ID   EDN2_MUSPF              Reviewed;         178 AA.
AC   Q8MJW9;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Endothelin-2;
DE            Short=ET-2;
DE   AltName: Full=Preproendothelin-2;
DE            Short=PPET2;
DE   Flags: Precursor;
GN   Name=EDN2;
OS   Mustela putorius furo (European domestic ferret) (Mustela furo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Mustelidae; Mustelinae;
OC   Mustela.
OX   NCBI_TaxID=9669;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Intestine;
RX   PubMed=12652909; DOI=10.1080/1042517021000060786;
RA   Uchide T., Fujimori Y., Sasaki T., Temma K., Lee Y.S., Saida K.;
RT   "cDNA and deduced amino acid sequences of ferret preproendothelin-2 and
RT   phylogenetic analysis.";
RL   DNA Seq. 13:369-374(2002).
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; AB079607; BAC06584.1; -; mRNA.
DR   RefSeq; NP_001297108.1; NM_001310179.1.
DR   AlphaFoldDB; Q8MJW9; -.
DR   STRING; 9668.ENSMPUP00000013968; -.
DR   Ensembl; ENSMPUT00000014191; ENSMPUP00000013968; ENSMPUG00000014076.
DR   GeneID; 101689173; -.
DR   CTD; 1907; -.
DR   eggNOG; ENOG502S5KM; Eukaryota.
DR   GeneTree; ENSGT00950000183053; -.
DR   HOGENOM; CLU_090013_2_1_1; -.
DR   InParanoid; Q8MJW9; -.
DR   OMA; PTAWCSV; -.
DR   Proteomes; UP000000715; Unassembled WGS sequence.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR   GO; GO:0031708; F:endothelin B receptor binding; IEA:Ensembl.
DR   GO; GO:0005179; F:hormone activity; IEA:Ensembl.
DR   GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
DR   GO; GO:0014824; P:artery smooth muscle contraction; IEA:Ensembl.
DR   GO; GO:0048675; P:axon extension; IEA:Ensembl.
DR   GO; GO:0019722; P:calcium-mediated signaling; IEA:Ensembl.
DR   GO; GO:0009932; P:cell tip growth; IEA:Ensembl.
DR   GO; GO:0019221; P:cytokine-mediated signaling pathway; IEA:Ensembl.
DR   GO; GO:0043542; P:endothelial cell migration; IEA:Ensembl.
DR   GO; GO:0097009; P:energy homeostasis; IEA:Ensembl.
DR   GO; GO:0048016; P:inositol phosphate-mediated signaling; IEA:Ensembl.
DR   GO; GO:0048286; P:lung alveolus development; IEA:Ensembl.
DR   GO; GO:0042116; P:macrophage activation; IEA:Ensembl.
DR   GO; GO:0048246; P:macrophage chemotaxis; IEA:Ensembl.
DR   GO; GO:0030593; P:neutrophil chemotaxis; IEA:Ensembl.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
DR   GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IEA:Ensembl.
DR   GO; GO:0010460; P:positive regulation of heart rate; IEA:Ensembl.
DR   GO; GO:0002690; P:positive regulation of leukocyte chemotaxis; IEA:Ensembl.
DR   GO; GO:0060585; P:positive regulation of prostaglandin-endoperoxide synthase activity; IEA:Ensembl.
DR   GO; GO:0045987; P:positive regulation of smooth muscle contraction; IEA:Ensembl.
DR   GO; GO:0001516; P:prostaglandin biosynthetic process; IEA:Ensembl.
DR   GO; GO:0003100; P:regulation of systemic arterial blood pressure by endothelin; IEA:Ensembl.
DR   GO; GO:0019229; P:regulation of vasoconstriction; IEA:InterPro.
DR   GO; GO:0001659; P:temperature homeostasis; IEA:Ensembl.
DR   GO; GO:0014826; P:vein smooth muscle contraction; IEA:Ensembl.
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_0000008096"
FT   PEPTIDE         49..69
FT                   /note="Endothelin-2"
FT                   /id="PRO_0000008097"
FT   PROPEP          70..178
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000008098"
FT   REGION          96..111
FT                   /note="Endothelin-like"
FT   REGION          158..178
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        158..172
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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;  19909 MW;  A05FE2A061CC7DB6 CRC64;
     MVAVPTAWCS VALALLLALQ EGKGQVAAAP DHPAPSPRAR GSHLRPRRCS CSSWLDKECV
     YFCHLDIIWV NTPGQTAPYG LGNPPRRRRR SLPKRCECSS SGDPACATFC HRRPWAEAVV
     VPGSRSPADV FQAGQRWTSA GELLQQLREI SATKIRFARQ HQEAEREPRP MYPRRRKT