EDN2_ATEAB
ID EDN2_ATEAB Reviewed; 180 AA.
AC Q5NRP8;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 53.
DE RecName: Full=Endothelin-2;
DE Short=ET-2;
DE AltName: Full=Preproendothelin-2;
DE Short=PPET2;
DE Flags: Precursor;
GN Name=EDN2;
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-2 cDNA.";
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Endothelins are endothelium-derived vasoconstrictor peptides.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the endothelin/sarafotoxin family.
CC {ECO:0000305}.
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DR EMBL; AB197701; BAD83373.1; -; mRNA.
DR AlphaFoldDB; Q5NRP8; -.
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; Secreted; Signal;
KW Vasoactive; Vasoconstrictor.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT PROPEP 27..47
FT /evidence="ECO:0000250"
FT /id="PRO_0000008078"
FT PEPTIDE 50..70
FT /note="Endothelin-2"
FT /id="PRO_0000008079"
FT PROPEP 71..180
FT /evidence="ECO:0000250"
FT /id="PRO_0000008080"
FT REGION 97..112
FT /note="Endothelin-like"
FT REGION 157..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 70..71
FT /note="Cleavage; by KEL"
FT /evidence="ECO:0000250"
FT DISULFID 50..64
FT /evidence="ECO:0000250"
FT DISULFID 52..60
FT /evidence="ECO:0000250"
SQ SEQUENCE 180 AA; 20382 MW; 08BBC520F8CFC753 CRC64;
MVALPTAWCS VALALLVALH EGKSQSAATS EEPPAPSARA RGSHLRLRRC SCNSWLDKEC
VYFCHLDIIW VNTPGQTAPY GLGNPPRRQR RSLPRRCECY STRDSACVTF CHQKPWPKAS
AVPGEGSPTD LLWTSKTRTT AGELLRRLRD IFAAKRNFTR HQQQKATREP ESSHSRWRKR