3SB1_HEMHA
ID 3SB1_HEMHA Reviewed; 61 AA.
AC P01471;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Cytotoxin 1;
DE AltName: Full=Hemolytic protein 12B {ECO:0000303|PubMed:4734897};
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, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=4734897; DOI=10.1021/bi00728a015;
RA Fryklund L., Eaker D.;
RT "Complete amino acid sequence of a nonneurotoxic hemolytic protein from the
RT venom of Haemachatus haemachates (African ringhals cobra).";
RL Biochemistry 12:661-667(1973).
CC -!- FUNCTION: This protein lyses red blood cells and has cardiotoxic and
CC hypotensive activities. {ECO:0000303|PubMed:4734897}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:4734897}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
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 PIR; A01731; H3RI1L.
DR AlphaFoldDB; P01471; -.
DR BMRB; P01471; -.
DR SMR; P01471; -.
DR PRIDE; P01471; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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 Cardiotoxin; Cytolysis; Direct protein sequencing; Disulfide bond;
KW Hemolysis; Hypotensive agent; Secreted; Toxin.
FT CHAIN 1..61
FT /note="Cytotoxin 1"
FT /evidence="ECO:0000269|PubMed:4734897"
FT /id="PRO_0000093476"
FT DISULFID 3..22
FT /evidence="ECO:0000250|UniProtKB:P60301"
FT DISULFID 15..39
FT /evidence="ECO:0000250|UniProtKB:P60301"
FT DISULFID 43..54
FT /evidence="ECO:0000250|UniProtKB:P60301"
FT DISULFID 55..60
FT /evidence="ECO:0000250|UniProtKB:P60301"
SQ SEQUENCE 61 AA; 6844 MW; EDF501522BB76087 CRC64;
LKCHNKLVPF LSKTCPEGKN LCYKMTMLKM PKIPIKRGCT DACPKSSLLV KVVCCNKDKC
N