3SDC4_OPHHA
ID 3SDC4_OPHHA Reviewed; 84 AA.
AC Q2VBN7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 62.
DE RecName: Full=Beta-cardiotoxin CTX14;
DE Flags: Precursor;
OS Ophiophagus hannah (King cobra) (Naja hannah).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus.
OX NCBI_TaxID=8665;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=16689684; DOI=10.1042/bj20060004;
RA Li J., Zhang H., Liu J., Xu K.;
RT "Novel genes encoding six kinds of three-finger toxins in Ophiophagus
RT hannah (king cobra) and function characterization of two recombinant long-
RT chain neurotoxins.";
RL Biochem. J. 398:233-242(2006).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=24297900; DOI=10.1073/pnas.1314702110;
RA Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J.,
RA McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J.,
RA Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A.,
RA de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C.,
RA Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M.,
RA Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., Dirks R.P.,
RA Spaink H.P., Duboule D., McGlinn E., Kini R.M., Richardson M.K.;
RT "The king cobra genome reveals dynamic gene evolution and adaptation in the
RT snake venom system.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(2013).
CC -!- FUNCTION: Acts as a beta-blocker by binding to beta-1 and beta-2
CC adrenergic receptors (ADRB1 and ADRB2). It dose-dependently decreases
CC the heart rate (bradycardia), whereas conventional cardiotoxins
CC increases it. At 100 mg/kg, intraperitoneal injection into mice
CC provokes labored breathing, impaired locomotion, lack of response to
CC external stimuli, and death (after 30 min).
CC {ECO:0000250|UniProtKB:Q69CK0}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:24297900}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:24297900}.
CC -!- MISCELLANEOUS: Does not affect blood coagulation and does not show
CC significant hemolytic activity. {ECO:0000250|UniProtKB:Q69CK0}.
CC -!- MISCELLANEOUS: Is classified as a P-type cytotoxin, since a proline
CC residue stands at position 52 (Pro-31 in standard classification).
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the snake three-finger toxin family. Short-chain
CC subfamily. Aminergic toxin sub-subfamily. {ECO:0000305}.
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DR EMBL; DQ273578; ABB83632.1; -; mRNA.
DR AlphaFoldDB; Q2VBN7; -.
DR SMR; Q2VBN7; -.
DR TCDB; 1.C.74.1.3; the snake cytotoxin (sct) family.
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 PRINTS; PR00282; CYTOTOXIN.
DR SUPFAM; SSF57302; SSF57302; 1.
DR PROSITE; PS00272; SNAKE_TOXIN; 1.
PE 1: Evidence at protein level;
KW Cardiotoxin; Disulfide bond; G-protein coupled receptor impairing toxin;
KW Secreted; Signal; Toxin.
FT SIGNAL 1..21
FT /evidence="ECO:0000250|UniProtKB:Q69CK0"
FT CHAIN 22..84
FT /note="Beta-cardiotoxin CTX14"
FT /id="PRO_5000006488"
FT DISULFID 24..43
FT /evidence="ECO:0000250|UniProtKB:Q69CK0"
FT DISULFID 36..61
FT /evidence="ECO:0000250|UniProtKB:Q69CK0"
FT DISULFID 65..76
FT /evidence="ECO:0000250|UniProtKB:Q69CK0"
FT DISULFID 77..82
FT /evidence="ECO:0000250|UniProtKB:Q69CK0"
SQ SEQUENCE 84 AA; 9256 MW; 8A57A07FCDDD655F CRC64;
MKTLLLTLVV VTIVCLDLGY TRKCLNTPLP LIYTTCPIGQ DKCVKMTIKK LPSKYDVIRG
CTDICPKSSA DVVVVCCDTN KCDK