ID FA5V_PSETE Reviewed; 1460 AA.
AC Q7SZN0;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 29-MAY-2013, entry version 54.
DE RecName: Full=Venom prothrombin activator pseutarin-C non-catalytic subunit;
DE Short=PCNS;
DE Short=vPA;
DE AltName: Full=Venom coagulation factor Va-like protein;
DE Contains:
DE RecName: Full=Pseutarin-C non-catalytic subunit heavy chain;
DE Contains:
DE RecName: Full=Pseutarin-C non-catalytic subunit light chain;
DE Flags: Precursor;
OS Pseudonaja textilis (Eastern brown snake).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Scleroglossa; Serpentes; Colubroidea;
OC Elapidae; Acanthophiinae; Pseudonaja.
OX NCBI_TaxID=8673;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 31-54; 58-124;
RP 141-160; 309-317; 331-340; 352-372; 378-392; 430-454; 477-499;
RP 507-530; 559-567; 821-840; 851-866; 868-886; 896-922; 926-949;
RP 968-996; 1037-1059; 1078-1089; 1119-1134; 1149-1175; 1266-1279;
RP 1327-1368; 1396-1405; 1413-1425; 1429-1435 AND 1443-1451, ABSENCE OF
RP GLYCOSYLATION AT ASN-385 AND ASN-1397, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND MASS SPECTROMETRY.
RC TISSUE=Venom, and Venom gland;
RX PubMed=12730119; DOI=10.1182/blood-2002-12-3839;
RA Rao V.S., Swarup S., Kini R.M.;
RT "The nonenzymatic subunit of pseutarin C, a prothrombin activator from
RT eastern brown snake (Pseudonaja textilis) venom, shows structural
RT similarity to mammalian coagulation factor V.";
RL Blood 102:1347-1354(2003).
RN [2]
RP PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Venom;
RX PubMed=12362232; DOI=10.1267/th02100611;
RA Rao V.S., Kini R.M.;
RT "Pseutarin C, a prothrombin activator from Pseudonaja textilis venom:
RT its structural and functional similarity to mammalian coagulation
RT factor Xa-Va complex.";
RL Thromb. Haemost. 88:611-619(2002).
RN [3]
RP NOMENCLATURE.
RX PubMed=11522026;
RA Manjunatha Kini R., Morita T., Rosing J.;
RT "Classification and nomenclature of prothrombin activators isolated
RT from snake venoms.";
RL Thromb. Haemost. 86:710-711(2001).
RN [4]
RP TISSUE SPECIFICITY.
RC TISSUE=Venom gland;
RX PubMed=15735790; DOI=10.1267/THRO05030420;
RA Minh Le T.N., Reza M.A., Swarup S., Kini R.M.;
RT "Gene duplication of coagulation factor V and origin of venom
RT prothrombin activator in Pseudonaja textilis snake.";
RL Thromb. Haemost. 93:420-429(2005).
CC -!- FUNCTION: Snake prothrombin activator that attacks the hemostatic
CC system of prey. This non-catalytic subunit is functionally similar
CC to blood coagulation factor V. It serves as a critical cofactor
CC for the prothrombinase activity of the catalytic subunit, which is
CC similar to the blood coagulation factor X.
CC -!- SUBUNIT: Heterodimer of a light and a heavy chains; non-disulfide-
CC linked. The interaction between the two chains is calcium-
CC dependent (By similarity). Found in its active form associated
CC with pseutarin-C catalytic subunit.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- PTM: In physiological conditions, blood coagulation factor V and
CC factor Va are inactivated by activated protein C (APC) through
CC proteolytic degradation of the heavy chain. However, pseutarin-C
CC non-catalytic subunit (factor V-like protein) retains its full
CC activity even at high concentration of APC. This has two
CC explanations: this protein has only one of the three cleavage
CC sites present in factor V that are targeted by the APC for
CC inactivation, and the binding with the catalytic subunit protect
CC the cleavage site from inactivation.
CC -!- MISCELLANEOUS: In contrast to blood coagulation factors that
CC circulate as inactive zymogen in plasma, venom prothrombin
CC activators are always found in the active form in the venom.
CC Hence, catalytic and non-catalytic subunits are found naturally in
CC venom as stable complexes.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC -!- SIMILARITY: Contains 3 F5/8 type A domains.
CC -!- SIMILARITY: Contains 2 F5/8 type C domains.
CC -!- SIMILARITY: Contains 6 plastocyanin-like domains.
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DR EMBL; AY168281; AAO38805.1; -; mRNA.
DR ProteinModelPortal; Q7SZN0; -.
DR SMR; Q7SZN0; 31-327, 1302-1460.
