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P29560 (EDN1_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 76. 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
Gene names
Name:EDN1
OrganismOryctolagus cuniculus (Rabbit) [Reference proteome]
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus

Protein attributes

Sequence length202 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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 componentSecreted
   DomainSignal
   Molecular functionVasoactive
Vasoconstrictor
   PTMCleavage on pair of basic residues
Disulfide bond
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbody fluid secretion

Inferred from electronic annotation. Source: Ensembl

calcium-mediated signaling

Inferred from electronic annotation. Source: Ensembl

cartilage development

Inferred from electronic annotation. Source: Ensembl

dorsal/ventral pattern formation

Inferred from electronic annotation. Source: Ensembl

glucose transport

Inferred from electronic annotation. Source: Ensembl

heart development

Inferred from electronic annotation. Source: Ensembl

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

inositol phosphate-mediated signaling

Inferred from electronic annotation. Source: Ensembl

middle ear morphogenesis

Inferred from electronic annotation. Source: Ensembl

negative regulation of cAMP biosynthetic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of cellular protein metabolic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of nitric-oxide synthase biosynthetic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

neural crest cell development

Inferred from electronic annotation. Source: Ensembl

nitric oxide transport

Inferred from electronic annotation. Source: Ensembl

patterning of blood vessels

Inferred from electronic annotation. Source: Ensembl

peptide hormone secretion

Inferred from electronic annotation. Source: Ensembl

phosphatidylinositol 3-kinase signaling

Inferred from electronic annotation. Source: Ensembl

phospholipase D-activating G-protein coupled receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of JUN kinase activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of cardiac muscle hypertrophy

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell migration

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell size

Inferred from electronic annotation. Source: Ensembl

positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G-protein coupled signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of heart rate

Inferred from electronic annotation. Source: Ensembl

positive regulation of hormone secretion

Inferred from electronic annotation. Source: Ensembl

positive regulation of mitosis

Inferred from electronic annotation. Source: Ensembl

positive regulation of prostaglandin-endoperoxide synthase activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of receptor biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of renal sodium excretion

Inferred from electronic annotation. Source: Ensembl

positive regulation of sarcomere organization

Inferred from electronic annotation. Source: Ensembl

positive regulation of smooth muscle cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of urine volume

Inferred from electronic annotation. Source: Ensembl

prostaglandin biosynthetic process

Inferred from electronic annotation. Source: Ensembl

protein kinase C deactivation

Inferred from electronic annotation. Source: Ensembl

protein kinase C-activating G-protein coupled receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

regulation of pH

Inferred from electronic annotation. Source: Ensembl

regulation of systemic arterial blood pressure by endothelin

Inferred from electronic annotation. Source: Ensembl

regulation of vasoconstriction

Inferred from electronic annotation. Source: InterPro

respiratory gaseous exchange

Inferred from electronic annotation. Source: Ensembl

response to hypoxia

Inferred from electronic annotation. Source: Ensembl

rhythmic excitation

Inferred from electronic annotation. Source: Ensembl

vein smooth muscle contraction

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: Ensembl

extracellular space

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Propeptide24 – 5027
PRO_0000008069
Peptide53 – 7321Endothelin-1
PRO_0000008070
Propeptide74 – 202129
PRO_0000008071

Regions

Region110 – 12415Endothelin-like

Sites

Site73 – 742Cleavage; by KEL By similarity

Amino acid modifications

Disulfide bond53 ↔ 67 By similarity
Disulfide bond55 ↔ 63 By similarity

Sequences

Sequence LengthMass (Da)Tools
P29560 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: 22B41EA286D51286

FASTA20222,828
        10         20         30         40         50         60 
MDYFSMMVSL LLVAFHGAPE TAASGTELST GAENPGEKPP ASAPWRPRRS KRCSCSSLMD 

        70         80         90        100        110        120 
KECVYFCHLD IIWVNTPGHI VPYGLGSPSR SKRSLKDLFP TRAAYHKNRC QCTSPHDKKC 

       130        140        150        160        170        180 
WNFCQAGTEL RAQETMEKGR NNLKKGKDCS KLGKKCILQK LMQGRKIRRL EAISNSIKTS 

       190        200 
FHAAQLRAQL HREQKVTHNR TH 

« Hide

References

[1]"Nucleotide sequence of endothelin-1 cDNA from rabbit endothelial cells."
Marsden P.A., Sultan P., Cybulsky M., Gimbrone M.A. Jr., Brenner B.M., Collins T.
Biochim. Biophys. Acta 1129:249-250(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X59931 mRNA. Translation: CAA42555.1.
PIRS20609.
RefSeqNP_001095166.1. NM_001101696.1.
UniGeneOcu.5758.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9986.ENSOCUP00000011526.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSOCUT00000013396; ENSOCUP00000011526; ENSOCUG00000013396.
GeneID100009270.

Organism-specific databases

CTD100009270.

Phylogenomic databases

eggNOGNOG46593.
GeneTreeENSGT00530000063310.
HOGENOMHOG000231110.
HOVERGENHBG051441.
OMARCQCASQ.
OrthoDBEOG7PS1H7.
TreeFamTF333184.

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_RABIT
AccessionPrimary (citable) accession number: P29560
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: February 19, 2014
This is version 76 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