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EDN2_RABIT
ID   EDN2_RABIT              Reviewed;         178 AA.
AC   Q765Z5;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Endothelin-2;
DE            Short=ET-2;
DE   AltName: Full=Preproendothelin-2;
DE            Short=PPET2;
DE   Flags: Precursor;
GN   Name=EDN2;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Uchide T.;
RT   "Cloning and sequencing of complete cDNA of rabbit preproendothelin-2.";
RL   Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
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; AB115085; BAD07478.1; -; mRNA.
DR   RefSeq; NP_001075481.1; NM_001082012.1.
DR   AlphaFoldDB; Q765Z5; -.
DR   STRING; 9986.ENSOCUP00000001041; -.
DR   GeneID; 100008634; -.
DR   KEGG; ocu:100008634; -.
DR   CTD; 1907; -.
DR   eggNOG; ENOG502S5KM; Eukaryota.
DR   InParanoid; Q765Z5; -.
DR   OrthoDB; 1264335at2759; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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   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_0000008102"
FT   PEPTIDE         49..69
FT                   /note="Endothelin-2"
FT                   /id="PRO_0000008103"
FT   PROPEP          70..178
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000008104"
FT   REGION          96..111
FT                   /note="Endothelin-like"
FT   REGION          154..178
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        154..170
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;  19644 MW;  F9AC9AACE9D7BA67 CRC64;
     MVSVPTAWCS VALALLVALH EGKDQAAATL EQPASSPRAR AAHLRLRRCS CSSWLDKECV
     YFCHLDIIWV NTPGQTAPYG LGNPPRRRRR SLPGRCECSS ARDPACATFC HQRSRADAVG
     VPGSQSSADA FQAGKTWATP GELLRTLRDI SAAKTHFAKR QQEATREPRT THSRHRKR
 
 
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