ID   CXA3_CERLA              Reviewed;          95 AA.
AC   P01527;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 54.
DE   RecName: Full=Cerebratulus toxin A-III {ECO:0000303|PubMed:8160185};
DE   AltName: Full=Cytolysin A-III {ECO:0000305};
DE   AltName: Full=Cytotoxin A-III {ECO:0000303|PubMed:6997292};
OS   Cerebratulus lacteus (Milky ribbon worm) (Micrura lactea).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Nemertea; Pilidiophora;
OC   Heteronemertea; Lineidae; Cerebratulus.
OX   NCBI_TaxID=6221;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=6997292; DOI=10.1016/s0021-9258(19)70641-3;
RA   Blumenthal K.M., Kem W.R.;
RT   "Structure and action of heteronemertine polypeptide toxins. Primary
RT   structure of Cerebratulus lacteus toxin A-III.";
RL   J. Biol. Chem. 255:8266-8272(1980).
RN   [2]
RP   DISULFIDE BONDS.
RX   PubMed=7410363; DOI=10.1016/s0021-9258(19)70642-5;
RA   Blumenthal K.M.;
RT   "Structure and action of heteronemertine polypeptide toxins. Disulfide
RT   bonds of Cerebratulus lacteus toxin A-III.";
RL   J. Biol. Chem. 255:8273-8274(1980).
RN   [3]
RP   SYNTHESIS OF 1-16 AND 63-95.
RX   PubMed=2874118; DOI=10.1111/j.1399-3011.1986.tb01049.x;
RA   Balasubramaniam A., Murphy R.F., Blumenthal K.M.;
RT   "Synthesis of sequences 1-16 and 63-95 of Cerebratulus lacteus toxin AIII.
RT   Hemolytic activity in a toxin fragment.";
RL   Int. J. Pept. Protein Res. 27:508-513(1986).
RN   [4]
RP   REVIEW.
RX   PubMed=8160185; DOI=10.1016/0300-483x(94)90251-8;
RA   Kem W.R.;
RT   "Structure and membrane actions of a marine worm protein cytolysin,
RT   Cerebratulus toxin A-III.";
RL   Toxicology 87:189-203(1994).
CC   -!- FUNCTION: Permeabilizes a variety of cells. Forms large pores which
CC       allows the release of large proteins almost as rapidly as small organic
CC       molecules and inorganic ions. At sublytic concentrations, the toxin
CC       also inhibits protein kinase C and endogenous voltage-gated cation
CC       selective (sodium, calcium) channels occurring in the nervous and
CC       cardiovascular systems.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the worm cytolysin family. {ECO:0000305}.
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DR   PIR; A01790; CWHNA3.
DR   AlphaFoldDB; P01527; -.
DR   PRIDE; P01527; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Cytolysis; Direct protein sequencing; Disulfide bond; Secreted; Toxin.
FT   CHAIN           1..95
FT                   /note="Cerebratulus toxin A-III"
FT                   /evidence="ECO:0000269|PubMed:6997292"
FT                   /id="PRO_0000221570"
FT   DISULFID        17..38
FT                   /evidence="ECO:0000269|PubMed:7410363"
FT   DISULFID        23..34
FT                   /evidence="ECO:0000269|PubMed:7410363"
FT   DISULFID        48..61
FT                   /evidence="ECO:0000269|PubMed:7410363"
SQ   SEQUENCE   95 AA;  9809 MW;  C592A569B46950E8 CRC64;
     ISWPSYPGSE GIRSSNCQKK LNCGTKNIAT KGVCKAFCLG RKRFWQKCGK NGSGSKGSKV
     CNAVLAHAVE KAGKGLIAVT DKAVAAIVKL AAGIA