ID   TXLR1_EISFE             Reviewed;         300 AA.
AC   O18424;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Lysenin-related protein 1;
DE            Short=LRP-1;
DE   AltName: Full=Lysenin-2;
DE   AltName: Full=efL2;
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=9210594; DOI=10.1016/s0378-1119(97)00047-4;
RA   Sekizawa Y., Kubo T., Kobayashi H., Nakajima T., Natori S.;
RT   "Molecular cloning of cDNA for lysenin, a novel protein in the earthworm
RT   Eisenia foetida that causes contraction of rat vascular smooth muscle.";
RL   Gene 191:97-102(1997).
RN   [2]
RP   FUNCTION, AND MUTAGENESIS OF ILE-211.
RX   PubMed=15274631; DOI=10.1021/bi049561j;
RA   Kiyokawa E., Makino A., Ishii K., Otsuka N., Yamaji-Hasegawa A.,
RA   Kobayashi T.;
RT   "Recognition of sphingomyelin by lysenin and lysenin-related proteins.";
RL   Biochemistry 43:9766-9773(2004).
CC   -!- FUNCTION: Pore-forming toxin that specifically binds sphingomyelin in
CC       the plasma membrane of various cells. Has hemolytic activity. Binding
CC       and hemolytic activities of this toxin are 10 times less than those of
CC       lysenin and lysenin-related protein 2. {ECO:0000269|PubMed:15274631}.
CC   -!- SUBUNIT: Binds to sphingomyelin as a monomer by using its C-terminal
CC       domain. Forms a nonamer when sphingomyelin/LRP-1 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; D85847; BAA21519.1; -; mRNA.
DR   AlphaFoldDB; O18424; -.
DR   SMR; O18424; -.
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   1: Evidence at protein 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 1"
FT                   /id="PRO_0000342607"
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"
FT   MUTAGEN         211
FT                   /note="I->F: Important increase in activity."
FT                   /evidence="ECO:0000269|PubMed:15274631"
SQ   SEQUENCE   300 AA;  33913 MW;  BD2CCFD8E6C03A35 CRC64;
     MSSSTVMADG FEEIEVDVVS VWKEGYAYEN RGNSSVQQKI TMTKGMKNLN SETKTLTATH
     TLGRTLKVGD PFEIASVEVS YTFSHQKSQV SMTQTEVYSS QVIEHTVTIP PNKKFTRWKL
     NADVGGTGIE YMYLIDEVTA IGADLTIPEV NKSRAKILVG RQIHLGETEI RIKHAERKEY
     MTVISRKSWP AATLGNSNLF KFVLFEDSSG IRIKTLNTMY PGYEWAYSSD QGGIYFDESS
     DNPKQRWALS KAMPLRHGDV VTFRNNFFTN SGMCYDDGPA TNVYCLEKRE DKWILEVVNT