FA5V_OXYMI
ID FA5V_OXYMI Reviewed; 1460 AA.
AC Q58L90;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Venom prothrombin activator omicarin-C non-catalytic subunit;
DE Short=vPA;
DE AltName: Full=Venom coagulation factor Va-like protein;
DE Contains:
DE RecName: Full=Omicarin-C non-catalytic subunit heavy chain;
DE Contains:
DE RecName: Full=Omicarin-C non-catalytic subunit light chain;
DE Flags: Precursor;
OS Oxyuranus microlepidotus (Inland taipan) (Diemenia microlepidota).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Acanthophiinae; Oxyuranus.
OX NCBI_TaxID=111177;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=15930152; DOI=10.1093/molbev/msi181;
RA St Pierre L., Masci P.P., Filippovich I., Sorokina N., Marsh N.,
RA Miller D.J., Lavin M.F.;
RT "Comparative analysis of prothrombin activators from the venom of
RT Australian elapids.";
RL Mol. Biol. Evol. 22:1853-1864(2005).
RN [2]
RP NOMENCLATURE.
RX PubMed=11522026;
RA Manjunatha Kini R., Morita T., Rosing J.;
RT "Classification and nomenclature of prothrombin activators isolated from
RT snake venoms.";
RL Thromb. Haemost. 86:710-711(2001).
CC -!- FUNCTION: Snake prothrombin activator that attacks the hemostatic
CC system of prey. This non-catalytic subunit is functionally similar to
CC blood coagulation factor V. It serves as a critical cofactor for the
CC prothrombinase activity of the catalytic subunit, which is similar to
CC the blood coagulation factor X. The complex converts prothrombin to
CC thrombin by sequential cleavage at two positions, Arg-320 followed by
CC Arg-271. Cleavage at Arg-320 produces an active intermediate known as
CC meizothrombin. Meizothrombin is the 'second' substrate for
CC prothrombinase, and it docks in an altered manner to present the second
CC cleavage site (271). Cleavage at Arg-271 releases active thrombin from
CC its pro-fragment. This order of events is reversed if the protease
CC component of prothrombinase is used on its own, suggesting that the 271
CC site is inherently more accessible to proteolysis.
CC {ECO:0000250|UniProtKB:Q7SZN0}.
CC -!- SUBUNIT: Heterodimer of a light and a heavy chains; non-disulfide-
CC linked. The interaction between the two chains is calcium-dependent.
CC Found in its active form associated with omicarin-C catalytic subunit
CC (AC Q58L95) (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- PTM: In physiological conditions, blood coagulation factor V and factor
CC Va are inactivated by activated protein C (APC) through proteolytic
CC degradation of the heavy chain. However, omicarin-C non-catalytic
CC subunit (factor V-like protein) retains its full activity even at high
CC concentration of APC. This has two explanations: this protein has only
CC one of the three cleavage sites present in factor V that are targeted
CC by the APC for inactivation, and the binding with the catalytic subunit
CC protect the cleavage site from inactivation (By similarity).
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: In contrast to blood coagulation factors that circulate
CC as inactive zymogen in plasma, venom prothrombin activators are always
CC found in the active form in the venom. Hence, catalytic and non-
CC catalytic subunits are found naturally in venom as stable complexes.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
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DR EMBL; AY940210; AAX37266.1; -; mRNA.
DR AlphaFoldDB; Q58L90; -.
DR SMR; Q58L90; -.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016504; F:peptidase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0044469; P:envenomation resulting in positive regulation of blood coagulation in another organism; ISS:UniProtKB.
DR GO; GO:0035807; P:positive regulation of blood coagulation in another organism; ISS:UniProtKB.
DR CDD; cd00057; FA58C; 2.
DR Gene3D; 2.60.40.420; -; 5.
DR InterPro; IPR011707; Cu-oxidase_N.
DR InterPro; IPR033138; Cu_oxidase_CS.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR024715; Factor_5/8-like.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR Pfam; PF07732; Cu-oxidase_3; 3.
DR Pfam; PF00754; F5_F8_type_C; 2.
DR PIRSF; PIRSF000354; Factors_V_VIII; 1.
DR SMART; SM00231; FA58C; 2.
DR SUPFAM; SSF49503; SSF49503; 6.
DR SUPFAM; SSF49785; SSF49785; 2.
DR PROSITE; PS01285; FA58C_1; 2.
DR PROSITE; PS01286; FA58C_2; 1.
DR PROSITE; PS50022; FA58C_3; 2.
DR PROSITE; PS00079; MULTICOPPER_OXIDASE1; 3.
PE 2: Evidence at transcript level;
KW Blood coagulation cascade activating toxin; Calcium; Disulfide bond;
KW Glycoprotein; Hemostasis impairing toxin; Metal-binding;
KW Prothrombin activator; Repeat; Secreted; Signal; Toxin.
