PE2R3_HUMAN
ID PE2R3_HUMAN Reviewed; 390 AA.
AC P43115; B0AZN4; B1AK19; B5BUP5; O00326; Q12943; Q12944; Q12945; Q147X8;
AC Q16546; Q5CZ59; Q5CZ61; Q5CZ62; Q5CZ63; Q5CZ64;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=Prostaglandin E2 receptor EP3 subtype;
DE Short=PGE receptor EP3 subtype;
DE Short=PGE2 receptor EP3 subtype;
DE AltName: Full=PGE2-R;
DE AltName: Full=Prostanoid EP3 receptor;
GN Name=PTGER3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS EP3A; EP3B AND EP3C), FUNCTION, AND
RP SUBCELLULAR LOCATION.
RX PubMed=8307176; DOI=10.1016/0014-5793(94)80358-7;
RA Adam M., Boie Y., Rushmore T.H., Mueller G., Bastien L., McKee K.T.,
RA Metters K.M., Abramovitz M.;
RT "Cloning and expression of three isoforms of the human EP3 prostanoid
RT receptor.";
RL FEBS Lett. 338:170-174(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS EP3A; EP3B; EP3C; EP3D; EP3E AND
RP EP3F), FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Uterus;
RX PubMed=7883006; DOI=10.1111/j.1432-1033.1995.tb20223.x;
RA Schmid A., Thierauch K.H., Schleuning W.-D., Dinter H.;
RT "Splice variants of the human EP3 receptor for prostaglandin E2.";
RL Eur. J. Biochem. 228:23-30(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM EP3A), FUNCTION, SUBCELLULAR LOCATION,
RP AND TISSUE SPECIFICITY.
RC TISSUE=Kidney;
RX PubMed=8117308; DOI=10.1006/bbrc.1994.1142;
RA Yang J., Xia M., Goetzl E.J., An S.;
RT "Cloning and expression of the EP3-subtype of human receptors for
RT prostaglandin E2.";
RL Biochem. Biophys. Res. Commun. 198:999-1006(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM EP3A), FUNCTION, AND TISSUE
RP SPECIFICITY.
RX PubMed=8135729; DOI=10.1042/bj2980263;
RA Kunapuli S.P., Fen Mao G., Bastepe M., Liu-Chen L.-Y., Li S., Cheung P.P.,
RA DeRiel J.K., Ashby B.;
RT "Cloning and expression of a prostaglandin E receptor EP3 subtype from
RT human erythroleukaemia cells.";
RL Biochem. J. 298:263-267(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS EP3B; EP3C AND EP3D), FUNCTION, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Uterus;
RX PubMed=7981210; DOI=10.1021/bi00252a016;
RA An S., Yang J., So S.W., Zeng L., Goetzl E.J.;
RT "Isoforms of the EP3 subtype of human prostaglandin E2 receptor transduce
RT both intracellular calcium and cAMP signals.";
RL Biochemistry 33:14496-14502(1994).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS EP3A; EP3B; EP3C AND EP3D).
RC TISSUE=Kidney;
RX PubMed=7476918;
RA Kotani M., Tanaka I., Ogawa Y., Usui T., Mori K., Ichikawa A., Narumiya S.,
RA Yoshimi T., Nakao K.;
RT "Molecular cloning and expression of multiple isoforms of human
RT prostaglandin E receptor EP3 subtype generated by alternative messenger RNA
RT splicing: multiple second messenger systems and tissue-specific
RT distributions.";
RL Mol. Pharmacol. 48:869-879(1995).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS EP3A; EP3B; EP3C AND EP3D).
RC TISSUE=Small intestine;
RX PubMed=8075855; DOI=10.1111/j.1476-5381.1994.tb13082.x;
RA Regan J.W., Bailey T.J., Donello J.E., Pierce K.L., Pepperl D.J., Zhang D.,
RA Kedzie K.M., Fairbairn C.E., Bogardus A.M., Woodward D.F., Gil D.W.;
RT "Molecular cloning and expression of human EP3 receptors: evidence of three
RT variants with differing carboxyl termini.";
RL Br. J. Pharmacol. 112:377-385(1994).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS EP3C; EP3E; EP3-III;
RP EP3-IV; EP3-V AND EP3E2), AND ALTERNATIVE SPLICING.
