ID   3SIMB_DENPO             Reviewed;          65 AA.
AC   P80495;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Adrenergic toxin rho-elapitoxin-Dp1a;
DE            Short=rho-EPTX-Dp1a;
DE   AltName: Full=Muscarinic toxin beta {ECO:0000303|PubMed:8536706};
DE            Short=MT-beta {ECO:0000303|PubMed:8536706};
OS   Dendroaspis polylepis polylepis (Black mamba).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Elapinae; Dendroaspis.
OX   NCBI_TaxID=8620;
RN   [1]
RP   PROTEIN SEQUENCE, SUBCELLULAR LOCATION, AND FUNCTION.
RC   TISSUE=Venom;
RX   PubMed=8536706; DOI=10.1111/j.1432-1033.1995.579_b.x;
RA   Jolkkonen M., van Giersbergen P.L.M., Hellman U., Wernstedt C., Oras A.,
RA   Satyapan N., Adem A., Karlsson E.;
RT   "Muscarinic toxins from the black mamba Dendroaspis polylepis.";
RL   Eur. J. Biochem. 234:579-585(1995).
RN   [2]
RP   PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom;
RX   PubMed=8154745; DOI=10.1111/j.1749-6632.1994.tb26623.x;
RA   Karlsson E., Jolkkonen M., Satyapan N., Adem A., Kumlin E., Hellman U.,
RA   Wernstedt C.;
RT   "Protein toxins that bind to muscarinic acetylcholine receptors.";
RL   Ann. N. Y. Acad. Sci. 710:153-161(1994).
RN   [3]
RP   MECHANISM OF BINDING, AND FUNCTION.
RX   PubMed=10978757; DOI=10.1016/s0041-0101(00)00141-0;
RA   Jolkkonen M., Oras A., Toomela T., Karlsson E., Jarv J., Akerman K.E.;
RT   "Kinetic evidence for different mechanisms of interaction of black mamba
RT   toxins MT alpha and MT beta with muscarinic receptors.";
RL   Toxicon 39:377-382(2001).
RN   [4]
RP   FUNCTION, AND SYNTHESIS.
RX   PubMed=23648423; DOI=10.1016/j.toxicon.2013.04.017;
RA   Blanchet G., Upert G., Mourier G., Gilquin B., Gilles N., Servent D.;
RT   "New alpha-adrenergic property for synthetic MTbeta and CM-3 three-finger
RT   fold toxins from black mamba.";
RL   Toxicon 75:160-167(2013).
CC   -!- FUNCTION: This toxin shows activities on different G-protein coupled
CC       receptors. It is highly potent on various alpha-adrenoceptors (ADRA)
CC       (subnanomolar affinity for ADRA1A). Order of potency is the following:
CC       ADRA1A > ADRA1B > ADRA1D > ADRA2C (PubMed:23648423). It is also found
CC       to reversibly bind to muscarinic acetylcholine receptors (CHRM), but
CC       the affinity is much weaker (CHRM1 and CHRM2, Ki>1 uM; CHRM3, Ki=140
CC       nM; CHRM4, Ki=120 nM; CHRM5, Ki=350 nM) (PubMed:8536706,
CC       PubMed:10978757, PubMed:23648423). {ECO:0000269|PubMed:10978757,
CC       ECO:0000269|PubMed:23648423}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8154745,
CC       ECO:0000269|PubMed:8536706}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:8154745, ECO:0000305|PubMed:8536706}.
CC   -!- MISCELLANEOUS: Is classified as a P-type cytotoxin, since a proline
CC       residue stands at position 33 (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   PIR; S67985; S67985.
DR   AlphaFoldDB; P80495; -.
DR   SMR; P80495; -.
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   InterPro; IPR035076; Toxin/TOLIP.
DR   Pfam; PF00087; Toxin_TOLIP; 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;
KW   G-protein coupled receptor impairing toxin; Neurotoxin;
KW   Postsynaptic neurotoxin; Secreted; Toxin.
FT   CHAIN           1..65
FT                   /note="Adrenergic toxin rho-elapitoxin-Dp1a"
FT                   /evidence="ECO:0000269|PubMed:8154745,
FT                   ECO:0000269|PubMed:8536706"
FT                   /id="PRO_0000093649"
FT   DISULFID        3..24
FT                   /evidence="ECO:0000250|UniProtKB:P60301"
FT   DISULFID        17..42
FT                   /evidence="ECO:0000250|UniProtKB:P60301"
FT   DISULFID        46..57
FT                   /evidence="ECO:0000250|UniProtKB:P60301"
FT   DISULFID        58..63
FT                   /evidence="ECO:0000250|UniProtKB:P60301"
SQ   SEQUENCE   65 AA;  7345 MW;  09BB9399CDE279F1 CRC64;
     LTCVTSKSIF GITTEDCPDG QNLCFKRRHY VVPKIYDITR GCVATCPIPE NYDSIHCCKT
     DKCNE