EDN1_PIG
ID EDN1_PIG Reviewed; 203 AA.
AC P09558;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=Endothelin-1;
DE Short=ET-1;
DE AltName: Full=Preproendothelin-1;
DE Short=PPET1;
DE Contains:
DE RecName: Full=Big endothelin-1;
DE Flags: Precursor;
GN Name=EDN1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 53-73, FUNCTION, AND
RP DISULFIDE BOND.
RC TISSUE=Endothelial cell;
RX PubMed=2451132; DOI=10.1038/332411a0;
RA Yanagisawa M., Kurihara H., Kimura S., Tomobe Y., Kobayashi M., Mitsui Y.,
RA Yasaki Y., Goto K., Masaki T.;
RT "A novel potent vasoconstrictor peptide produced by vascular endothelial
RT cells.";
RL Nature 332:411-415(1988).
RN [2]
RP PROTEIN SEQUENCE OF 53-82.
RC TISSUE=Endothelial cell;
RX PubMed=2669747; DOI=10.1016/0006-291x(89)90813-9;
RA Sawamura T., Kimura S., Shinmi O., Sugita Y., Yanagisawa M., Masaki T.;
RT "Analysis of endothelin related peptides in culture supernatant of porcine
RT aortic endothelial cells: evidence for biosynthetic pathway of endothelin-
RT 1.";
RL Biochem. Biophys. Res. Commun. 162:1287-1294(1989).
RN [3]
RP PROTEIN SEQUENCE OF 53-82.
RC TISSUE=Endothelial cell;
RX PubMed=2665739; DOI=10.1016/0006-291x(89)92001-9;
RA Shinmi O., Kimura S., Yoshizawa T., Sawamura T., Uchiyama Y., Sugita Y.,
RA Kanazawa I., Yanagisawa M., Goto K., Masaki T.;
RT "Presence of endothelin-1 in porcine spinal cord: isolation and sequence
RT determination.";
RL Biochem. Biophys. Res. Commun. 162:340-346(1989).
RN [4]
RP DEGRADATION BY CHYMOTRYPSIN.
RX PubMed=2205205; DOI=10.1042/bj2700541;
RA Takaoka M., Miyata Y., Takenobu Y., Ikegawa R., Matsumura Y., Morimoto S.;
RT "Mode of cleavage of pig big endothelin-1 by chymotrypsin. Production and
RT degradation of mature endothelin-1.";
RL Biochem. J. 270:541-544(1990).
CC -!- FUNCTION: Endothelins are endothelium-derived vasoconstrictor peptides
CC (PubMed:2451132). Probable ligand for G-protein coupled receptors EDNRA
CC and EDNRB which activates PTK2B, BCAR1, BCAR3 and, GTPases RAP1 and
CC RHOA cascade in glomerular mesangial cells (By similarity). Also binds
CC the DEAR/FBXW7-AS1 receptor (By similarity).
CC {ECO:0000250|UniProtKB:P05305, ECO:0000269|PubMed:2451132}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the endothelin/sarafotoxin family.
CC {ECO:0000305}.
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DR EMBL; X07383; CAA30296.1; -; mRNA.
DR PIR; S03159; ANPG.
DR RefSeq; NP_999047.1; NM_213882.1.
DR AlphaFoldDB; P09558; -.
DR BMRB; P09558; -.
DR STRING; 9823.ENSSSCP00000001121; -.
DR PaxDb; P09558; -.
DR Ensembl; ENSSSCT00065037539; ENSSSCP00065015808; ENSSSCG00065027852.
DR GeneID; 396915; -.
DR KEGG; ssc:396915; -.
DR CTD; 1906; -.
DR eggNOG; ENOG502S1NV; Eukaryota.
DR InParanoid; P09558; -.
DR OrthoDB; 1264335at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0031707; F:endothelin A receptor binding; IBA:GO_Central.
DR GO; GO:0031708; F:endothelin B receptor binding; IBA:GO_Central.
DR GO; GO:0005179; F:hormone activity; IBA:GO_Central.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IBA:GO_Central.
DR GO; GO:0086100; P:endothelin receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0060585; P:positive regulation of prostaglandin-endoperoxide synthase activity; IBA:GO_Central.
DR GO; GO:0003100; P:regulation of systemic arterial blood pressure by endothelin; IBA:GO_Central.
DR GO; GO:0019229; P:regulation of vasoconstriction; IEA:InterPro.
DR GO; GO:0014826; P:vein smooth muscle contraction; IBA:GO_Central.
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 1: Evidence at protein level;
KW Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Reference proteome; Secreted; Signal;
KW Vasoactive; Vasoconstrictor.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT PROPEP 26..50
FT /evidence="ECO:0000250|UniProtKB:P22388"
FT /id="PRO_0000008065"
FT PEPTIDE 53..82
FT /note="Big endothelin-1"
FT /evidence="ECO:0000269|PubMed:2665739,
FT ECO:0000269|PubMed:2669747"
FT /id="PRO_0000008066"
FT PEPTIDE 53..73
FT /note="Endothelin-1"
FT /evidence="ECO:0000269|PubMed:2451132"
FT /id="PRO_0000008067"
FT PROPEP 83..203
FT /id="PRO_0000008068"
FT REGION 27..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 110..124
FT /note="Endothelin-like"
FT SITE 73..74
FT /note="Cleavage; by KEL"
FT /evidence="ECO:0000250|UniProtKB:P05305"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 53..67
FT /evidence="ECO:0000269|PubMed:2451132"
FT DISULFID 55..63
FT /evidence="ECO:0000269|PubMed:2451132"
SQ SEQUENCE 203 AA; 23259 MW; AE47E7A8634B157D CRC64;
MDYFPMIIAL LFVAFQGAPE TAVLGAELSP EAESQGETPS PHASWRPRRS KRCSCSSLMD
KECVYFCHLD IIWVNTPEHI VPYGLGSPSR SRRSLKDLFP AKAADRRDRC QCASQKDKKC
WSFCQAGKEI GRDQDTMEKR WDNQKKGTDC SKLGEKCIHR QLVMGRKIRR LEAISNSIKT
SFHIAKLKAE LYRDKKVTHN RTH
