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3SDC7_OPHHA
ID   3SDC7_OPHHA             Reviewed;          84 AA.
AC   Q69CK0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Beta-cardiotoxin CTX27;
DE   AltName: Full=OH-27;
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=15302536; DOI=10.1016/j.toxicon.2004.06.003;
RA   He Y.-Y., Lee W.-H., Zhang Y.;
RT   "Cloning and purification of alpha-neurotoxins from king cobra (Ophiophagus
RT   hannah).";
RL   Toxicon 44:295-303(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 22-51, FUNCTION, MASS
RP   SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=17616557; DOI=10.1096/fj.07-8658com;
RA   Rajagopalan N., Pung Y.F., Zhu Y.Z., Wong P.T.H., Kumar P.P., Kini R.M.;
RT   "Beta-cardiotoxin: a new three-finger toxin from Ophiophagus hannah (king
RT   cobra) venom with beta-blocker activity.";
RL   FASEB J. 21:3685-3695(2007).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
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).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.41 ANGSTROMS) OF 22-84, AND DISULFIDE BONDS.
RA   Roy A., Qingxiang S., Kini R.M., Sivaraman J.;
RT   "Crystal structure of beta-cardiotoxin, a novel three- cardiotoxin from the
RT   venom of Ophiophagus hannah.";
RL   Submitted (NOV-2010) to the PDB data bank.
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:0000269|PubMed:17616557}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17616557}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=7012.42; Mass_error=0.91; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:17616557};
CC   -!- MISCELLANEOUS: Does not affect blood coagulation and does not show
CC       significant hemolytic activity. {ECO:0000269|PubMed:17616557}.
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; AY596935; AAT97257.1; -; mRNA.
DR   EMBL; AY354198; AAR10440.1; -; mRNA.
DR   PDB; 3PLC; X-ray; 2.41 A; A/B/C=22-84.
DR   PDBsum; 3PLC; -.
DR   AlphaFoldDB; Q69CK0; -.
DR   SMR; Q69CK0; -.
DR   PRIDE; Q69CK0; -.
DR   TopDownProteomics; Q69CK0; -.
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; 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   3D-structure; Cardiotoxin; Direct protein sequencing; Disulfide bond;
KW   G-protein coupled receptor impairing toxin; Secreted; Signal; Toxin.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000269|PubMed:17616557"
FT   CHAIN           22..84
FT                   /note="Beta-cardiotoxin CTX27"
FT                   /evidence="ECO:0000305|PubMed:17616557"
FT                   /id="PRO_0000316089"
FT   DISULFID        24..43
FT                   /evidence="ECO:0000269|Ref.4, ECO:0000312|PDB:3PLC"
FT   DISULFID        36..61
FT                   /evidence="ECO:0000269|Ref.4, ECO:0000312|PDB:3PLC"
FT   DISULFID        65..76
FT                   /evidence="ECO:0000269|Ref.4, ECO:0000312|PDB:3PLC"
FT   DISULFID        77..82
FT                   /evidence="ECO:0000269|Ref.4, ECO:0000312|PDB:3PLC"
FT   STRAND          23..25
FT                   /evidence="ECO:0007829|PDB:3PLC"
FT   STRAND          27..31
FT                   /evidence="ECO:0007829|PDB:3PLC"
FT   STRAND          33..35
FT                   /evidence="ECO:0007829|PDB:3PLC"
FT   STRAND          42..50
FT                   /evidence="ECO:0007829|PDB:3PLC"
FT   STRAND          58..64
FT                   /evidence="ECO:0007829|PDB:3PLC"
FT   STRAND          73..77
FT                   /evidence="ECO:0007829|PDB:3PLC"
SQ   SEQUENCE   84 AA;  9311 MW;  A745B26852DD7085 CRC64;
     MKTLLLTLVV VTIVCLDLGY TRKCLNTPLP LIYTTCPIGQ DKCVKMTIKK LPSKYDVIRG
     CIDICPKSSA DVEVLCCDTN KCNK
 
 
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