3SAPF_NAJAT
ID 3SAPF_NAJAT Reviewed; 81 AA.
AC Q91135;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=Cytotoxin I-like P-15;
DE AltName: Full=Cardiotoxin I-like P-15;
DE Flags: Precursor;
OS Naja atra (Chinese cobra).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Naja.
OX NCBI_TaxID=8656;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RA Chang L.-S., Lin J., Wu P.-F.;
RT "Nucleotide sequence encoding cardiotoxin I-like protein with Thr-15 from
RT Naja naja atra.";
RL Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Shows cytolytic activity on many different cells by forming
CC pore in lipid membranes. In vivo, increases heart rate or kills the
CC animal by cardiac arrest. In addition, it binds to heparin with high
CC affinity, interacts with Kv channel-interacting protein 1 (KCNIP1) in a
CC calcium-independent manner, and binds to integrin alpha-V/beta-3
CC (ITGAV/ITGB3) with moderate affinity. {ECO:0000250|UniProtKB:P60301,
CC ECO:0000250|UniProtKB:P60304}.
CC -!- SUBUNIT: Monomer in solution; Homodimer and oligomer in the presence of
CC negatively charged lipids forming a pore with a size ranging between 20
CC and 30 Angstroms. {ECO:0000250|UniProtKB:P60301}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Target cell membrane
CC {ECO:0000250|UniProtKB:P60301}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC -!- MISCELLANEOUS: Is classified as a S-type cytotoxin, since a serine
CC residue stands at position 49 (Ser-29 in standard classification).
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the snake three-finger toxin family. Short-chain
CC subfamily. Type IA cytotoxin sub-subfamily. {ECO:0000305}.
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DR EMBL; X94317; CAA63978.1; -; mRNA.
DR AlphaFoldDB; Q91135; -.
DR SMR; Q91135; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0019835; P:cytolysis; 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 3: Inferred from homology;
KW Cardiotoxin; Cytolysis; Disulfide bond; Membrane; Secreted; Signal;
KW Target cell membrane; Target membrane; Toxin.
FT SIGNAL 1..21
FT /evidence="ECO:0000250"
FT CHAIN 22..81
FT /note="Cytotoxin I-like P-15"
FT /id="PRO_0000035389"
FT DISULFID 24..42
FT /evidence="ECO:0000250|UniProtKB:P60301"
FT DISULFID 35..59
FT /evidence="ECO:0000250|UniProtKB:P60301"
FT DISULFID 63..74
FT /evidence="ECO:0000250|UniProtKB:P60301"
FT DISULFID 75..80
FT /evidence="ECO:0000250|UniProtKB:P60301"
SQ SEQUENCE 81 AA; 8911 MW; 19C5396F5E17467D CRC64;
MKTLLLTLAA ATIVCLDLGY TLKCNKLIPI ASKTCPAGMN LCYKMFMMSD LTIPVKRGCI
DVCPKNSLLV KYVCCNTDRC N