ID   3SOE_HEMHA              Reviewed;          63 AA.
AC   P24778;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Cytotoxin homolog;
DE   AltName: Full=Toxin 9B/9BB {ECO:0000303|PubMed:404150};
OS   Hemachatus haemachatus (Rinkhals) (Sepedon haemachatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Elapinae; Hemachatus.
OX   NCBI_TaxID=8626;
RN   [1]
RP   PROTEIN SEQUENCE, TOXIC DOSE, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=404150; DOI=10.1111/j.1432-1033.1977.tb11403.x;
RA   Joubert F.J.;
RT   "Snake venom toxins. The amino-acid sequences of three toxins (9B, 11 and
RT   12A) from Hemachatus haemachatus (Ringhals) venom.";
RL   Eur. J. Biochem. 74:387-396(1977).
CC   -!- FUNCTION: This toxin has a very low toxicity.
CC       {ECO:0000269|PubMed:404150}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:404150}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC   -!- TOXIC DOSE: LD(50) is 33.5 mg/kg by intravenous injection into mice.
CC       {ECO:0000269|PubMed:404150}.
CC   -!- MISCELLANEOUS: Is classified as a P-type cytotoxin, since a proline
CC       residue stands at position 31 (Pro-31 in standard classification).
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the snake three-finger toxin family. Short-chain
CC       subfamily. Orphan group XIV sub-subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P24778; -.
DR   SMR; P24778; -.
DR   PRIDE; P24778; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   CDD; cd00206; snake_toxin; 1.
DR   Gene3D; 2.10.60.10; -; 1.
DR   InterPro; IPR003572; Cytotoxin_Cobra.
DR   InterPro; IPR003571; Snake_3FTx.
DR   InterPro; IPR045860; Snake_toxin-like_sf.
DR   InterPro; IPR018354; Snake_toxin_con_site.
DR   InterPro; IPR035076; Toxin/TOLIP.
DR   Pfam; PF00087; Toxin_TOLIP; 1.
DR   PRINTS; PR00282; CYTOTOXIN.
DR   SUPFAM; SSF57302; SSF57302; 1.
DR   PROSITE; PS00272; SNAKE_TOXIN; 1.
PE   1: Evidence at protein level;
KW   Cardiotoxin; Direct protein sequencing; Disulfide bond; Secreted; Toxin.
FT   CHAIN           1..63
FT                   /note="Cytotoxin homolog"
FT                   /evidence="ECO:0000269|PubMed:404150"
FT                   /id="PRO_0000093479"
FT   DISULFID        3..22
FT                   /evidence="ECO:0000250|UniProtKB:P60301"
FT   DISULFID        15..40
FT                   /evidence="ECO:0000250|UniProtKB:P60301"
FT   DISULFID        44..55
FT                   /evidence="ECO:0000250|UniProtKB:P60301"
FT   DISULFID        56..61
FT                   /evidence="ECO:0000250|UniProtKB:P60301"
FT   VARIANT         37
FT                   /note="K -> R (in toxin 9BB)"
SQ   SEQUENCE   63 AA;  7193 MW;  F41FF0BAE13206FF CRC64;
     LICHNRPLPF LHKTCPEGQN ICYKMTLKKT PMKLSVKRGC AATCPSERPL VQVECCKTDK
     CNW