RX PubMed=9073510; DOI=10.1006/geno.1996.4585;
RA Kotani M., Tanaka I., Ogawa Y., Usui T., Tamura N., Mori K., Narumiya S.,
RA Yoshimi T., Nakao K.;
RT "Structural organization of the human prostaglandin EP3 receptor subtype
RT gene (PTGER3).";
RL Genomics 40:425-434(1997).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM EP3G).
RC TISSUE=Placenta;
RA Kopatz S.A., Aronstam R.S., Sharma S.V.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM EP3A).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM EP3B).
RX PubMed=19054851; DOI=10.1038/nmeth.1273;
RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y.,
RA Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A.,
RA Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y.,
RA Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T.,
RA Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y.,
RA Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S.,
RA Nomura N.;
RT "Human protein factory for converting the transcriptome into an in vitro-
RT expressed proteome.";
RL Nat. Methods 5:1011-1017(2008).
RN [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [13]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [14]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS EP3D AND 12).
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [15]
RP TISSUE SPECIFICITY.
RX PubMed=18023986; DOI=10.1016/j.plefa.2007.09.005;
RA Kotelevets L., Foudi N., Louedec L., Couvelard A., Chastre E., Norel X.;
RT "A new mRNA splice variant coding for the human EP3-I receptor isoform.";
RL Prostaglandins Leukot. Essent. Fatty Acids 77:195-201(2007).
CC -!- FUNCTION: Receptor for prostaglandin E2 (PGE2) (PubMed:8307176,
CC PubMed:7883006, PubMed:8117308, PubMed:8135729, PubMed:7981210). The
CC activity of this receptor can couple to both the inhibition of
CC adenylate cyclase mediated by G(i) proteins, and to an elevation of
CC intracellular calcium (PubMed:7883006, PubMed:8117308, PubMed:8135729,
CC PubMed:7981210). Required for normal development of fever in response
CC to pyrinogens, including IL1B, prostaglandin E2 and bacterial
CC lipopolysaccharide (LPS). Required for normal potentiation of platelet
CC aggregation by prostaglandin E2, and thus plays a role in the
CC regulation of blood coagulation. Required for increased HCO3(-)
CC secretion in the duodenum in response to mucosal acidification, and
CC thereby contributes to the protection of the mucosa against acid-
CC induced ulceration. Not required for normal kidney function, normal
CC urine volume and osmolality (By similarity).
CC {ECO:0000250|UniProtKB:P30557, ECO:0000269|PubMed:7883006,
CC ECO:0000269|PubMed:7981210, ECO:0000269|PubMed:8117308,
CC ECO:0000269|PubMed:8135729, ECO:0000269|PubMed:8307176}.
CC -!- SUBUNIT: Interacts (via C-terminus) with MKLN1.
CC {ECO:0000250|UniProtKB:P34980}.
