ID   EDN1_ATEAB              Reviewed;         202 AA.
AC   Q5NRP9;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 45.
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   Atelerix albiventris (Middle-African hedgehog) (Four-toed hedgehog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae; Atelerix.
OX   NCBI_TaxID=9368;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Uchide T.;
RT   "Cloning of hedgehog preproendothelin-1 cDNA.";
RL   Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Endothelins are endothelium-derived vasoconstrictor peptides
CC       (By similarity). 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:0000250|UniProtKB:P09558}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the endothelin/sarafotoxin family.
CC       {ECO:0000305}.
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DR   EMBL; AB197700; BAD83372.1; -; mRNA.
DR   AlphaFoldDB; Q5NRP9; -.
DR   PRIDE; Q5NRP9; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0086100; P:endothelin receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0019229; P:regulation of vasoconstriction; IEA:InterPro.
DR   GO; GO:0042310; P:vasoconstriction; IEA:UniProtKB-KW.
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; 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_0000008043"
FT   PEPTIDE         53..91
FT                   /note="Big endothelin-1"
FT                   /evidence="ECO:0000250|UniProtKB:P22388"
FT                   /id="PRO_0000436392"
FT   PEPTIDE         53..73
FT                   /note="Endothelin-1"
FT                   /id="PRO_0000008044"
FT   PROPEP          74..202
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000008045"
FT   REGION          28..49
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   DISULFID        53..67
FT                   /evidence="ECO:0000250|UniProtKB:P05305"
FT   DISULFID        55..63
FT                   /evidence="ECO:0000250|UniProtKB:P05305"
SQ   SEQUENCE   202 AA;  23124 MW;  7661CA9EA4BF36AC CRC64;
     MDYFPMIFSL LFVAFHGAPE TVVLGAELST ESEQGGEQPS PSPPWRPRRS KRCSCSSLMD
     KECVYFCHLD IIWVNTPEHV VPYGLGSPLR SRRSLKNSFP TKAADHRNRC RCASQKDKKC
     WNFCQAGKGL RLQDTMEKDW NNQKKGKDCS KLGDKCIHQQ LVEGRKIRRL EAISNSIKTS
     FHIAKLKAEL YREKKVTHNG TH