LOPAP_LONON
ID LOPAP_LONON Reviewed; 201 AA.
AC Q5ECE3; Q5MGF3; Q5MGH7;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Lopap;
DE EC=3.4.21.-;
DE AltName: Full=Lipocalin-1/4;
DE AltName: Full=Prothrombin activator;
DE Flags: Precursor;
OS Lonomia obliqua (Moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Saturniidae; Hemileucinae; Lonomia.
OX NCBI_TaxID=304329;
RN [1] {ECO:0000312|EMBL:AAV91447.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Larval bristle {ECO:0000312|EMBL:AAV91447.1}, and
RC Tegument {ECO:0000312|EMBL:AAV91423.1};
RX PubMed=16023793; DOI=10.1016/j.gene.2005.05.002;
RA Veiga A.B.G., Ribeiro J.M.C., Guimaraes J.A., Francischetti I.M.B.;
RT "A catalog for the transcripts from the venomous structures of the
RT caterpillar Lonomia obliqua: identification of the proteins potentially
RT involved in the coagulation disorder and hemorrhagic syndrome.";
RL Gene 355:11-27(2005).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAW88441.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 21-62; 72-78; 172-189 AND
RP 191-201, FUNCTION, ACTIVITY REGULATION, AND SUBUNIT.
RC TISSUE=Larval bristle {ECO:0000269|PubMed:16734589};
RX PubMed=16734589; DOI=10.1042/bj20060325;
RA Reis C.V., Andrade S.A., Ramos O.H.P., Ramos C.R.R., Ho P.L.,
RA Batista I.F.C., Chudzinski-Tavassi A.M.;
RT "Lopap, a prothrombin activator from Lonomia obliqua belonging to the
RT lipocalin family: recombinant production, biochemical characterization and
RT structure-function insights.";
RL Biochem. J. 398:295-302(2006).
RN [3] {ECO:0000305}
RP PROTEIN SEQUENCE OF 17-62; 72-79; 136-151; 172-189 AND 191-201, FUNCTION,
RP ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Larval bristle {ECO:0000269|PubMed:11395128};
RX PubMed=11395128; DOI=10.1016/s0049-3848(01)00265-1;
RA Reis C.V., Portaro F.C.V., Andrade S.A., Fritzen M., Fernandes B.L.,
RA Sampaio C.A.M., Camargo A.C.M., Chudzinski-Tavassi A.M.;
RT "A prothrombin activator serine protease from the Lonomia obliqua
RT caterpillar venom (Lopap) biochemical characterization.";
RL Thromb. Res. 102:427-436(2001).
RN [4] {ECO:0000305}
RP PROTEIN SEQUENCE OF 17-28; 33-46; 74-132; 142-149 AND 177-185.
RC TISSUE=Larval bristle {ECO:0000269|PubMed:18342903};
RX PubMed=18342903; DOI=10.1016/j.toxicon.2008.01.013;
RA Ricci-Silva M.E., Valente R.H., Leon I.R., Tambourgi D.V., Ramos O.H.P.,
RA Perales J., Chudzinski-Tavassi A.M.;
RT "Immunochemical and proteomic technologies as tools for unravelling toxins
RT involved in envenoming by accidental contact with Lonomia obliqua
RT caterpillars.";
RL Toxicon 51:1017-1028(2008).
RN [5] {ECO:0000305}
RP FUNCTION.
RX PubMed=11910193; DOI=10.1159/000048071;
RA Chudzinski-Tavassi A.M., Schattner M., Fritzen M., Pozner R.G., Reis C.V.,
RA Lourenco D., Lazzari M.A.;
RT "Effects of lopap on human endothelial cells and platelets.";
RL Haemostasis 31:257-265(2001).
RN [6] {ECO:0000305}
RP FUNCTION.
RX PubMed=11395129; DOI=10.1016/s0049-3848(01)00268-7;
RA Reis C.V., Farsky S.H.P., Fernandes B.L., Santoro M.L., Oliva M.L.V.,
RA Mariano M., Chudzinski-Tavassi A.M.;
RT "In vivo characterization of Lopap, a prothrombin activator serine protease
RT from the Lonomia obliqua caterpillar venom.";
RL Thromb. Res. 102:437-443(2001).
RN [7] {ECO:0000305}
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=15963468; DOI=10.1016/j.bbrc.2005.05.140;
RA Fritzen M., Flores M.P.A., Reis C.V., Chudzinski-Tavassi A.M.;
RT "A prothrombin activator (Lopap) modulating inflammation, coagulation and
RT cell survival mechanisms.";
RL Biochem. Biophys. Res. Commun. 333:517-523(2005).