CC -!- INTERACTION:
CC P43115-12; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-10234038, EBI-10173507;
CC P43115-12; P32320: CDA; NbExp=3; IntAct=EBI-10234038, EBI-9250559;
CC P43115-12; O95967: EFEMP2; NbExp=3; IntAct=EBI-10234038, EBI-743414;
CC P43115-12; Q0VD86: INCA1; NbExp=3; IntAct=EBI-10234038, EBI-6509505;
CC P43115-12; Q15323: KRT31; NbExp=3; IntAct=EBI-10234038, EBI-948001;
CC P43115-12; O76015: KRT38; NbExp=3; IntAct=EBI-10234038, EBI-1047263;
CC P43115-12; Q6A162: KRT40; NbExp=3; IntAct=EBI-10234038, EBI-10171697;
CC P43115-12; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-10234038, EBI-10172290;
CC P43115-12; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-10234038, EBI-10171774;
CC P43115-12; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-10234038, EBI-10172052;
CC P43115-12; P50222: MEOX2; NbExp=3; IntAct=EBI-10234038, EBI-748397;
CC P43115-12; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-10234038, EBI-945833;
CC P43115-12; Q04864: REL; NbExp=3; IntAct=EBI-10234038, EBI-307352;
CC P43115-12; Q9UGC6: RGS17; NbExp=3; IntAct=EBI-10234038, EBI-3918154;
CC P43115-12; O76081: RGS20; NbExp=3; IntAct=EBI-10234038, EBI-1052678;
CC P43115-12; O76081-6: RGS20; NbExp=3; IntAct=EBI-10234038, EBI-10178530;
CC P43115-12; O43597: SPRY2; NbExp=3; IntAct=EBI-10234038, EBI-742487;
CC P43115-12; P15884: TCF4; NbExp=3; IntAct=EBI-10234038, EBI-533224;
CC P43115-12; Q8IWZ5: TRIM42; NbExp=3; IntAct=EBI-10234038, EBI-5235829;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:7883006,
CC ECO:0000269|PubMed:7981210, ECO:0000269|PubMed:8117308,
CC ECO:0000269|PubMed:8307176}; Multi-pass membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=12;
CC Comment=Additional isoforms seem to exist.;
CC Name=EP3A; Synonyms=EP3-I, EP3a1, EP3a2, EP(3-Ic);
CC IsoId=P43115-1; Sequence=Displayed;
CC Name=EP3C; Synonyms=EP3-II;
CC IsoId=P43115-2; Sequence=VSP_001935;
CC Name=EP3B; Synonyms=EP3-III;
CC IsoId=P43115-3; Sequence=VSP_001936;
CC Name=EP3D; Synonyms=EP3-IV;
CC IsoId=P43115-4; Sequence=VSP_001937;
CC Name=EP3E;
CC IsoId=P43115-5; Sequence=VSP_001938;
CC Name=EP3F;
CC IsoId=P43115-6; Sequence=VSP_001939;
CC Name=EP3G;
CC IsoId=P43115-7; Sequence=VSP_013271;
CC Name=EP3-III;
CC IsoId=P43115-8; Sequence=VSP_053774;
CC Name=EP3-IV;
CC IsoId=P43115-9; Sequence=VSP_053775;
CC Name=EP3-V;
CC IsoId=P43115-10; Sequence=VSP_053776;
CC Name=EP3E2;
CC IsoId=P43115-11; Sequence=VSP_053777;
CC Name=12;
CC IsoId=P43115-12; Sequence=VSP_058943;
CC -!- TISSUE SPECIFICITY: Detected in kidney (PubMed:8117308,
CC PubMed:8135729). Expressed in small intestine, heart, pancreas, gastric
CC fundic mucosa, mammary artery and pulmonary vessels.
CC {ECO:0000269|PubMed:18023986, ECO:0000269|PubMed:8117308,
CC ECO:0000269|PubMed:8135729}.
CC -!- MISCELLANEOUS: [Isoform EP3C]: Known as EP3D in PubMed:8075855.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform EP3B]: Known as EP3E in PubMed:8075855.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform EP3D]: Known as EP3F in PubMed:8075855.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA58742.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; S69200; AAB29854.1; -; mRNA.
DR EMBL; L27488; AAC13372.1; -; mRNA.
DR EMBL; L27489; AAC13373.1; -; mRNA.
DR EMBL; L27490; AAC13374.1; -; mRNA.
DR EMBL; X83857; CAA58737.1; -; mRNA.
DR EMBL; X83858; CAA58738.1; -; mRNA.
DR EMBL; X83859; CAA58739.1; -; mRNA.
DR EMBL; X83860; CAA58740.1; -; mRNA.
DR EMBL; X83861; CAA58741.1; -; mRNA.
DR EMBL; X83862; CAA58742.1; ALT_FRAME; mRNA.