FT SIGNAL 1..30
FT /evidence="ECO:0000250"
FT CHAIN 31..771
FT /note="Omicarin-C non-catalytic subunit heavy chain"
FT /id="PRO_0000409904"
FT PROPEP 772..817
FT /note="Activation peptide (connecting region)"
FT /evidence="ECO:0000250"
FT /id="PRO_0000409905"
FT CHAIN 818..1460
FT /note="Omicarin-C non-catalytic subunit light chain"
FT /id="PRO_0000409906"
FT DOMAIN 32..330
FT /note="F5/8 type A 1"
FT DOMAIN 32..196
FT /note="Plastocyanin-like 1"
FT DOMAIN 206..330
FT /note="Plastocyanin-like 2"
FT DOMAIN 350..685
FT /note="F5/8 type A 2"
FT DOMAIN 351..529
FT /note="Plastocyanin-like 3"
FT DOMAIN 539..685
FT /note="Plastocyanin-like 4"
FT DOMAIN 823..1143
FT /note="F5/8 type A 3"
FT DOMAIN 823..991
FT /note="Plastocyanin-like 5"
FT DOMAIN 1000..1143
FT /note="Plastocyanin-like 6"
FT DOMAIN 1147..1298
FT /note="F5/8 type C 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT DOMAIN 1303..1457
FT /note="F5/8 type C 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT REGION 693..817
FT /note="B"
FT REGION 740..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 124
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7SZN0"
FT BINDING 139
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7SZN0"
FT BINDING 142
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7SZN0"
FT BINDING 143
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7SZN0"
FT BINDING 919
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q7SZN0"
FT BINDING 934
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q7SZN0"
FT BINDING 937
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q7SZN0"
FT BINDING 938
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q7SZN0"
FT SITE 771..772
FT /note="Cleavage; by thrombin"
FT /evidence="ECO:0000250"
FT SITE 817..818
FT /note="Cleavage; by thrombin"
FT /evidence="ECO:0000250"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 385
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 471
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 557
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 943
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1000
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1397
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 170..196
FT /evidence="ECO:0000250|UniProtKB:Q7SZN0"
FT DISULFID 251..332
FT /evidence="ECO:0000250|UniProtKB:Q7SZN0"
FT DISULFID 503..529
FT /evidence="ECO:0000250|UniProtKB:Q7SZN0"
FT DISULFID 672..1031
FT /evidence="ECO:0000250|UniProtKB:Q7SZN0"
FT DISULFID 965..991
FT /evidence="ECO:0000250|UniProtKB:Q7SZN0"
FT DISULFID 1147..1298
FT /evidence="ECO:0000250|UniProtKB:Q7SZN0"
FT DISULFID 1303..1457
FT /evidence="ECO:0000250|UniProtKB:Q7SZN0"
SQ SEQUENCE 1460 AA; 166082 MW; F7BCEC4838695087 CRC64;
MGRYSVSPVP KCLLLMFLGW SGLKYYQVNA AQLREYRIAA QLEDWDYNPQ PEELSRLSES
ELTFKKIVYR EYELDFKQEK PRDELSGLLG PTLRGEVGDI LIIYFKNFAT QPVSIHPQSA
VYNKWSEGSS YSDGTSDVER LDDAVPPGQS FKYVWNITAE IGPKKADPPC LTYAYYSHVN
MVRDFNSGLI GALLICKEGS LNANGAQKFF NREYVLMFSV FDESKNWYRK PSLQYTINGF
ANGTLPDVQA CAYDHISWHL IGMSSSPEIF SVHFNGQTLE QNHYKVSTIN LVGGASVTAN
MSVSRTGKWL ISSLVAKHLQ AGMYGYLNIK DCGHPNTLTR KLSFRELRRI MNWEYFIAAE
EITWDYAPEI PSSVDRRYKA QYLDNFSNFI GKKYKKAVFR QYEDGNFTKP TYAIWPKERG
ILGPVIKAKV RDTVTIVFKN LASRPYSIYV HGVSVSKDAE GAIYPSDPKE NITHGKAVEP
GQVYTYKWTV LDTDEPTVKD SECITKLYHS AVDMTRDIAS GLIGPLLVCK LKALSVKGVQ
NKADVEQHAV FAVFDENKSW YLEDNIKKYC SNPSSVKKDD PKFYKSNVMY TLNGYASDRT
EVLGFHQSEV VQWHLTSVGT VDEIVPVHLS GHTFLSKGKH QDILNLFPMS GESATVTMDN
LGTWLLSSWG SCEMSNGMRL RFLDANYDDE DEGNEEEEED DGDIFADIFS PPEVVKKKEE
VPVNFVPDPE SDALAKELGL LDDEDNPEQS RSEQTEDDEE QLMIASVLGL RSFKGSVAEE
ELKHTALALE EDAHASDPRI DSNSARNSDD IAGRYLRTIN RRNKRRYYIA AEEVLWDYSP
IGKSQVRSLP AKTTFKKAIF RSYLDDTFQT PSTGGEYEKH LGILGPIIRA EVDDVIEVQF
RNLASRPYSL HAHGLLYEKS SEGRSYDDNS PELFKKDDAI MPNGTYTYVW QVPPRSGPTD
NTEKCKSWAY YSGVNPEKDI HSGLIGPILI CQKGMIDKYN RTIDIREFVL FFMVFDEEKS
WYFPKSDKST CEEKLIGVQS SHHTFPAING IPYQLQGLMM YKDENVHWHL LNMGGPKDIH
VVNFHGQTFT EEGREDNQLG VLPLLPGTFA SIKMKPSKIG TWLLETEVGE NQERGMQALF
TVIDKDCKLP MGLASGIIQD SQISASGHVE YWEPKLARLN NTGMFNAWSI IKKEHEHPWI
QIDLQRQVVI TGIQTQGTVQ LLKHSYTVEY FVTYSKDGQN WITFKGRHSE TQMHFEGNSD
GTTVKENHID PPIIARYIRL HPTKFYNTPT FRIELLGCEV EGCSVPLGME SGAIKNSEIT
ASSYKKTWWS SWEPFLARLN LEGGTNAWQP EVNNKDQWLQ IDLQHLTKIT SIITQGATSM
TTAMYVKTFS IHYTDDNSTW KPYLDVRTSM EKVFTGNINS DGHVKHFFKP PILSRFIRII
PKTWNQYIAL RIELFGCEVF
