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P09558 (EDN1_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Endothelin-1

Short name=ET-1
Alternative name(s):
Preproendothelin-1
Short name=PPET1

Cleaved into the following chain:

  1. Big endothelin-1
Gene names
Name:EDN1
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length203 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Endothelins are endothelium-derived vasoconstrictor peptides.

Subcellular location

Secreted.

Sequence similarities

Belongs to the endothelin/sarafotoxin family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Propeptide26 – 5025
PRO_0000008065
Peptide53 – 8230Big endothelin-1 Ref.2 Ref.3
PRO_0000008066
Peptide53 – 7321Endothelin-1 Ref.1
PRO_0000008067
Propeptide83 – 203121
PRO_0000008068

Regions

Region110 – 12415Endothelin-like

Sites

Site73 – 742Cleavage; by KEL By similarity

Amino acid modifications

Glycosylation2001N-linked (GlcNAc...) Potential
Disulfide bond53 ↔ 67
Disulfide bond55 ↔ 63

Sequences

Sequence LengthMass (Da)Tools
P09558 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: AE47E7A8634B157D

FASTA20323,259
        10         20         30         40         50         60 
MDYFPMIIAL LFVAFQGAPE TAVLGAELSP EAESQGETPS PHASWRPRRS KRCSCSSLMD 

        70         80         90        100        110        120 
KECVYFCHLD IIWVNTPEHI VPYGLGSPSR SRRSLKDLFP AKAADRRDRC QCASQKDKKC 

       130        140        150        160        170        180 
WSFCQAGKEI GRDQDTMEKR WDNQKKGTDC SKLGEKCIHR QLVMGRKIRR LEAISNSIKT 

       190        200 
SFHIAKLKAE LYRDKKVTHN RTH 

« Hide

References

[1]"A novel potent vasoconstrictor peptide produced by vascular endothelial cells."
Yanagisawa M., Kurihara H., Kimura S., Tomobe Y., Kobayashi M., Mitsui Y., Yasaki Y., Goto K., Masaki T.
Nature 332:411-415(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 53-73.
Tissue: Endothelial cell.
[2]"Analysis of endothelin related peptides in culture supernatant of porcine aortic endothelial cells: evidence for biosynthetic pathway of endothelin-1."
Sawamura T., Kimura S., Shinmi O., Sugita Y., Yanagisawa M., Masaki T.
Biochem. Biophys. Res. Commun. 162:1287-1294(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 53-82.
Tissue: Endothelial cell.
[3]"Presence of endothelin-1 in porcine spinal cord: isolation and sequence determination."
Shinmi O., Kimura S., Yoshizawa T., Sawamura T., Uchiyama Y., Sugita Y., Kanazawa I., Yanagisawa M., Goto K., Masaki T.
Biochem. Biophys. Res. Commun. 162:340-346(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 53-82.
Tissue: Endothelial cell.
[4]"Mode of cleavage of pig big endothelin-1 by chymotrypsin. Production and degradation of mature endothelin-1."
Takaoka M., Miyata Y., Takenobu Y., Ikegawa R., Matsumura Y., Morimoto S.
Biochem. J. 270:541-544(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: DEGRADATION BY CHYMOTRYPSIN.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X07383 mRNA. Translation: CAA30296.1.
PIRANPG. S03159.
RefSeqNP_999047.1. NM_213882.1.
UniGeneSsc.9364.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9823.ENSSSCP00000001121.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID396915.
KEGGssc:396915.

Organism-specific databases

CTD1906.

Phylogenomic databases

eggNOGNOG46593.
HOGENOMHOG000231110.
HOVERGENHBG051441.
KOK16366.

Family and domain databases

InterProIPR020475. Bibrotoxin/Sarafotoxin-D.
IPR019764. Endothelin_toxin_CS.
IPR001928. Endothln-like_toxin.
[Graphical view]
PfamPF00322. Endothelin. 1 hit.
[Graphical view]
PRINTSPR00365. ENDOTHELIN.
SMARTSM00272. END. 2 hits.
[Graphical view]
PROSITEPS00270. ENDOTHELIN. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameEDN1_PIG
AccessionPrimary (citable) accession number: P09558
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: November 13, 2013
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families