ID   3SBH_HEMHA              Reviewed;          61 AA.
AC   B3EWH9;
DT   28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2012, sequence version 1.
DT   03-AUG-2022, entry version 30.
DE   RecName: Full=Three-finger hemachatoxin;
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   X-RAY CRYSTALLOGRAPHY (2.43 ANGSTROMS), PROTEIN SEQUENCE, MASS
RP   SPECTROMETRY, DISULFIDE BONDS, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=23144733; DOI=10.1371/journal.pone.0048112;
RA   Girish V.M., Kumar S., Joseph L., Jobichen C., Kini R.M., Sivaraman J.;
RT   "Identification and structural characterization of a new three-finger toxin
RT   hemachatoxin from Hemachatus haemachatus venom.";
RL   PLoS ONE 7:E48112-E48112(2012).
CC   -!- FUNCTION: This protein lyses red blood cells and has cardiotoxic and
CC       hypotensive activities. {ECO:0000250|UniProtKB:P01471}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23144733}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=6835.68; Mass_error=0.94; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:23144733};
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. Type IB cytotoxin sub-subfamily. {ECO:0000305}.
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DR   PDB; 3VTS; X-ray; 2.43 A; A/B=1-61.
DR   PDBsum; 3VTS; -.
DR   AlphaFoldDB; B3EWH9; -.
DR   SMR; B3EWH9; -.
DR   PRIDE; B3EWH9; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR   GO; GO:0008217; P:regulation of blood pressure; 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   PRINTS; PR00282; CYTOTOXIN.
DR   SUPFAM; SSF57302; SSF57302; 1.
DR   PROSITE; PS00272; SNAKE_TOXIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cardiotoxin; Cytolysis; Direct protein sequencing;
KW   Disulfide bond; Hemolysis; Hypotensive agent; Secreted; Toxin.
FT   CHAIN           1..61
FT                   /note="Three-finger hemachatoxin"
FT                   /evidence="ECO:0000269|PubMed:23144733"
FT                   /id="PRO_0000420427"
FT   DISULFID        3..22
FT                   /evidence="ECO:0000269|PubMed:23144733,
FT                   ECO:0000312|PDB:3VTS"
FT   DISULFID        15..39
FT                   /evidence="ECO:0000269|PubMed:23144733,
FT                   ECO:0000312|PDB:3VTS"
FT   DISULFID        43..54
FT                   /evidence="ECO:0000269|PubMed:23144733,
FT                   ECO:0000312|PDB:3VTS"
FT   DISULFID        55..60
FT                   /evidence="ECO:0000269|PubMed:23144733,
FT                   ECO:0000312|PDB:3VTS"
FT   STRAND          2..4
FT                   /evidence="ECO:0007829|PDB:3VTS"
FT   STRAND          6..10
FT                   /evidence="ECO:0007829|PDB:3VTS"
FT   STRAND          12..14
FT                   /evidence="ECO:0007829|PDB:3VTS"
FT   STRAND          21..27
FT                   /evidence="ECO:0007829|PDB:3VTS"
FT   STRAND          30..42
FT                   /evidence="ECO:0007829|PDB:3VTS"
FT   STRAND          48..55
FT                   /evidence="ECO:0007829|PDB:3VTS"
SQ   SEQUENCE   61 AA;  6844 MW;  EDF4ABE381076087 CRC64;
     LKCHNKLVPF LSKTCPEGKN LCYKMTLMKM PKIPIKRGCT DACPKSSLLV KVVCCNKDKC
     N