ID   TXLR3_EISFE             Reviewed;         300 AA.
AC   Q3LX99;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 45.
DE   RecName: Full=Lysenin-related protein 3;
DE            Short=LRP-3;
DE   AltName: Full=eflr3;
DE            Short=efL3;
OS   Eisenia fetida (Red wiggler worm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Clitellata;
OC   Oligochaeta; Crassiclitellata; Lumbricina; Lumbricidae; Lumbricinae;
OC   Eisenia.
OX   NCBI_TaxID=6396;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Coelomocyte;
RX   PubMed=16386304; DOI=10.1016/j.dci.2005.09.002;
RA   Bruhn H., Winkelmann J., Andersen C., Andra J., Leippe M.;
RT   "Dissection of the mechanisms of cytolytic and antibacterial activity of
RT   lysenin, a defence protein of the annelid Eisenia fetida.";
RL   Dev. Comp. Immunol. 30:597-606(2006).
CC   -!- FUNCTION: Pore-forming toxin that specifically binds sphingomyelin in
CC       the plasma membrane of various cells. Has antibacterial and hemolytic
CC       activity (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Binds to sphingomyelin as a monomer by using its C-terminal
CC       domain. Forms a nonamer when sphingomyelin/LRP-3 ratio is lower than ca
CC       500. Oligomerization, but not binding, is influenced by the fluidity of
CC       sphingomyelin. {ECO:0000250|UniProtKB:O18423}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O18423}. Target
CC       cell membrane {ECO:0000250|UniProtKB:O18423}. Note=Forms a beta-barrel
CC       pore in the membrane. {ECO:0000250|UniProtKB:O18423}.
CC   -!- TISSUE SPECIFICITY: Expressed by coelomocytes.
CC   -!- SIMILARITY: Belongs to the lysenin family. {ECO:0000305}.
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DR   EMBL; DQ144453; ABA18726.1; -; mRNA.
DR   AlphaFoldDB; Q3LX99; -.
DR   SMR; Q3LX99; -.
DR   TCDB; 1.C.43.1.3; the earthworm lysenin toxin (lysenin) 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:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR   GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
PE   2: Evidence at transcript level;
KW   Antibiotic; Antimicrobial; Cytolysis; Disulfide bond; Hemolysis;
KW   Ion transport; Membrane; Secreted; Target cell membrane; Target membrane;
KW   Toxin; Transmembrane; Transport.
FT   CHAIN           1..300
FT                   /note="Lysenin-related protein 3"
FT                   /id="PRO_0000342609"
FT   REGION          12..35
FT                   /note="N-terminal cap domain"
FT                   /evidence="ECO:0000250|UniProtKB:O18423"
FT   REGION          36..109
FT                   /note="Beta-hairpin domain"
FT                   /evidence="ECO:0000250|UniProtKB:O18423"
FT   REGION          110..158
FT                   /note="N-terminal cap domain"
FT                   /evidence="ECO:0000250|UniProtKB:O18423"
FT   REGION          159..299
FT                   /note="C-terminal receptor-binding domain"
FT                   /evidence="ECO:0000250|UniProtKB:O18423"
FT   BINDING         187
FT                   /ligand="an N-(acyl)-sphingosylphosphocholine"
FT                   /ligand_id="ChEBI:CHEBI:64583"
FT                   /evidence="ECO:0000250|UniProtKB:O18423"
FT   BINDING         229
FT                   /ligand="an N-(acyl)-sphingosylphosphocholine"
FT                   /ligand_id="ChEBI:CHEBI:64583"
FT                   /evidence="ECO:0000250|UniProtKB:O18423"
FT   BINDING         235
FT                   /ligand="an N-(acyl)-sphingosylphosphocholine"
FT                   /ligand_id="ChEBI:CHEBI:64583"
FT                   /evidence="ECO:0000250|UniProtKB:O18423"
FT   BINDING         284
FT                   /ligand="an N-(acyl)-sphingosylphosphocholine"
FT                   /ligand_id="ChEBI:CHEBI:64583"
FT                   /evidence="ECO:0000250|UniProtKB:O18423"
FT   SITE            22
FT                   /note="Crucial for binding sphingomyelin and inducing
FT                   hemolysis"
FT                   /evidence="ECO:0000250"
FT   SITE            189
FT                   /note="Crucial for binding sphingomyelin and important for
FT                   inducing hemolysis"
FT                   /evidence="ECO:0000250"
FT   SITE            247
FT                   /note="Crucial for binding sphingomyelin and inducing
FT                   hemolysis"
FT                   /evidence="ECO:0000250"
FT   SITE            293
FT                   /note="Crucial for binding sphingomyelin and inducing
FT                   hemolysis"
FT                   /evidence="ECO:0000250"
FT   DISULFID        274..285
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   300 AA;  33841 MW;  ACC60A0CACF860DF CRC64;
     MSATAVTADG LEEIEVDVVA VWKEGYVYEN RGDTSVEQKI TMTKGMKNLN SETKTLTATH
     TVGRTLKVGD PFEIGSVEVS YSFSHQESQV SMTQTEVYSS QVIEHTVTIP PTSKFTRWKL
     NADVGGTDIE YMYLIDEVTP ISVTQTIPQV IRSRAKILVG RQIHLGTTAV RIKHAERQEY
     MTVIERKKWP AATLGKSNLF KFVLFEDSSG TRIKTLNTMY PGYEWAYSSD QGGVYFDESS
     DNPKQRWALS KALPLRHGDV VTFMNKYFTN SGLCYDDGPA TNVYCLDKRE DKWILEVVNP