EDN3_RAT
ID EDN3_RAT Reviewed; 167 AA.
AC P13207;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 3.
DT 25-MAY-2022, entry version 126.
DE RecName: Full=Endothelin-3;
DE Short=ET-3;
DE AltName: Full=Preproendothelin-3;
DE Short=PPET3;
DE Flags: Precursor;
GN Name=Edn3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1378731; DOI=10.1016/s0006-291x(05)80849-6;
RA Shiba R., Sakurai T., Yamada G., Morimoto H., Saito A., Masaki T., Goto K.;
RT "Cloning and expression of rat preproendothelin-3 cDNA.";
RL Biochem. Biophys. Res. Commun. 186:588-594(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 48-77.
RX PubMed=3045827; DOI=10.1073/pnas.85.18.6964;
RA Yanagisawa M., Inoue A., Ishikawa T., Kasuya Y., Kimura S., Kumagaye S.,
RA Nakajima K., Watanabe T.X., Sakakibara S., Goto K., Masaki T.;
RT "Primary structure, synthesis, and biological activity of rat endothelin,
RT an endothelium-derived vasoconstrictor peptide.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:6964-6967(1988).
CC -!- FUNCTION: Endothelins are endothelium-derived vasoconstrictor peptides.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the endothelin/sarafotoxin family.
CC {ECO:0000305}.
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DR EMBL; S39779; AAB22502.1; -; mRNA.
DR EMBL; J04075; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; JC1102; JC1102.
DR RefSeq; NP_001071118.1; NM_001077650.1.
DR AlphaFoldDB; P13207; -.
DR BMRB; P13207; -.
DR STRING; 10116.ENSRNOP00000009826; -.
DR PaxDb; P13207; -.
DR GeneID; 366270; -.
DR KEGG; rno:366270; -.
DR UCSC; RGD:2534; rat.
DR CTD; 1908; -.
DR RGD; 2534; Edn3.
DR eggNOG; ENOG502S4W0; Eukaryota.
DR InParanoid; P13207; -.
DR OrthoDB; 1264335at2759; -.
DR PhylomeDB; P13207; -.
DR Reactome; R-RNO-375276; Peptide ligand-binding receptors.
DR Reactome; R-RNO-416476; G alpha (q) signalling events.
DR PRO; PR:P13207; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:0031705; F:bombesin receptor binding; TAS:RGD.
DR GO; GO:0031708; F:endothelin B receptor binding; ISO:RGD.
DR GO; GO:0005179; F:hormone activity; ISO:RGD.
DR GO; GO:0048675; P:axon extension; ISO:RGD.
DR GO; GO:0007411; P:axon guidance; ISO:RGD.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; ISO:RGD.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; ISO:RGD.
DR GO; GO:0010961; P:cellular magnesium ion homeostasis; ISO:RGD.
DR GO; GO:0048016; P:inositol phosphate-mediated signaling; ISO:RGD.
DR GO; GO:0030318; P:melanocyte differentiation; ISO:RGD.
DR GO; GO:0046888; P:negative regulation of hormone secretion; IDA:RGD.
DR GO; GO:0001755; P:neural crest cell migration; ISO:RGD.
DR GO; GO:0030182; P:neuron differentiation; ISO:RGD.
DR GO; GO:0031175; P:neuron projection development; ISO:RGD.
DR GO; GO:0030593; P:neutrophil chemotaxis; ISO:RGD.
DR GO; GO:0030072; P:peptide hormone secretion; ISO:RGD.
DR GO; GO:0045597; P:positive regulation of cell differentiation; ISO:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0010460; P:positive regulation of heart rate; ISO:RGD.
DR GO; GO:0046887; P:positive regulation of hormone secretion; ISO:RGD.
DR GO; GO:0002690; P:positive regulation of leukocyte chemotaxis; ISO:RGD.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; ISO:RGD.
DR GO; GO:0045840; P:positive regulation of mitotic nuclear division; ISO:RGD.
DR GO; GO:1901381; P:positive regulation of potassium ion transmembrane transport; ISO:RGD.
DR GO; GO:0060585; P:positive regulation of prostaglandin-endoperoxide synthase activity; IBA:GO_Central.
DR GO; GO:0030334; P:regulation of cell migration; ISO:RGD.
DR GO; GO:0048070; P:regulation of developmental pigmentation; ISO:RGD.
DR GO; GO:0010468; P:regulation of gene expression; ISO:RGD.
DR GO; GO:0046928; P:regulation of neurotransmitter secretion; IDA:RGD.
DR GO; GO:0003100; P:regulation of systemic arterial blood pressure by endothelin; ISO:RGD.
DR GO; GO:0019229; P:regulation of vasoconstriction; TAS:RGD.
DR GO; GO:0042310; P:vasoconstriction; ISO:RGD.
DR GO; GO:0014826; P:vein smooth muscle contraction; ISO:RGD.
DR InterPro; IPR020475; Endothelin.
DR InterPro; IPR019764; Endothelin_toxin_CS.
DR InterPro; IPR001928; Endothln-like_toxin.
DR PANTHER; PTHR13874; PTHR13874; 1.
DR Pfam; PF00322; Endothelin; 1.
DR PRINTS; PR00365; ENDOTHELIN.
DR SMART; SM00272; END; 2.
DR PROSITE; PS00270; ENDOTHELIN; 2.
PE 2: Evidence at transcript level;
KW Cleavage on pair of basic residues; Disulfide bond; Reference proteome;
KW Secreted; Signal; Vasoactive; Vasoconstrictor.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..50
FT /id="PRO_0000008120"
FT PEPTIDE 53..73
FT /note="Endothelin-3"
FT /id="PRO_0000008121"
FT PROPEP 74..167
FT /id="PRO_0000008122"
FT REGION 22..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..135
FT /note="Endothelin-like"
FT REGION 140..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 73..74
FT /note="Cleavage; by KEL"
FT /evidence="ECO:0000250"
FT DISULFID 53..67
FT /evidence="ECO:0000250"
FT DISULFID 55..63
FT /evidence="ECO:0000250"
SQ SEQUENCE 167 AA; 18453 MW; B219DA1D7C375DC2 CRC64;
MELGLWLLLG LTVTSAAAAL PAQPGNAGQE RGPGRSGDQE EKRVPAHHRP RRCTCFTYKD
KECVYYCHLD IIWINTPEQT VPYGLSNHRG SLRGKRSSGP VPESSQSSPQ TRLRCACSGV
DDKACAYFCA HVTSYSRRAE KAAAEEKQET GGPRQRLKSR TDKVHQP
