EDN3_MOUSE
ID EDN3_MOUSE Reviewed; 214 AA.
AC P48299; Q543L0;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Endothelin-3;
DE Short=ET-3;
DE AltName: Full=Preproendothelin-3;
DE Short=PPET3;
DE Flags: Precursor;
GN Name=Edn3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8001160; DOI=10.1016/0092-8674(94)90018-3;
RA Baynash A.G., Hosoda K., Giaid A., Richardson J.A., Emoto N., Hammer R.E.,
RA Yanagisawa M.;
RT "Interaction of endothelin-3 with endothelin-B receptor is essential for
RT development of epidermal melanocytes and enteric neurons.";
RL Cell 79:1277-1285(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head, and Spinal cord;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
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; U32330; AAB60509.1; -; mRNA.
DR EMBL; AK048006; BAC33211.1; -; mRNA.
DR EMBL; AK049775; BAC33915.1; -; mRNA.
DR EMBL; AK079150; BAC37561.1; -; mRNA.
DR CCDS; CCDS17156.1; -.
DR PIR; I49351; I49351.
DR RefSeq; NP_031929.1; NM_007903.5.
DR AlphaFoldDB; P48299; -.
DR BMRB; P48299; -.
DR STRING; 10090.ENSMUSP00000029030; -.
DR PhosphoSitePlus; P48299; -.
DR PaxDb; P48299; -.
DR PRIDE; P48299; -.
DR ProteomicsDB; 277683; -.
DR Antibodypedia; 29284; 302 antibodies from 30 providers.
DR DNASU; 13616; -.
DR Ensembl; ENSMUST00000029030; ENSMUSP00000029030; ENSMUSG00000027524.
DR GeneID; 13616; -.
DR KEGG; mmu:13616; -.
DR UCSC; uc008ofi.2; mouse.
DR CTD; 1908; -.
DR MGI; MGI:95285; Edn3.
DR VEuPathDB; HostDB:ENSMUSG00000027524; -.
DR eggNOG; ENOG502S4W0; Eukaryota.
DR GeneTree; ENSGT00950000183053; -.
DR InParanoid; P48299; -.
DR OMA; QPSKWTL; -.
DR OrthoDB; 1264335at2759; -.
DR PhylomeDB; P48299; -.
DR TreeFam; TF333184; -.
DR Reactome; R-MMU-375276; Peptide ligand-binding receptors.
DR Reactome; R-MMU-416476; G alpha (q) signalling events.
DR BioGRID-ORCS; 13616; 0 hits in 72 CRISPR screens.
DR PRO; PR:P48299; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P48299; protein.
DR Bgee; ENSMUSG00000027524; Expressed in iris and 130 other tissues.
DR ExpressionAtlas; P48299; baseline and differential.
DR Genevisible; P48299; MM.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0031708; F:endothelin B receptor binding; ISO:MGI.
DR GO; GO:0005179; F:hormone activity; ISO:MGI.
DR GO; GO:0048675; P:axon extension; IDA:MGI.
DR GO; GO:0007411; P:axon guidance; IMP:MGI.
DR GO; GO:0008283; P:cell population proliferation; IDA:MGI.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; ISO:MGI.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IGI:MGI.
DR GO; GO:0010961; P:cellular magnesium ion homeostasis; IGI:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IGI:MGI.
DR GO; GO:0048016; P:inositol phosphate-mediated signaling; ISO:MGI.
DR GO; GO:0030318; P:melanocyte differentiation; IDA:MGI.
DR GO; GO:0046888; P:negative regulation of hormone secretion; ISO:MGI.
DR GO; GO:0001755; P:neural crest cell migration; IMP:MGI.
DR GO; GO:0030182; P:neuron differentiation; IMP:MGI.
DR GO; GO:0031175; P:neuron projection development; IDA:MGI.
DR GO; GO:0030593; P:neutrophil chemotaxis; ISO:MGI.
DR GO; GO:0030072; P:peptide hormone secretion; ISO:MGI.
DR GO; GO:0045597; P:positive regulation of cell differentiation; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:MGI.
DR GO; GO:0010460; P:positive regulation of heart rate; ISO:MGI.
DR GO; GO:0046887; P:positive regulation of hormone secretion; ISO:MGI.
DR GO; GO:0002690; P:positive regulation of leukocyte chemotaxis; ISO:MGI.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; ISO:MGI.
DR GO; GO:0045840; P:positive regulation of mitotic nuclear division; ISO:MGI.
DR GO; GO:1901381; P:positive regulation of potassium ion transmembrane transport; IGI:MGI.
DR GO; GO:0060585; P:positive regulation of prostaglandin-endoperoxide synthase activity; IBA:GO_Central.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IGI:MGI.
DR GO; GO:0030334; P:regulation of cell migration; IMP:MGI.
DR GO; GO:0048070; P:regulation of developmental pigmentation; IMP:MGI.
DR GO; GO:0010468; P:regulation of gene expression; ISO:MGI.
DR GO; GO:0046928; P:regulation of neurotransmitter secretion; ISO:MGI.
DR GO; GO:0003100; P:regulation of systemic arterial blood pressure by endothelin; ISO:MGI.
DR GO; GO:0019229; P:regulation of vasoconstriction; IEA:InterPro.
DR GO; GO:0042310; P:vasoconstriction; ISO:MGI.
DR GO; GO:0014826; P:vein smooth muscle contraction; ISO:MGI.
DR InterPro; IPR020475; Endothelin.
DR InterPro; IPR019764; Endothelin_toxin_CS.
DR InterPro; IPR001928; Endothln-like_toxin.
DR PANTHER; PTHR13874; PTHR13874; 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..16
FT /evidence="ECO:0000255"
FT PROPEP 17..94
FT /id="PRO_0000008114"
FT PEPTIDE 97..117
FT /note="Endothelin-3"
FT /id="PRO_0000008115"
FT PROPEP 118..214
FT /id="PRO_0000008116"
FT REGION 24..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 159..173
FT /note="Endothelin-like"
FT REGION 183..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..214
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 117..118
FT /note="Cleavage; by KEL"
FT /evidence="ECO:0000250"
FT DISULFID 97..111
FT /evidence="ECO:0000250"
FT DISULFID 99..107
FT /evidence="ECO:0000250"
SQ SEQUENCE 214 AA; 23322 MW; 8911260872D6A713 CRC64;
MEPGLWLLLG LTVTSAAGLV PCPQSGDSGR ASVSQGPPEA GSERGCEETV AGPGERIVSP
TVALPAQPES AGQERAPGRS GKQEDKGLPA HHRPRRCTCF TYKDKECVYY CHLDIIWINT
PEQTVPYGLS NYRESLRGKR SLGPVPESSQ PSPWTRLRCT CMGADDKACA HFCARTRDVT
SYSGRAERPA AEEMRETGGP RQRLMSRTDK AHRP
