ID   HLYS1_HYDVD             Reviewed;         244 AA.
AC   Q86LR2;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Hydralysin-1;
GN   Name=Hln-1 {ECO:0000303|PubMed:15824108};
OS   Hydra viridissima (Green hydra) (Chlorohydra viridissima).
OC   Eukaryota; Metazoa; Cnidaria; Hydrozoa; Hydroidolina; Anthoathecata;
OC   Aplanulata; Hydridae; Hydra.
OX   NCBI_TaxID=6082;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR
RP   LOCATION, TOXIC DOSE, AND TISSUE SPECIFICITY.
RX   PubMed=12885226; DOI=10.1021/bi0343929;
RA   Zhang M., Fishman Y., Sher D., Zlotkin E.;
RT   "Hydralysin, a novel animal group-selective paralytic and cytolytic protein
RT   from a noncnidocystic origin in hydra.";
RL   Biochemistry 42:8939-8944(2003).
RN   [2] {ECO:0000305}
RP   FUNCTION, AND TOXIC DOSE.
RX   PubMed=15824108; DOI=10.1074/jbc.m503242200;
RA   Sher D., Fishman Y., Zhang M., Lebendiker M., Gaathon A., Mancheno J.-M.,
RA   Zlotkin E.;
RT   "Hydralysins, a new category of beta-pore-forming toxins in cnidaria.";
RL   J. Biol. Chem. 280:22847-22855(2005).
CC   -!- FUNCTION: Induces an immediate fast muscle contraction followed by
CC       flaccid paralysis when injected into blowfly larvae. The paralytic
CC       effect is lower in mice and fish. Has strong cytolytic activity against
CC       insect Sf9 cells and human HeLa cells, weak activity against human JAR
CC       cells, and no activity against human HEK293 cells. Binds to erythrocyte
CC       membranes and has weak hemolytic activity, probably mediated by
CC       oligomerization and pore formation. {ECO:0000269|PubMed:12885226,
CC       ECO:0000269|PubMed:15824108}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12885226}. Target
CC       cell membrane {ECO:0000305|PubMed:12885226}. Note=Forms a membrane
CC       channel in the prey. {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Found in whole body extract but not in the
CC       cnidocyst. {ECO:0000269|PubMed:12885226}.
CC   -!- TOXIC DOSE: PD(50) is 0.36 mg/kg by injection in blowfly larvae, in
CC       PubMed:12885226.
CC   -!- TOXIC DOSE: PD(50) is 0.557 mg/kg by injection in blowfly larvae, in
CC       PubMed:15824108.
CC   -!- SIMILARITY: Belongs to the hydralysin family. {ECO:0000255}.
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DR   EMBL; AY178276; AAO39163.1; -; mRNA.
DR   AlphaFoldDB; Q86LR2; -.
DR   SMR; Q86LR2; -.
DR   TCDB; 1.C.4.4.1; the aerolysin channel-forming toxin (aerolysin) family.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IDA:UniProtKB.
DR   GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR   GO; GO:0044616; P:modulation of relaxation of muscle in another organism; IDA:UniProtKB.
DR   InterPro; IPR004991; Aerolysin-like.
DR   Pfam; PF03318; ETX_MTX2; 1.
PE   1: Evidence at protein level;
KW   Cytolysis; Direct protein sequencing; Hemolysis; Membrane; Neurotoxin;
KW   Secreted; Target cell membrane; Target membrane; Toxin.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..244
FT                   /note="Hydralysin-1"
FT                   /id="PRO_0000221558"
FT   CONFLICT        28
FT                   /note="E -> Q (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   244 AA;  26212 MW;  E1B53A719B7442DA CRC64;
     MGKELLTFSD LTWLDSSPDT VRSAFTREYG TTPDGIALNS EGYFGYHSPP ITEQYGRPCY
     KQTGETKITL QELGPSTDAV LGNSTAVNRG DSSIDLTVSV EGKWSDSTSW STSTETGVKM
     SSEFEVEGAF KMGGEFSLTL SVGKSGSSSV EKTSTSSVQV TVPPRSKVVV SMVGIMKKEK
     VFFEVPVTVD GSFGANFPST VQGHYFWFMD ARSCLNKTSG VIKGTIDHAN VFDVSVEVGP
     SEPL