ID   SRTXL_ATRMM             Reviewed;         351 AA.
AC   Q6RY98;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   22-FEB-2023, entry version 56.
DE   RecName: Full=Long-sarafotoxin;
DE            Short=L-SRTX;
DE   Contains:
DE     RecName: Full=Sarafotoxin-m;
DE              Short=SRTX-m;
DE   Contains:
DE     RecName: Full=Sarafotoxin-m1;
DE              Short=SRTX-m1;
DE   Contains:
DE     RecName: Full=Sarafotoxin-m2;
DE              Short=SRTX-m2;
DE   Contains:
DE     RecName: Full=Sarafotoxin-m3;
DE              Short=SRTX-m3;
DE   Contains:
DE     RecName: Full=Sarafotoxin-m4;
DE              Short=SRTX-m4;
DE   Contains:
DE     RecName: Full=Sarafotoxin-m5;
DE              Short=SRTX-m5;
DE   Flags: Precursor; Fragment;
OS   Atractaspis microlepidota microlepidota.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Lamprophiidae; Atractaspidinae; Atractaspis.
OX   NCBI_TaxID=172021;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 30-53; 78-101; 126-149;
RP   174-197; 222-245; 270-293 AND 318-341, FUNCTION, SUBCELLULAR LOCATION,
RP   TISSUE SPECIFICITY, TOXIC DOSE, SYNTHESIS OF SARAFOTOXIN-M, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Venom, and Venom gland;
RX   PubMed=15350691; DOI=10.1016/j.peptides.2004.05.010;
RA   Hayashi M.A.F., Ligny-Lemaire C., Wollberg Z., Wery M., Galat A., Ogawa T.,
RA   Muller B.H., Lamthanh H., Doljansky Y., Bdolah A., Stoecklin R.,
RA   Ducancel F.;
RT   "Long-sarafotoxins: characterization of a new family of endothelin-like
RT   peptides.";
RL   Peptides 25:1243-1251(2004).
RN   [2]
RP   STRUCTURE BY NMR OF SARAFOTOXIN-M, DISULFIDE BONDS, AND MUTAGENESIS OF
RP   51-ASP--PRO-53.
RX   PubMed=21889567; DOI=10.1016/j.biochi.2011.08.014;
RA   Mourier G., Hajj M., Cordier F., Zorba A., Gao X., Coskun T., Herbet A.,
RA   Marcon E., Beau F., Delepierre M., Ducancel F., Servent D.;
RT   "Pharmacological and structural characterization of long-sarafotoxins, a
RT   new family of endothelin-like peptides: role of the C-terminus extension.";
RL   Biochimie 94:461-470(2012).
CC   -!- FUNCTION: Vasoconstrictor activity. These toxins cause cardiac arrest
CC       probably as a result of coronary vasospasm. The major effects of
CC       sarafotoxin-m are a progressive decrease in heart rate (bradycardia)
CC       that turns into an arrhythmic phase that is followed by an A-V block.
CC       {ECO:0000269|PubMed:15350691}.
CC   -!- FUNCTION: [Sarafotoxin-m]: Vasoconstrictor activity. Causes cardiac
CC       arrest probably as a result of coronary vasospasm (By similarity).
CC       Displays low agonistic activities towards endothelin-2 receptor (EDNRB)
CC       (displays affinity in the micromolar range) (PubMed:21889567).
CC       {ECO:0000250, ECO:0000269|PubMed:15350691,
CC       ECO:0000269|PubMed:21889567}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15350691}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:15350691}.
CC   -!- TOXIC DOSE: [Sarafotoxin-m]: LD(50) is 27-37 ug/kg by intravenous
CC       injection into mice. {ECO:0000269|PubMed:15350691}.
CC   -!- SIMILARITY: Belongs to the endothelin/sarafotoxin family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY485934; AAR84382.1; -; mRNA.
DR   PDB; 2LDF; NMR; -; A=270-293.
DR   PDBsum; 2LDF; -.
DR   AlphaFoldDB; Q6RY98; -.
DR   SMR; Q6RY98; -.
DR   EvolutionaryTrace; Q6RY98; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0019229; P:regulation of vasoconstriction; IEA:InterPro.
DR   GO; GO:0042310; P:vasoconstriction; IEA:UniProtKB-KW.
DR   InterPro; IPR020475; Endothelin.
DR   InterPro; IPR019764; Endothelin_toxin_CS.
DR   InterPro; IPR001928; Endothln-like_toxin.
DR   PANTHER; PTHR13874; ENDOTHELIN; 1.
DR   Pfam; PF00322; Endothelin; 7.
DR   PRINTS; PR00365; ENDOTHELIN.
DR   SMART; SM00272; END; 7.
DR   PROSITE; PS00270; ENDOTHELIN; 7.
PE   1: Evidence at protein level;
KW   3D-structure; Cardiotoxin; Direct protein sequencing; Disulfide bond;
KW   G-protein coupled receptor impairing toxin; Repeat; Secreted; Toxin;
KW   Vasoactive; Vasoconstrictor.