DR EMBL; X83863; CAA58743.1; -; mRNA.
DR EMBL; L26976; AAA60076.1; -; mRNA.
DR EMBL; S69326; AAB30208.1; -; mRNA.
DR EMBL; L32660; AAA68191.1; -; mRNA.
DR EMBL; L32661; AAA68192.1; -; mRNA.
DR EMBL; L32662; AAA68193.1; -; mRNA.
DR EMBL; D38297; BAA07416.1; -; mRNA.
DR EMBL; D38298; BAA07417.1; -; mRNA.
DR EMBL; D38299; BAA07418.1; -; mRNA.
DR EMBL; D38300; BAA07419.1; -; mRNA.
DR EMBL; D38301; BAA07420.1; -; mRNA.
DR EMBL; U13214; AAA21130.1; -; mRNA.
DR EMBL; U13215; AAA21131.1; -; mRNA.
DR EMBL; U13216; AAA21132.1; -; mRNA.
DR EMBL; U13217; AAA21133.1; -; mRNA.
DR EMBL; U13218; AAA21134.1; -; mRNA.
DR EMBL; D86096; BAA19951.1; -; Genomic_DNA.
DR EMBL; D86096; BAA19952.1; -; Genomic_DNA.
DR EMBL; D86096; BAA19953.1; -; Genomic_DNA.
DR EMBL; D86096; BAA19954.1; -; Genomic_DNA.
DR EMBL; D86096; BAA19956.1; -; Genomic_DNA.
DR EMBL; D86096; BAA19957.1; -; Genomic_DNA.
DR EMBL; D86098; BAA19959.1; -; mRNA.
DR EMBL; AY429108; AAR07903.1; -; mRNA.
DR EMBL; AK315825; BAF98716.1; -; mRNA.
DR EMBL; AB451481; BAG70295.1; -; mRNA.
DR EMBL; AL031429; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL158087; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX06439.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX06446.1; -; Genomic_DNA.
DR EMBL; BC024229; AAH24229.1; -; mRNA.
DR EMBL; BC118578; AAI18579.1; -; mRNA.
DR CCDS; CCDS44160.1; -. [P43115-3]
DR CCDS; CCDS652.1; -. [P43115-4]
DR CCDS; CCDS655.1; -. [P43115-5]
DR CCDS; CCDS656.1; -. [P43115-1]
DR CCDS; CCDS657.1; -. [P43115-1]
DR CCDS; CCDS658.1; -. [P43115-2]
DR PIR; B55995; B55995.
DR PIR; I38747; I38747.
DR PIR; I38748; I38748.
DR PIR; I38750; I38750.
DR PIR; JC2056; JC2056.
DR PIR; S43375; S43375.
DR PIR; S68994; S51313.
DR PIR; S68995; S51315.
DR PIR; S68996; S51316.
DR PIR; S68997; S51317.
DR PIR; S68998; S51318.
DR PIR; S68999; S51319.
DR RefSeq; NP_001119516.1; NM_001126044.1. [P43115-1]
DR RefSeq; NP_942007.1; NM_198714.1. [P43115-1]
DR RefSeq; NP_942008.1; NM_198715.2. [P43115-2]
DR RefSeq; NP_942009.1; NM_198716.1. [P43115-4]
DR RefSeq; NP_942010.1; NM_198717.1. [P43115-3]
DR RefSeq; NP_942011.1; NM_198718.1. [P43115-5]
DR RefSeq; NP_942012.1; NM_198719.1. [P43115-1]
DR PDB; 6AK3; X-ray; 2.90 A; A/B=43-359.
DR PDB; 6M9T; X-ray; 2.50 A; A=2-259, A=273-353.
DR PDBsum; 6AK3; -.
DR PDBsum; 6M9T; -.
DR AlphaFoldDB; P43115; -.
DR SMR; P43115; -.
DR BioGRID; 111705; 119.
DR IntAct; P43115; 78.
DR STRING; 9606.ENSP00000349003; -.
