P09558 (EDN1_PIG) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Sus scrofa (Pig) [Reference proteome]

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length	203 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Vasoactive Vasoconstrictor
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	regulation of vasoconstriction Inferred from electronic annotation. Source: InterPro vasoconstriction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 25	25	Potential
	Propeptide	26 – 50	25			PRO_0000008065
	Peptide	53 – 82	30	Big endothelin-1 Ref.2 Ref.3		PRO_0000008066
	Peptide	53 – 73	21	Endothelin-1 Ref.1		PRO_0000008067
	Propeptide	83 – 203	121			PRO_0000008068
Regions
	Region	110 – 124	15	Endothelin-like
Sites
	Site	73 – 74	2	Cleavage; by KEL By similarity
Amino acid modifications
	Glycosylation	200	1	N-linked (GlcNAc...) Potential
	Disulfide bond	53 ↔ 67
	Disulfide bond	55 ↔ 63

Sequences

	Sequence		Length	Mass (Da)
	P09558 [UniParc]. Last modified July 1, 1989. Version 1. Checksum: AE47E7A8634B157D	FASTA	203	23,259
	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

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.
PIR	ANPG. S03159.
RefSeq	NP_999047.1. NM_213882.1.
UniGene	Ssc.9364.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	9823.ENSSSCP00000001121.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	396915.
KEGG	ssc:396915.
Organism-specific databases
CTD	1906.
Phylogenomic databases
eggNOG	NOG46593.
HOGENOM	HOG000231110.
HOVERGEN	HBG051441.
KO	K16366.
OrthoDB	EOG4QZ7N8.
Family and domain databases
InterPro	IPR020475. Bibrotoxin/Sarafotoxin-D. IPR019764. Endothelin_toxin_CS. IPR001928. Endothln-like_toxin. [Graphical view]
Pfam	PF00322. Endothelin. 1 hit. [Graphical view]
PRINTS	PR00365. ENDOTHELIN.
SMART	SM00272. END. 2 hits. [Graphical view]
PROSITE	PS00270. ENDOTHELIN. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

EDN1_PIG

Accession

Primary (citable) accession number: P09558

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	April 3, 2013
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program