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Protein

Long-sarafotoxin

Gene
N/A
Organism
Atractaspis microlepidota microlepidota
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Vasoconstrictor activity. These toxins cause cardiac arrest probably as a result of coronary vasospasm. The major effects of sarafotoxin-m are a progressive decrease in heart rate (bradycardia) that turns into an arrhythmic phase that is followed by an A-V block.1 Publication
Sarafotoxin-m: vasoconstrictor activity. Causes cardiac arrest probably as a result of coronary vasospasm (By similarity). Displays low agonistic activities towards endothelin-2 receptor (EDNRB) (displays affinity in the micromolar range) (PubMed:21889567).By similarity2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei2Endothelin-receptor binding siteBy similarity1
Sitei50Endothelin-receptor binding siteBy similarity1
Sitei98Endothelin-receptor binding siteBy similarity1
Sitei146Endothelin-receptor binding siteBy similarity1
Sitei194Endothelin-receptor binding siteBy similarity1
Sitei242Endothelin-receptor binding siteBy similarity1
Sitei290Endothelin-receptor binding siteBy similarity1
Sitei338Endothelin-receptor binding siteBy similarity1

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Cardiotoxin, G-protein coupled receptor impairing toxin, Toxin, Vasoactive, Vasoconstrictor

Names & Taxonomyi

Protein namesi
Recommended name:
Long-sarafotoxin
Short name:
L-SRTX
Cleaved into the following 6 chains:
Sarafotoxin-m
Short name:
SRTX-m
Sarafotoxin-m1
Short name:
SRTX-m1
Sarafotoxin-m2
Short name:
SRTX-m2
Sarafotoxin-m3
Short name:
SRTX-m3
Sarafotoxin-m4
Short name:
SRTX-m4
Sarafotoxin-m5
Short name:
SRTX-m5
OrganismiAtractaspis microlepidota microlepidota
Taxonomic identifieri172021 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaLamprophiidaeAtractaspidinaeAtractaspis

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Toxic dosei

Sarafotoxin-m: LD50 is 27-37 µg/kg by intravenous injection into mice.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi51 – 53Missing : Drastic 4-orders or magnitude increase in affinity for ET-B receptors. 1 Publication3

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PeptideiPRO_0000315373‹1 – 5Sarafotoxin-m5›5
PropeptideiPRO_00003153746 – 291 PublicationAdd BLAST24
PeptideiPRO_500009248130 – 53Sarafotoxin-mAdd BLAST24
PropeptideiPRO_000031537554 – 771 PublicationAdd BLAST24
PeptideiPRO_500009248278 – 101Sarafotoxin-m1Add BLAST24
PropeptideiPRO_0000315376102 – 1251 PublicationAdd BLAST24
PeptideiPRO_5000092483126 – 149Sarafotoxin-m3Add BLAST24
PropeptideiPRO_0000315377150 – 1731 PublicationAdd BLAST24
PeptideiPRO_5000092484174 – 197Sarafotoxin-m2Add BLAST24
PropeptideiPRO_0000315378198 – 2211 PublicationAdd BLAST24
PeptideiPRO_5000092485222 – 245Sarafotoxin-m2Add BLAST24
PropeptideiPRO_0000315379246 – 2691 PublicationAdd BLAST24
PeptideiPRO_5000092486270 – 293Sarafotoxin-mAdd BLAST24
PropeptideiPRO_0000315380294 – 3171 PublicationAdd BLAST24
PeptideiPRO_5000092487318 – 341Sarafotoxin-m4Add BLAST24
PropeptideiPRO_0000315381342 – 35110

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi30 ↔ 441 Publication
Disulfide bondi32 ↔ 401 Publication
Disulfide bondi78 ↔ 92By similarity
Disulfide bondi80 ↔ 88By similarity
Disulfide bondi126 ↔ 140By similarity
Disulfide bondi128 ↔ 136By similarity
Disulfide bondi174 ↔ 188By similarity
Disulfide bondi176 ↔ 184By similarity
Disulfide bondi222 ↔ 236By similarity
Disulfide bondi224 ↔ 232By similarity
Disulfide bondi270 ↔ 284By similarity
Disulfide bondi272 ↔ 280By similarity
Disulfide bondi318 ↔ 332By similarity
Disulfide bondi320 ↔ 328By similarity

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Expressed by the venom gland.1 Publication

Structurei

Secondary structure

1351
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi273 – 275Combined sources3
Helixi277 – 286Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2LDFNMR-A270-293[»]
SMRiQ6RY98.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ6RY98.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati6 – 531Add BLAST48
Repeati54 – 1012Add BLAST48
Repeati102 – 1493Add BLAST48
Repeati150 – 1974Add BLAST48
Repeati198 – 2455Add BLAST48
Repeati246 – 2936Add BLAST48
Repeati294 – 3417Add BLAST48

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni6 – 3417 X 48 AA tandem repeatsAdd BLAST336

Sequence similaritiesi

Belongs to the endothelin/sarafotoxin family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

HOVERGENiHBG017852.

Family and domain databases

InterProiIPR020475. Bibrotoxin/Sarafotoxin-D.
IPR019764. Endothelin_toxin_CS.
IPR001928. Endothln-like_toxin.
[Graphical view]
PfamiPF00322. Endothelin. 7 hits.
[Graphical view]
PRINTSiPR00365. ENDOTHELIN.
SMARTiSM00272. END. 7 hits.
[Graphical view]
PROSITEiPS00270. ENDOTHELIN. 7 hits.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q6RY98-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
IWDEPVVVSA RDTEEAARVP SPQKRSQPLC SCNDINDKEC MYFCHQDVIW
60 70 80 90 100
DEPVVVSVRD TEEAARVPSP QKRPQPRCSC NDMNDKECMY FCHQDVIWDE
110 120 130 140 150
PVVVSVRDTE EAARVPSPQK RSQPRCSCND MNDKECVYFC HLDIIWDEPV
160 170 180 190 200
VVSVRDTEEA TRVPSPQKRS QPLCSCNDIN DKECMYFCHQ DIIWDEPVVV
210 220 230 240 250
SVRDTEEAAR VPSPQKRSQP LCSCNDINDK ECMYFCHQDI IWDEPVVVSV
260 270 280 290 300
RDTEEAARVP SPQKRSQPLC SCNDINDKEC MYFCHQDVIW DEPVVVSVQD
310 320 330 340 350
TEEAARVPSP QKRSQPLCSC NNMSDKECLN FCNLDIIWEN VDTSADPEFL

G
Length:351
Mass (Da):40,341
Last modified:July 5, 2004 - v1
Checksum:iF901846C8D6E01CC
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY485934 mRNA. Translation: AAR84382.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY485934 mRNA. Translation: AAR84382.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2LDFNMR-A270-293[»]
SMRiQ6RY98.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG017852.

Miscellaneous databases

EvolutionaryTraceiQ6RY98.

Family and domain databases

InterProiIPR020475. Bibrotoxin/Sarafotoxin-D.
IPR019764. Endothelin_toxin_CS.
IPR001928. Endothln-like_toxin.
[Graphical view]
PfamiPF00322. Endothelin. 7 hits.
[Graphical view]
PRINTSiPR00365. ENDOTHELIN.
SMARTiSM00272. END. 7 hits.
[Graphical view]
PROSITEiPS00270. ENDOTHELIN. 7 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSRTXL_ATRMM
AccessioniPrimary (citable) accession number: Q6RY98
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 5, 2004
Last modified: November 30, 2016
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.