CC -!- FUNCTION: Serine protease. Activates thrombin by cleavage of
CC prothrombin. Does not activate factor X. When injected into rats,
CC causes thrombus formation, fibrinogen depletion, uncoagulable blood,
CC decreased platelet count, inhibition of collagen-induced platelet
CC aggregation, leukocyte infiltration in lungs, congestion and hemorrhage
CC in renal glomeruli and necrosis in renal distal tubules. Causes
CC increase in surface expression of ICAM-1 and E-selectin on human
CC umbilical vein endothelial cells (HUVEC), but does not affect
CC expression of VCAM-1, or the expression of mediators involved in
CC coagulation and fibrinolysis systems (TF, vWF and t-PA). Increases
CC expression of the platelet activation inhibitors NO and PGI2. Increases
CC viability of HUVEC, and inhibits apoptosis.
CC {ECO:0000269|PubMed:11395128, ECO:0000269|PubMed:11395129,
CC ECO:0000269|PubMed:11910193, ECO:0000269|PubMed:15963468,
CC ECO:0000269|PubMed:16734589}.
CC -!- ACTIVITY REGULATION: Activated by calcium ions. Inhibited by EDTA,
CC activity is recovered by the addition of calcium ions, but not
CC magnesium or zinc ions. Inhibited by PMSF.
CC {ECO:0000269|PubMed:11395128, ECO:0000269|PubMed:16734589}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.5 uM for Abz-YQTFFNPRTGSQ-EDDnp {ECO:0000269|PubMed:11395128};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:16734589}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Larval bristle. {ECO:0000269|PubMed:11395128,
CC ECO:0000269|PubMed:11395129}.
CC -!- DEVELOPMENTAL STAGE: Eggs and larvae. {ECO:0000269|PubMed:15963468}.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC {ECO:0000305}.
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DR EMBL; AY829809; AAV91423.1; -; mRNA.
DR EMBL; AY829833; AAV91447.1; -; mRNA.
DR EMBL; AY908986; AAW88441.1; -; mRNA.
DR AlphaFoldDB; Q5ECE3; -.
DR SMR; Q5ECE3; -.
DR BRENDA; 3.4.21.60; 8181.
DR SABIO-RK; Q5ECE3; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016504; F:peptidase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0031409; F:pigment binding; IEA:InterPro.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.40.128.20; -; 1.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR003057; Invtbrt_color.
DR InterPro; IPR022271; Lipocalin_ApoD.
DR InterPro; IPR022272; Lipocalin_CS.
DR InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR Pfam; PF00061; Lipocalin; 1.
DR PIRSF; PIRSF036893; Lipocalin_ApoD; 1.
DR PRINTS; PR01273; INVTBRTCOLOR.
DR SUPFAM; SSF50814; SSF50814; 1.
DR PROSITE; PS00213; LIPOCALIN; 1.
PE 1: Evidence at protein level;
KW Blood coagulation cascade activating toxin; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Hemostasis impairing toxin; Hydrolase;
KW Protease; Prothrombin activator; Secreted; Serine protease; Signal; Toxin.
FT SIGNAL 1..16
FT /evidence="ECO:0000269|PubMed:11395128,
FT ECO:0000269|PubMed:18342903"
FT CHAIN 17..201
FT /note="Lopap"
FT /evidence="ECO:0000269|PubMed:11395128"
FT /id="PRO_0000296384"
FT CARBOHYD 154
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 24..131
FT /evidence="ECO:0000250|UniProtKB:P09464"
FT DISULFID 58..187
FT /evidence="ECO:0000250|UniProtKB:P09464"
FT CONFLICT 4..8
FT /note="FGLFL -> MGRA (in Ref. 1; AAV91423)"
FT /evidence="ECO:0000305"
FT CONFLICT 35
FT /note="M -> I (in Ref. 1; AAV91423)"
FT /evidence="ECO:0000305"
FT CONFLICT 73
FT /note="R -> G (in Ref. 1; AAV91423)"
FT /evidence="ECO:0000305"
FT CONFLICT 79
FT /note="D -> N (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 94
FT /note="G -> D (in Ref. 2; AAW88441)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="W -> R (in Ref. 1; AAV91423)"
FT /evidence="ECO:0000305"
FT CONFLICT 118
FT /note="V -> L (in Ref. 2; AAW88441)"
FT /evidence="ECO:0000305"
FT CONFLICT 139
FT /note="Q -> A (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 154..156
FT /note="NES -> TET (in Ref. 1; AAV91447)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 201 AA; 22432 MW; 28B7623E0AD258C7 CRC64;
MKFFGLFLAI LASTAADVVI DGACPDMKAV SKFDMNAYQG TWYEIKKFPV ANEANGDCGS
VEYTPDNGLL KVRAGHVEDD IEKFVVGVLT KNAGTSDAEL TLSVVVGDYV RVAPLWIVST
DYDNYAIGYS CKDYKKSNQH RVNIWILSRT KTLNESSKST VNKFLKEHSK EFDQSKFVET
DFSEKACFFK KSHVYTVPFG A
