TXLR2_EISFE
ID TXLR2_EISFE Reviewed; 300 AA.
AC O18425; Q39712;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Lysenin-related protein 2;
DE Short=LRP-2;
DE AltName: Full=Fetidin;
DE AltName: Full=Hemolysin;
DE AltName: Full=Lysenin-3;
DE AltName: Full=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 [GENOMIC DNA], AND FUNCTION.
RC TISSUE=Coelomic fluid, and Coelomocyte;
RX PubMed=9219536; DOI=10.1111/j.1432-1033.1997.00756.x;
RA Lassegues M., Milochau A., Doignon F., Du Pasquier L., Valembois P.;
RT "Sequence and expression of an Eisenia-fetida-derived cDNA clone that
RT encodes the 40-kDa fetidin antibacterial protein.";
RL Eur. J. Biochem. 246:756-762(1997).
RN [2]
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 [3]
RP FUNCTION.
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).
RN [4]
RP GENE EXPRESSION.
RX PubMed=16051356; DOI=10.1016/j.dci.2005.06.014;
RA Prochazkova P., Silerova M., Felsberg J., Joskova R., Beschin A.,
RA De Baetselier P., Bilej M.;
RT "Relationship between hemolytic molecules in Eisenia fetida earthworms.";
RL Dev. Comp. Immunol. 30:381-392(2006).
CC -!- FUNCTION: Pore-forming toxin that specifically binds sphingomyelin in
CC the plasma membrane of various cells (By similarity). Has hemolytic
CC activity. It also has antibacterial activities against B.megaterium.
CC {ECO:0000250, ECO:0000269|PubMed:15274631, ECO:0000269|PubMed:9219536}.
CC -!- SUBUNIT: Binds to sphingomyelin as a monomer by using its C-terminal
CC domain. Forms a nonamer when sphingomyelin/LRP-2 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; U02710; AAB67727.1; -; Genomic_DNA.
DR EMBL; D85848; BAA21520.1; -; mRNA.
DR AlphaFoldDB; O18425; -.
DR SMR; O18425; -.
DR TCDB; 1.C.43.1.2; 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 2"
FT /id="PRO_0000342608"
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 211
FT /note="Important for activity"
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; 34143 MW; B63DACBF537FEA3D CRC64;
MSSRAGIAEG YEQIEVDVVA VWKEGYVYEN RGSTSVEQKI KITKGMRNLN SETKTLTASH
SIGSTISTGD LFEIATVDVS YSYSHEESQV SMTETEVYES KEIEHTITIP PTSKFTRWQL
NADVGGADIE YMYLIDEVTP IGGTLSIPQV IKSRAKILVG REIYLGETEI RIKHADRKEY
MTVVSRKSWP AATLGHSKLY KFVLYEDMYG FRIKTLNTMY SGYEYAYSSD QGGIYFDQGS
DNPKQRWAIN KSLPLRHGDV VTFMNKYFTR SGLCYYDGPA TDVYCLDKRE DKWILEVVKP