DR BindingDB; P43115; -.
DR ChEMBL; CHEMBL3710; -.
DR DrugBank; DB00905; Bimatoprost.
DR DrugBank; DB11113; Castor oil.
DR DrugBank; DB00917; Dinoprostone.
DR DrugBank; DB08964; Gemeprost.
DR DrugBank; DB09211; Limaprost.
DR DrugBank; DB00929; Misoprostol.
DR DrugCentral; P43115; -.
DR GuidetoPHARMACOLOGY; 342; -.
DR GlyGen; P43115; 2 sites.
DR iPTMnet; P43115; -.
DR PhosphoSitePlus; P43115; -.
DR BioMuta; PTGER3; -.
DR DMDM; 1172071; -.
DR MassIVE; P43115; -.
DR PaxDb; P43115; -.
DR PeptideAtlas; P43115; -.
DR PRIDE; P43115; -.
DR ProteomicsDB; 3010; -.
DR ProteomicsDB; 55580; -. [P43115-1]
DR ProteomicsDB; 55581; -. [P43115-2]
DR ProteomicsDB; 55582; -. [P43115-3]
DR ProteomicsDB; 55583; -. [P43115-4]
DR ProteomicsDB; 55584; -. [P43115-5]
DR ProteomicsDB; 55585; -. [P43115-6]
DR ProteomicsDB; 55586; -. [P43115-7]
DR ProteomicsDB; 60186; -.
DR Antibodypedia; 2758; 472 antibodies from 39 providers.
DR DNASU; 5733; -.
DR Ensembl; ENST00000306666.10; ENSP00000302313.5; ENSG00000050628.21. [P43115-1]
DR Ensembl; ENST00000356595.8; ENSP00000349003.4; ENSG00000050628.21. [P43115-5]
DR Ensembl; ENST00000370924.4; ENSP00000359962.3; ENSG00000050628.21. [P43115-2]
DR Ensembl; ENST00000370931.7; ENSP00000359969.3; ENSG00000050628.21. [P43115-1]
DR Ensembl; ENST00000460330.5; ENSP00000418073.1; ENSG00000050628.21. [P43115-4]
DR Ensembl; ENST00000479353.5; ENSP00000421583.1; ENSG00000050628.21. [P43115-7]
DR Ensembl; ENST00000628037.2; ENSP00000486617.1; ENSG00000050628.21. [P43115-3]
DR GeneID; 5733; -.
DR KEGG; hsa:5733; -.
DR MANE-Select; ENST00000306666.10; ENSP00000302313.5; NM_198719.2; NP_942012.1.
DR UCSC; uc001dfg.2; human. [P43115-1]
DR CTD; 5733; -.
DR DisGeNET; 5733; -.
DR GeneCards; PTGER3; -.
DR HGNC; HGNC:9595; PTGER3.
DR HPA; ENSG00000050628; Tissue enhanced (adipose tissue, endometrium, kidney, smooth muscle).
DR MIM; 176806; gene.
DR neXtProt; NX_P43115; -.
DR OpenTargets; ENSG00000050628; -.
DR PharmGKB; PA288; -.
DR VEuPathDB; HostDB:ENSG00000050628; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01030000234559; -.
DR InParanoid; P43115; -.
DR OMA; SSKQWGR; -.
DR OrthoDB; 972015at2759; -.
DR PhylomeDB; P43115; -.
DR TreeFam; TF324982; -.
DR PathwayCommons; P43115; -.
DR Reactome; R-HSA-391908; Prostanoid ligand receptors.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR SignaLink; P43115; -.
DR SIGNOR; P43115; -.
DR BioGRID-ORCS; 5733; 22 hits in 1086 CRISPR screens.
DR ChiTaRS; PTGER3; human.
DR GenomeRNAi; 5733; -.
DR Pharos; P43115; Tclin.
DR PRO; PR:P43115; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P43115; protein.
DR Bgee; ENSG00000050628; Expressed in nephron tubule and 203 other tissues.
