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