DR HOVERGEN; HBG005631; -.
DR GO; GO:0005576; C:extracellular region; IDA: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:0007155; P:cell adhesion; IEA:InterPro.
DR GO; GO:0044469; P:envenomation resulting in positive regulation of blood coagulation in other organism; IDA:UniProtKB.
DR GO; GO:0035807; P:positive regulation of blood coagulation in other organism; IDA:UniProtKB.
DR Gene3D; 2.60.120.260; -; 2.
DR Gene3D; 2.60.40.420; -; 6.
DR InterPro; IPR000421; Coagulation_fac_5/8-C_type_dom.
DR InterPro; IPR011707; Cu-oxidase_3.
DR InterPro; IPR002355; Cu_oxidase_Cu_BS.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR008979; Galactose-bd-like.
DR Pfam; PF07732; Cu-oxidase_3; 3.
DR Pfam; PF00754; F5_F8_type_C; 2.
DR SMART; SM00231; FA58C; 2.
DR SUPFAM; SSF49503; Cupredoxin; 6.
DR SUPFAM; SSF49785; Gal_bind_like; 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 1: Evidence at protein level;
KW Blood coagulation cascade activating toxin; Calcium;
KW Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Hemostasis impairing toxin; Metal-binding; Phosphoprotein;
KW Prothrombin activator; Repeat; Secreted; Signal; Toxin.
FT SIGNAL 1 30
FT CHAIN 31 772 Pseutarin-C non-catalytic subunit heavy
FT chain (Probable).
FT /FTId=PRO_5000089286.
FT PROPEP 773 818 Activation peptide (connecting region).
FT /FTId=PRO_0000408521.
FT CHAIN 819 1460 Pseutarin-C non-catalytic subunit light
FT chain.
FT /FTId=PRO_0000408522.
FT DOMAIN 32 330 F5/8 type A 1.
FT DOMAIN 32 196 Plastocyanin-like 1.
FT DOMAIN 206 330 Plastocyanin-like 2.
FT DOMAIN 351 685 F5/8 type A 2.
FT DOMAIN 351 529 Plastocyanin-like 3.
FT DOMAIN 539 685 Plastocyanin-like 4.
FT DOMAIN 824 1143 F5/8 type A 3.
FT DOMAIN 824 992 Plastocyanin-like 5.
FT DOMAIN 1001 1143 Plastocyanin-like 6.
FT DOMAIN 1147 1298 F5/8 type C 1.
FT DOMAIN 1303 1457 F5/8 type C 2.
FT REGION 693 818 B.
FT COMPBIAS 695 699 Poly-Glu.
FT METAL 142 142 Calcium (By similarity).
FT METAL 143 143 Calcium (By similarity).
FT SITE 385 385 Not glycosylated.
FT SITE 537 538 Cleavage; by activated protein C (By
FT similarity).
FT SITE 772 773 Cleavage; by thrombin (By similarity).
FT SITE 818 819 Cleavage; by thrombin (By similarity).
FT SITE 1397 1397 Not glycosylated.
FT CARBOHYD 156 156 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 204 204 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 242 242 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 406 406 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 471 471 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 557 557 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 944 944 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 1001 1001 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 1180 1180 N-linked (GlcNAc...) (Potential).
FT DISULFID 170 196 By similarity.
FT DISULFID 251 332 By similarity.
FT DISULFID 503 529 By similarity.
FT DISULFID 966 992 Probable.
FT DISULFID 1147 1298 By similarity.
FT DISULFID 1303 1457 By similarity.
FT CONFLICT 80 82 EPR -> KPQ (in Ref. 1; AA sequence).
FT CONFLICT 103 103 I -> Q (in Ref. 1; AA sequence).
FT CONFLICT 119 124 SAVYNK -> DAVKIG (in Ref. 1; AA
FT sequence).
FT CONFLICT 146 146 P -> A (in Ref. 1; AA sequence).
FT CONFLICT 156 156 N -> E (in Ref. 1; AA sequence).
FT CONFLICT 350 363 IKNWEYFIAAEEIT -> AQLWEYHIAAQKED (in Ref.
FT 1; AA sequence).
FT CONFLICT 440 444 NLASR -> DLAVQ (in Ref. 1; AA sequence).
FT CONFLICT 522 523 LI -> IL (in Ref. 1; AA sequence).
FT CONFLICT 820 827 INRGNKRR -> QNTGNKLY (in Ref. 1; AA
FT sequence).
FT CONFLICT 840 840 S -> I (in Ref. 1; AA sequence).
FT CONFLICT 876 876 G -> GK (in Ref. 1; AA sequence).
FT CONFLICT 902 902 K -> R (in Ref. 1; AA sequence).