DR ExpressionAtlas; P43115; baseline and differential.
DR Genevisible; P43115; HS.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005635; C:nuclear envelope; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0004957; F:prostaglandin E receptor activity; IBA:GO_Central.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0008219; P:cell death; TAS:ProtInc.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR GO; GO:0014827; P:intestine smooth muscle contraction; IBA:GO_Central.
DR GO; GO:0060455; P:negative regulation of gastric acid secretion; IBA:GO_Central.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR GO; GO:0031622; P:positive regulation of fever generation; ISS:BHF-UCL.
DR InterPro; IPR001481; EP3_rcpt_2.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR008365; Prostanoid_rcpt.
DR InterPro; IPR001244; Prostglndn_DP_rcpt.
DR InterPro; IPR000265; Prostglndn_EP3_rcpt.
DR PANTHER; PTHR11866; PTHR11866; 1.
DR PANTHER; PTHR11866:SF10; PTHR11866:SF10; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00428; PROSTAGLNDNR.
DR PRINTS; PR01788; PROSTANOIDR.
DR PRINTS; PR00584; PRSTNOIDE32R.
DR PRINTS; PR00582; PRSTNOIDEP3R.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane;
KW G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane; Palmitate;
KW Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..390
FT /note="Prostaglandin E2 receptor EP3 subtype"
FT /id="PRO_0000070058"
FT TOPO_DOM 1..53
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..78
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 79..91
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 113..131
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..153
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 154..175
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..197
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 198..227
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 228..253
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 254..283
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 284..307
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 308..327
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 328..349
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 350..390
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 18
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 36
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 360..390
FT /note="IRYHTNNYASSSTSLPCQCSSTLMWSDHLER -> MRKRRLREQFWRPASSG
FT SGCQQIRCLMESCSLTQTGVQWSDFRSLQPSPPPLTAIFASWVQVILLPQPPK (in
FT isoform 12)"
FT /id="VSP_058943"
FT VAR_SEQ 360..390
FT /note="IRYHTNNYASSSTSLPCQCSSTLMWSDHLER -> VANAVSSCSNDGQKGQP
FT ISLSNEIIQTEAEEFWGN (in isoform EP3-III)"
FT /evidence="ECO:0000303|PubMed:9073510"
FT /id="VSP_053774"
FT VAR_SEQ 360..390
FT /note="IRYHTNNYASSSTSLPCQCSSTLMWSDHLER -> VANAVSSCSNDGQKGQP
FT ISLSNEIIQTEAMRKRRLREQEEFWGN (in isoform EP3-IV)"
FT /evidence="ECO:0000303|PubMed:9073510"
FT /id="VSP_053775"
FT VAR_SEQ 360..390
FT /note="IRYHTNNYASSSTSLPCQCSSTLMWSDHLER -> VANAVSSCSNDGQKGQP
