LOSAC_LONON
ID LOSAC_LONON Reviewed; 413 AA.
AC Q1HLC0;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=Hemolin {ECO:0000303|PubMed:21177860};
DE EC=3.4.21.-;
DE AltName: Full=Lonomia obliqua Stuart factor activator {ECO:0000303|PubMed:21177860};
DE Short=Losac {ECO:0000303|PubMed:21177860};
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]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP IDENTIFICATION BY MASS SPECTROMETRY, 3D-STRUCTURE MODELING, AND RECOMBINANT
RP EXPRESSION.
RX PubMed=21177860; DOI=10.1074/jbc.m110.167718;
RA Alvarez-Flores M.P., Furlin D., Ramos O.H., Balan A., Konno K.,
RA Chudzinski-Tavassi A.M.;
RT "Losac, the first hemolin that exhibits procoagulant activity through
RT selective factor X proteolytic activation.";
RL J. Biol. Chem. 286:6918-6928(2011).
RN [2]
RP FUNCTION.
RC TISSUE=Larval bristle;
RX PubMed=16597435; DOI=10.1016/j.bbrc.2006.03.068;
RA Alvarez Flores M.P., Fritzen M., Reis C.V., Chudzinski-Tavassi A.M.;
RT "Losac, a factor X activator from Lonomia obliqua bristle extract: its role
RT in the pathophysiological mechanisms and cell survival.";
RL Biochem. Biophys. Res. Commun. 343:1216-1223(2006).
CC -!- FUNCTION: Bristle toxin involved in caterpillar defense by
CC participating in hemorrhagic syndrome characterized by a consumptive
CC coagulopathy (PubMed:21177860). Exhibits procoagulant activity through
CC selective factor X proteolytic activation (PubMed:21177860). Activates
CC factor X in a dose- and time-dependent manner but does not activate
CC gamma-carboxyglutamic acid domainless factor X (PubMed:21177860). Its
CC activity does not depend on calcium ions (PubMed:21177860). Also
CC functions as a growth stimulator and an inhibitor of cellular death for
CC endothelial cells (PubMed:16597435). In vitro, increases proliferation
CC of human umbilical vein endothelial cells (HUVEC) and inhibits the
CC apoptosis induced by starvation (PubMed:16597435). Also increases
CC slightly the complement decay-accelerating factor (CD55), which
CC protects cells from complement-mediated lysis (PubMed:16597435). On the
CC other hand, does not alter the release or expression of von Willebrand
CC factor (VWF), tissue factor (F3), intercellular adhesion molecule-1
CC (ICAM1), interleukin-8 (CXCL8), and prostacyclin (PubMed:16597435).
CC Does not show fibrinolytic or fibrinogenolytic activities
CC (PubMed:21177860). {ECO:0000269|PubMed:16597435,
CC ECO:0000269|PubMed:21177860}.
CC -!- ACTIVITY REGULATION: Increased activity in presence of phospholipids
CC (low concentrations) and calcium ions. Inhibited by PMSF. Not affected
CC by EDTA and E-64. {ECO:0000269|PubMed:21177860}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=188 nM for factor X in presence of phospholipids and calcium ions
CC {ECO:0000269|PubMed:21177860};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in larval bristles.
CC {ECO:0000269|PubMed:21177860}.
CC -!- DEVELOPMENTAL STAGE: Larvae. {ECO:0000269|PubMed:21177860}.
CC -!- MISCELLANEOUS: The recombinant protein is recognized by an antilonomic
CC horse hyperimmune serum. {ECO:0000269|PubMed:21177860}.
CC -!- SIMILARITY: Belongs to the hemolin family. {ECO:0000305}.
CC -!- CAUTION: Has no homology to any known proteases.
CC {ECO:0000269|PubMed:21177860}.
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DR EMBL; DQ479435; ABF21073.1; -; mRNA.
DR AlphaFoldDB; Q1HLC0; -.
DR SMR; Q1HLC0; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; 2.60.40.10; -; 4.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR Pfam; PF07679; I-set; 2.
DR SMART; SM00409; IG; 4.
DR SMART; SM00408; IGc2; 4.
DR SUPFAM; SSF48726; SSF48726; 4.
DR PROSITE; PS50835; IG_LIKE; 4.
PE 1: Evidence at protein level;
KW Blood coagulation cascade activating toxin; Disulfide bond; Glycoprotein;
KW Hemostasis impairing toxin; Hydrolase; Immunoglobulin domain; Protease;
KW Repeat; Secreted; Serine protease; Signal; Toxin.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:21177860"
FT CHAIN 19..413
FT /note="Hemolin"
FT /evidence="ECO:0000269|PubMed:21177860"
FT /id="PRO_5004190132"
FT DOMAIN 25..112
FT /note="Ig-like C2-type 1"
FT /evidence="ECO:0000255"
FT DOMAIN 122..211
FT /note="Ig-like C2-type 2"
FT /evidence="ECO:0000255"
FT DOMAIN 233..322
FT /note="Ig-like C2-type 3"
FT /evidence="ECO:0000255"
FT DOMAIN 327..413
FT /note="Ig-like C2-type 4"
FT /evidence="ECO:0000255"
FT CARBOHYD 283
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 46..97
FT /evidence="ECO:0000250|UniProtKB:P25033"
FT DISULFID 140..199
FT /evidence="ECO:0000250|UniProtKB:P25033"
FT DISULFID 252..305
FT /evidence="ECO:0000250|UniProtKB:P25033"
FT DISULFID 349..395
FT /evidence="ECO:0000250|UniProtKB:P25033"
SQ SEQUENCE 413 AA; 45114 MW; 9BD4BC83B52AB906 CRC64;
MASKSLVVLS ACIIIGSAVP VEKLPVLKSQ PAEVLFRESQ PTVLECIIEG QEEGVKYTWT
KDGKDFKWTE HNAAQRTNEG SLVFLSPQPS DEGHYQCFAQ TAAGVASSRV ISFKRTYLVA
EPAKTHEKTP VEGKPFQLDC VIPNAYPKPE IFWKKSLSGA DPNADSANLG RRVTAGPDGN
LYFTTVEKED VSDIYKYVCV AKSPAHDGEV RLVEYIIKEV TKDTSGYKGE LVPQYLSKDI
VAKVGSVTMI YCMYGGKPQG FPDYFKDGKD VNGDAGGRIT RHNRTSGKRL LIKETLLEDQ
GTYTCEESNG VGKPVKHSLK VTVVSAPKYV KSPEKVIIAK QGQDVTIPCQ VTGLPAPKVT
WTHNAQPLSG GKTTVTESGL IIKGLQKGDK GYYGCRSTNE HGDEYVETLV QVN