FT   PEPTIDE         <1..5
FT                   /note="Sarafotoxin-m5"
FT                   /id="PRO_0000315373"
FT   PROPEP          6..29
FT                   /evidence="ECO:0000269|PubMed:15350691"
FT                   /id="PRO_0000315374"
FT   PEPTIDE         30..53
FT                   /note="Sarafotoxin-m"
FT                   /id="PRO_5000092481"
FT   PROPEP          54..77
FT                   /evidence="ECO:0000269|PubMed:15350691"
FT                   /id="PRO_0000315375"
FT   PEPTIDE         78..101
FT                   /note="Sarafotoxin-m1"
FT                   /id="PRO_5000092482"
FT   PROPEP          102..125
FT                   /evidence="ECO:0000269|PubMed:15350691"
FT                   /id="PRO_0000315376"
FT   PEPTIDE         126..149
FT                   /note="Sarafotoxin-m3"
FT                   /id="PRO_5000092483"
FT   PROPEP          150..173
FT                   /evidence="ECO:0000269|PubMed:15350691"
FT                   /id="PRO_0000315377"
FT   PEPTIDE         174..197
FT                   /note="Sarafotoxin-m2"
FT                   /id="PRO_5000092484"
FT   PROPEP          198..221
FT                   /evidence="ECO:0000269|PubMed:15350691"
FT                   /id="PRO_0000315378"
FT   PEPTIDE         222..245
FT                   /note="Sarafotoxin-m2"
FT                   /id="PRO_5000092485"
FT   PROPEP          246..269
FT                   /evidence="ECO:0000269|PubMed:15350691"
FT                   /id="PRO_0000315379"
FT   PEPTIDE         270..293
FT                   /note="Sarafotoxin-m"
FT                   /id="PRO_5000092486"
FT   PROPEP          294..317
FT                   /evidence="ECO:0000269|PubMed:15350691"
FT                   /id="PRO_0000315380"
FT   PEPTIDE         318..341
FT                   /note="Sarafotoxin-m4"
FT                   /id="PRO_5000092487"
FT   PROPEP          342..351
FT                   /id="PRO_0000315381"
FT   REPEAT          6..53
FT                   /note="1"
FT   REPEAT          54..101
FT                   /note="2"
FT   REPEAT          102..149
FT                   /note="3"
FT   REPEAT          150..197
FT                   /note="4"
FT   REPEAT          198..245
FT                   /note="5"
FT   REPEAT          246..293
FT                   /note="6"
FT   REPEAT          294..341
FT                   /note="7"
FT   REGION          6..341
FT                   /note="7 X 48 AA tandem repeats"
FT   SITE            2
FT                   /note="Endothelin-receptor binding site"
FT                   /evidence="ECO:0000250"
FT   SITE            50
FT                   /note="Endothelin-receptor binding site"
FT                   /evidence="ECO:0000250"
FT   SITE            98
FT                   /note="Endothelin-receptor binding site"
FT                   /evidence="ECO:0000250"
FT   SITE            146
FT                   /note="Endothelin-receptor binding site"
FT                   /evidence="ECO:0000250"
FT   SITE            194
FT                   /note="Endothelin-receptor binding site"
FT                   /evidence="ECO:0000250"
FT   SITE            242
FT                   /note="Endothelin-receptor binding site"
FT                   /evidence="ECO:0000250"
FT   SITE            290
FT                   /note="Endothelin-receptor binding site"
FT                   /evidence="ECO:0000250"
FT   SITE            338
FT                   /note="Endothelin-receptor binding site"
FT                   /evidence="ECO:0000250"
FT   DISULFID        30..44
FT                   /evidence="ECO:0000269|PubMed:21889567"
FT   DISULFID        32..40
FT                   /evidence="ECO:0000269|PubMed:21889567"
FT   DISULFID        78..92
FT                   /evidence="ECO:0000250"
FT   DISULFID        80..88
FT                   /evidence="ECO:0000250"
FT   DISULFID        126..140
FT                   /evidence="ECO:0000250"
FT   DISULFID        128..136
FT                   /evidence="ECO:0000250"
FT   DISULFID        174..188
FT                   /evidence="ECO:0000250"
FT   DISULFID        176..184
FT                   /evidence="ECO:0000250"
FT   DISULFID        222..236
FT                   /evidence="ECO:0000250"
FT   DISULFID        224..232
FT                   /evidence="ECO:0000250"
FT   DISULFID        270..284
FT                   /evidence="ECO:0000250"
FT   DISULFID        272..280
FT                   /evidence="ECO:0000250"
FT   DISULFID        318..332
FT                   /evidence="ECO:0000250"
FT   DISULFID        320..328
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         51..53
FT                   /note="Missing: Drastic 4-orders or magnitude increase in
FT                   affinity for ET-B receptors."
FT                   /evidence="ECO:0000269|PubMed:21889567"
FT   NON_TER         1
FT   STRAND          273..275
FT                   /evidence="ECO:0007829|PDB:2LDF"
FT   HELIX           277..286
FT                   /evidence="ECO:0007829|PDB:2LDF"
SQ   SEQUENCE   351 AA;  40341 MW;  F901846C8D6E01CC CRC64;
     IWDEPVVVSA RDTEEAARVP SPQKRSQPLC SCNDINDKEC MYFCHQDVIW DEPVVVSVRD
     TEEAARVPSP QKRPQPRCSC NDMNDKECMY FCHQDVIWDE PVVVSVRDTE EAARVPSPQK
     RSQPRCSCND MNDKECVYFC HLDIIWDEPV VVSVRDTEEA TRVPSPQKRS QPLCSCNDIN
     DKECMYFCHQ DIIWDEPVVV SVRDTEEAAR VPSPQKRSQP LCSCNDINDK ECMYFCHQDI
     IWDEPVVVSV RDTEEAARVP SPQKRSQPLC SCNDINDKEC MYFCHQDVIW DEPVVVSVQD
     TEEAARVPSP QKRSQPLCSC NNMSDKECLN FCNLDIIWEN VDTSADPEFL G
//