIIARYIRL HPTKFYNTPT FRIELLGCEV
1310 1320 1330 1340 1350
EGCSVPLGME SGAIKNSEIT ASSYKKTWWS SWEPFLARLN LEGGTNAWQP
1360 1370 1380 1390 1400
EVNNKDQWLQ IDLQHLTKIT SIITQGATSM TTAMYVKTFS IHYTDDNSTW
1410 1420 1430 1440 1450
KPYLDVRTSM EKVFTGNINS DGHVKHFFKP PILSRFIRII PKTWNQYIAL
1460
RIELFGCEVF
Length:1,460
Mass (Da):166,082
Last modified:April 26, 2005 - v1
Checksum:iF7BCEC4838695087
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY940210 mRNA. Translation: AAX37266.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY940210 mRNA. Translation: AAX37266.1.

3D structure databases

ProteinModelPortaliQ58L90.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG005631.

Family and domain databases

Gene3Di2.60.120.260. 2 hits.
2.60.40.420. 6 hits.
InterProiIPR011707. Cu-oxidase_3.
IPR033138. Cu_oxidase_CS.
IPR008972. Cupredoxin.
IPR000421. FA58C.
IPR029821. Factor_V.
IPR008979. Galactose-bd-like.
[Graphical view]
PANTHERiPTHR10127:SF597. PTHR10127:SF597. 3 hits.
PfamiPF07732. Cu-oxidase_3. 3 hits.
PF00754. F5_F8_type_C. 2 hits.
[Graphical view]
SMARTiSM00231. FA58C. 2 hits.
[Graphical view]
SUPFAMiSSF49503. SSF49503. 6 hits.
SSF49785. SSF49785. 2 hits.
PROSITEiPS01285. FA58C_1. 2 hits.
PS01286. FA58C_2. 1 hit.
PS50022. FA58C_3. 2 hits.
PS00079. MULTICOPPER_OXIDASE1. 3 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFA5V_OXYMI
AccessioniPrimary (citable) accession number: Q58L90
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 28, 2011
Last sequence update: April 26, 2005
Last modified: October 5, 2016
This is version 58 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

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. 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.