SRTXL_ATRMM
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 25-MAY-2022, entry version 54.
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}.
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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; PTHR13874; 7.
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
