ID   REDT_TRIIF              Reviewed;         260 AA.
AC   Q8T0Z3; Q8T0Z4;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   23-FEB-2022, sequence version 2.
DT   03-AUG-2022, entry version 22.
DE   RecName: Full=Trialysin {ECO:0000303|PubMed:11751887};
DE   AltName: Full=Triatoma infestans cytolysin {ECO:0000303|PubMed:11751887};
DE   Flags: Precursor;
OS   Triatoma infestans (Assassin bug).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Paraneoptera; Hemiptera; Heteroptera; Panheteroptera;
OC   Cimicomorpha; Reduviidae; Triatominae; Triatoma.
OX   NCBI_TaxID=30076;
RN   [1] {ECO:0000312|EMBL:AAL82381.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 56-75, FUNCTION, SYNTHESIS
RP   OF 61-87, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Saliva, and Salivary gland;
RX   PubMed=11751887; DOI=10.1074/jbc.m109874200;
RA   Amino R., Martins R.M., Procopio J., Hirata I.Y., Juliano M.A.,
RA   Schenkman S.;
RT   "Trialysin, a novel pore-forming protein from saliva of hematophagous
RT   insects activated by limited proteolysis.";
RL   J. Biol. Chem. 277:6207-6213(2002).
CC   -!- FUNCTION: Pore-forming protein that induces lysis of T.cruzi
CC       trypomastigotes, bacteria E.coli and human red blood cells
CC       (PubMed:11751887). The parasite lysis is much more important than the
CC       hemolysis, probably due to difference in membrane composition
CC       (PubMed:11751887). Its action on protozoan parasites and bacteria may
CC       indicate a role in the control of microorganism growth in the salivary
CC       glands (PubMed:11751887). {ECO:0000269|PubMed:11751887}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11751887}. Target
CC       cell membrane {ECO:0000305|PubMed:11751887}.
CC   -!- TISSUE SPECIFICITY: Expressed in salivary glands.
CC       {ECO:0000269|PubMed:11751887}.
CC   -!- MISCELLANEOUS: Has an amphipathic alpha-helical structure with positive
CC       charges on one side and hydrophobic amino acids on the opposite side.
CC       {ECO:0000305|PubMed:11751887}.
CC   -!- SIMILARITY: Belongs to the redulysin-like family. {ECO:0000305}.
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DR   EMBL; AF427486; AAL82380.1; -; mRNA.
DR   EMBL; AF427487; AAL82381.1; -; mRNA.
DR   TCDB; 1.C.86.1.1; the pore-forming trialysin (trialysin) family.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0051715; P:cytolysis in another organism; IDA:UniProtKB.
DR   GO; GO:0042742; P:defense response to bacterium; IDA:UniProtKB.
DR   GO; GO:0044179; P:hemolysis in another organism; IDA:UniProtKB.
DR   GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR   GO; GO:0035915; P:pore formation in membrane of another organism; IDA:UniProtKB.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Cytolysis; Direct protein sequencing; Hemolysis;
KW   Ion transport; Membrane; Secreted; Signal; Target cell membrane;
KW   Target membrane; Transmembrane; Transport.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..55
FT                   /note="Removed in mature form, probably by the serine
FT                   protease triapsin"
FT                   /evidence="ECO:0000305|PubMed:11751887"
FT                   /id="PRO_0000454325"
FT   CHAIN           56..260
FT                   /note="Trialysin"
FT                   /evidence="ECO:0000305|PubMed:11751887"
FT                   /id="PRO_5004313654"
FT   VARIANT         67
FT                   /note="F -> L"
FT                   /evidence="ECO:0000305|PubMed:11751887"
FT   VARIANT         83
FT                   /note="A -> L"
FT                   /evidence="ECO:0000305|PubMed:11751887"
FT   VARIANT         100
FT                   /note="G -> L"
FT                   /evidence="ECO:0000305|PubMed:11751887"
FT   VARIANT         178
FT                   /note="M -> T"
FT                   /evidence="ECO:0000305|PubMed:11751887"
FT   VARIANT         224
FT                   /note="I -> V"
FT                   /evidence="ECO:0000305|PubMed:11751887"
FT   VARIANT         238
FT                   /note="D -> E"
FT                   /evidence="ECO:0000305|PubMed:11751887"
FT   CONFLICT        72
FT                   /note="G -> S (in Ref. 1; AAL82381)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        111
FT                   /note="K -> N (in Ref. 1; AAL82381)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   260 AA;  28593 MW;  41DDECBE75BA19A2 CRC64;
     MSKFWLLLLL VAAFQFAHSY PAAEYELDET TNDEVRQFIG DGYFEDEGDD GDEERFKIKP
     GKVLDKFGKI VGKVLKQLKK VSAVAKVAMK KGAALLKKMG VKISPLKCEE KTCKSCVIFK
     IPTENSFCLT IRFMKTNIAT YLVVAGEINR KSKFEEKLKL GNMPRCVNVE GFIGKVCMKG
     IEGHAKSSSG QANVNFCLGL VAEKFGVGAK LCGIYANKKV RVKISPQLFP GATSLDGDIV
     KLDDNGEDAT TLDVDEVEID