ID   EDN2_HORSE              Reviewed;         178 AA.
AC   Q867D0;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Endothelin-2;
DE            Short=ET-2;
DE   AltName: Full=Preproendothelin-2;
DE            Short=PPET2;
DE   Flags: Precursor;
GN   Name=EDN2;
OS   Equus caballus (Horse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=15838341; DOI=10.1097/01.fjc.0000166312.53506.06;
RA   Uchide T., Fujimori Y., Temma K., Sasaki T., Kizaki K., Hara Y.,
RA   Takizawa S., Saida K.;
RT   "cDNA cloning, sequence analysis and organ distribution of horse
RT   preproendothelin-2.";
RL   J. Cardiovasc. Pharmacol. 44:S430-S434(2004).
CC   -!- FUNCTION: Endothelins are endothelium-derived vasoconstrictor peptides.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the endothelin/sarafotoxin family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB079136; BAC54893.1; -; mRNA.
DR   RefSeq; NP_001075292.1; NM_001081823.2.
DR   AlphaFoldDB; Q867D0; -.
DR   STRING; 9796.ENSECAP00000042152; -.
DR   PRIDE; Q867D0; -.
DR   Ensembl; ENSECAT00000024760; ENSECAP00000020586; ENSECAG00000023173.
DR   GeneID; 100033847; -.
DR   KEGG; ecb:100033847; -.
DR   CTD; 1907; -.
DR   VGNC; VGNC:58625; EDN2.
DR   GeneTree; ENSGT00950000183053; -.
DR   InParanoid; Q867D0; -.
DR   OrthoDB; 1264335at2759; -.
DR   Proteomes; UP000002281; Chromosome 2.
DR   Bgee; ENSECAG00000023173; Expressed in zone of skin and 6 other tissues.
DR   GO; GO:0005615; C:extracellular space; 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: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   InterPro; IPR015658; ET-2.
DR   PANTHER; PTHR13874; PTHR13874; 1.
DR   PANTHER; PTHR13874:SF9; PTHR13874:SF9; 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..24
FT                   /evidence="ECO:0000255"
FT   PROPEP          25..46
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000008087"
FT   PEPTIDE         49..69
FT                   /note="Endothelin-2"
FT                   /id="PRO_0000008088"
FT   PROPEP          70..178
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000008089"
FT   REGION          25..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          96..111
FT                   /note="Endothelin-like"
FT   SITE            69..70
FT                   /note="Cleavage; by KEL"
FT                   /evidence="ECO:0000250"
FT   DISULFID        49..63
FT                   /evidence="ECO:0000250"
FT   DISULFID        51..59
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   178 AA;  19795 MW;  815C39BA0B891634 CRC64;
     MVAMPPAWCS VALALLVALH EGEGQATATP EQPVPSPRAQ GSHLRPRRCS CSSWLDKECV
     YFCHLDIIWV NTPGQTAPYG LGNPPRRRRR SLPRRCECSS ARDPACATFC HRRPWADAVA
     VPGSDSPEDT FQAGKTWTTA GELLQQLRGI SAANIRFARR QQEAIRAPRP TPSRRRKR