FT CONFLICT 944 944 N -> F (in Ref. 1; AA sequence).
FT CONFLICT 981 995 IHSGLIGPILICQKG -> VEPGLIGPLYSIAEEAV (in
FT Ref. 1; AA sequence).
FT CONFLICT 1041 1043 SLH -> NLG (in Ref. 1; AA sequence).
FT CONFLICT 1055 1058 LQGL -> GK (in Ref. 1; AA sequence).
FT CONFLICT 1166 1170 SGHVG -> AGHVQ (in Ref. 1; AA sequence).
FT CONFLICT 1274 1274 I -> V (in Ref. 1; AA sequence).
FT CONFLICT 1369 1369 I -> K (in Ref. 1; AA sequence).
FT CONFLICT 1400 1404 WKPYL -> YKPYG (in Ref. 1; AA sequence).
FT CONFLICT 1433 1434 LS -> SL (in Ref. 1; AA sequence).
SQ SEQUENCE 1460 AA; 165932 MW; 6AFB63E2D5D275A6 CRC64;
MGRYSVSPVP KCLLLMFLGW SGLKYYQVNA AQLREYHIAA QLEDWDYNPQ PEELSRLSES
DLTFKKIVYR EYELDFKQEE PRDALSGLLG PTLRGEVGDS LIIYFKNFAT QPVSIHPQSA
VYNKWSEGSS YSDGTSDVER LDDAVPPGQS FKYVWNITAE IGPKKADPPC LTYAYYSHVN
MVRDFNSGLI GALLICKEGS LNANGSQKFF NREYVLMFSV FDESKNWYRK PSLQYTINGF
ANGTLPDVQA CAYDHISWHL IGMSSSPEIF SVHFNGQTLE QNHYKVSTIN LVGGASVTAD
MSVSRTGKWL ISSLVAKHLQ AGMYGYLNIK DCGNPDTLTR KLSFRELMKI KNWEYFIAAE
EITWDYAPEI PSSVDRRYKA QYLDNFSNFI GKKYKKAVFR QYEDGNFTKP TYAIWPKERG
ILGPVIKAKV RDTVTIVFKN LASRPYSIYV HGVSVSKDAE GAIYPSDPKE NITHGKAVEP
GQVYTYKWTV LDTDEPTVKD SECITKLYHS AVDMTRDIAS GLIGPLLVCK HKALSVKGVQ
NKADVEQHAV FAVFDENKSW YLEDNIKKYC SNPSAVKKDD PKFYKSNVMY TLNGYASDRT
EVLRFHQSEV VQWHLTSVGT VDEIVPVHLS GHTFLSKGKH QDILNLFPMS GESATVTMDN
LGTWLLSSWG SCEMSNGMRL RFLDANYDDE DEGNEEEEED DGDIFADIFI PSEVVKKKEE
VPVNFVPDPE SDALAKELGL IDDEGNPIIQ PRREQTEDDE EQLMKASMLG LRSFKGSVAE
EELKHTALAL EEDAHASDPR IDSNSARNPD DIAGRYLRTI NRGNKRRYYI AAEEVLWDYS
PIGKSQVRSR AAKTTFKKAI FRSYLDDTFQ TPSTGGEYEK HLGILGPIIR AEVDDVIEIQ
FKNLASRPYS LHAHGLLYEK SSEGRSYDDK SPELFKKDDA IMPNGTYTYV WQVPPRSGPT
DNTEKCKSWA YYSGVNPEKD IHSGLIGPIL ICQKGMIDKY NRTIDIREFV LFFMVFDEEK
SWYFPKSDKS TCEEKLIGVQ SLHTFPAING IPYQLQGLTM YKDENVHWHL LNMGGPKDIH
VVNFHGQTFT EEGREDNQLG VLPLLPGTFA SIKMKPSKIG TWLLETEVGE NQERGMQALF
TVIDKDCKLP MGLASGIIQD SQISASGHVG YWEPKLARLN NTGKYNAWSI IKKEHEHPWI
QIDLQRQVVI TGIQTQGTVQ LLQHSYTVEY FVTYSEDGQN WITFKGRHSE TQMHFEGNSD
GTTVKENHID PPIIARYIRL HPTKFYNRPT FRIELLGCEV EGCSVPLGME SGAIKNSEIT
ASSYKKTWWS SWEPSLARLN LEGGTNAWQP EVNNKDQWLQ IDLQHLTKIT SIITQGATSM
TTSMYVKTFS IHYTDDNSTW KPYLDVRTSM EKVFTGNINS DGHVKHFFKP PILSRFIRII
PKTWNQYIAL RIELFGCEVF
//
