3SOF2_NAJME
ID 3SOF2_NAJME Reviewed; 61 AA.
AC P01474;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Cytotoxin homolog 2;
DE AltName: Full=Cytotoxin homolog V-II-2/V-II-3 {ECO:0000303|PubMed:4842298};
OS Naja melanoleuca (Forest cobra) (Black-lipped cobra).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Naja.
OX NCBI_TaxID=8643;
RN [1]
RP PROTEIN SEQUENCE, TOXIC DOSE, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=4842298; DOI=10.1016/s0006-291x(74)80202-0;
RA Carlsson F.H.H.;
RT "Snake venom toxins. The primary structures of two novel cytotoxin
RT homologues from the venom of forest cobra (Naja melanoleuca).";
RL Biochem. Biophys. Res. Commun. 59:269-276(1974).
CC -!- FUNCTION: Has low cytotoxic activity. {ECO:0000250|UniProtKB:P14541}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:4842298}. Target
CC cell membrane {ECO:0000250|UniProtKB:P62375}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC -!- TOXIC DOSE: LD(50) is 6.25 mg/kg by intravenous injection.
CC {ECO:0000269|PubMed:4842298}.
CC -!- MISCELLANEOUS: These two sequences have Gly and Leu at positions 25 and
CC 27, respectively, instead of 2 Met that are found in most cytotoxins.
CC The low toxicity of these 2 proteins may possibly be correlated with
CC these changes. {ECO:0000305|PubMed:4842298}.
CC -!- MISCELLANEOUS: Is classified as a P-type cytotoxin, since a proline
CC residue stands at position 30 (Pro-31 in standard classification).
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the snake three-finger toxin family. Short-chain
CC subfamily. Orphan group XV sub-subfamily. {ECO:0000305}.
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DR PIR; A01734; H3NJ2W.
DR AlphaFoldDB; P01474; -.
DR SMR; P01474; -.
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 CDD; cd00206; snake_toxin; 1.
DR Gene3D; 2.10.60.10; -; 1.
DR InterPro; IPR003572; Cytotoxin_Cobra.
DR InterPro; IPR016054; LY6_UPA_recep-like.
DR InterPro; IPR003571; Snake_3FTx.
DR InterPro; IPR045860; Snake_toxin-like_sf.
DR InterPro; IPR018354; Snake_toxin_con_site.
DR Pfam; PF00021; UPAR_LY6; 1.
DR PRINTS; PR00282; CYTOTOXIN.
DR SUPFAM; SSF57302; SSF57302; 1.
DR PROSITE; PS00272; SNAKE_TOXIN; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Membrane; Secreted;
KW Target cell membrane; Target membrane; Toxin.
FT CHAIN 1..61
FT /note="Cytotoxin homolog 2"
FT /evidence="ECO:0000269|PubMed:4842298"
FT /id="PRO_0000093503"
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"
FT VARIANT 36
FT /note="N -> K (in V-II-3)"
SQ SEQUENCE 61 AA; 6850 MW; C80D099A6D6A930B CRC64;
IKCHNTLLPF IYKTCPEGQN LCFKGTLKFP KKTTYNRGCA ATCPKSSLLV KYVCCNTNKC
N