FT ISLSNEIIQTEAMRKRRLREQEMGPDGRCFCHAWRQVPRTWCSSHDREPCSVQLS (in
FT isoform EP3-V)"
FT /evidence="ECO:0000303|PubMed:9073510"
FT /id="VSP_053776"
FT VAR_SEQ 360..390
FT /note="IRYHTNNYASSSTSLPCQCSSTLMWSDHLER -> EEFWGN (in
FT isoform EP3B)"
FT /evidence="ECO:0000303|PubMed:19054851,
FT ECO:0000303|PubMed:7476918, ECO:0000303|PubMed:7883006,
FT ECO:0000303|PubMed:7981210, ECO:0000303|PubMed:8075855,
FT ECO:0000303|PubMed:8307176, ECO:0000303|PubMed:9073510"
FT /id="VSP_001936"
FT VAR_SEQ 360..390
FT /note="IRYHTNNYASSSTSLPCQCSSTLMWSDHLER -> VANAVSSCSNDGQKGQP
FT ISLSNEIIQTEA (in isoform EP3C)"
FT /evidence="ECO:0000303|PubMed:7476918,
FT ECO:0000303|PubMed:7883006, ECO:0000303|PubMed:7981210,
FT ECO:0000303|PubMed:8075855, ECO:0000303|PubMed:8307176,
FT ECO:0000303|PubMed:9073510"
FT /id="VSP_001935"
FT VAR_SEQ 360..390
FT /note="IRYHTNNYASSSTSLPCQCSSTLMWSDHLER -> MRKRRLREQEEFWGN
FT (in isoform EP3D)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:7476918, ECO:0000303|PubMed:7883006,
FT ECO:0000303|PubMed:7981210, ECO:0000303|PubMed:8075855,
FT ECO:0000303|PubMed:9073510"
FT /id="VSP_001937"
FT VAR_SEQ 360..390
FT /note="IRYHTNNYASSSTSLPCQCSSTLMWSDHLER -> MRKRRLREQLICSLQNS
FT QIQRATAHCGQVQTYRVLNREEMEVLVSSINVYTRISTVKTE (in isoform
FT EP3E)"
FT /evidence="ECO:0000303|PubMed:7883006,
FT ECO:0000303|PubMed:9073510"
FT /id="VSP_001938"
FT VAR_SEQ 360..390
FT /note="IRYHTNNYASSSTSLPCQCSSTLMWSDHLER -> VANAVSSCSNDGQKGQP
FT ISLSNEIIQTEAMRKRRLREQLICSLRTLRYRGQLHIVGKYKPIVC (in isoform
FT EP3E2)"
FT /evidence="ECO:0000303|PubMed:9073510"
FT /id="VSP_053777"
FT VAR_SEQ 360..390
FT /note="IRYHTNNYASSSTSLPCQCSSTLMWSDHLER -> MRKRRLREQAPLLPTPT
FT VIDPSRFCAQPFRWFLDLSFPAMSSSHPQLPLTLASFKLLREPCSVQLS (in
FT isoform EP3F)"
FT /evidence="ECO:0000303|PubMed:7883006"
FT /id="VSP_001939"
FT VAR_SEQ 360..390
FT /note="IRYHTNNYASSSTSLPCQCSSTLMWSDHLER -> EMGPDGRCFCHAWRQVP
FT RTWCSSHDREPCSVQLS (in isoform EP3G)"
FT /evidence="ECO:0000303|Ref.9"
FT /id="VSP_013271"
FT VARIANT 169
FT /note="M -> L (in dbSNP:rs5670)"
FT /id="VAR_014694"
FT VARIANT 319
FT /note="T -> M (in dbSNP:rs13306020)"
FT /id="VAR_049436"
FT VARIANT 366
FT /note="N -> S (in dbSNP:rs13306014)"
FT /id="VAR_029218"
FT VARIANT 375
FT /note="P -> L (in dbSNP:rs5694)"
FT /id="VAR_014695"
FT CONFLICT 28..29
FT /note="ER -> DG (in Ref. 3, 4 and 7)"
FT /evidence="ECO:0000305"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:6M9T"
FT HELIX 53..77
FT /evidence="ECO:0007829|PDB:6M9T"
FT HELIX 86..115
FT /evidence="ECO:0007829|PDB:6M9T"
FT HELIX 120..123
FT /evidence="ECO:0007829|PDB:6M9T"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:6M9T"
FT HELIX 128..160
FT /evidence="ECO:0007829|PDB:6M9T"
FT HELIX 162..167
FT /evidence="ECO:0007829|PDB:6M9T"
FT HELIX 172..189
FT /evidence="ECO:0007829|PDB:6M9T"
FT HELIX 191..194
FT /evidence="ECO:0007829|PDB:6M9T"
FT STRAND 199..202
FT /evidence="ECO:0007829|PDB:6M9T"
FT TURN 203..206
FT /evidence="ECO:0007829|PDB:6M9T"
FT STRAND 207..210
FT /evidence="ECO:0007829|PDB:6M9T"
FT HELIX 225..258
FT /evidence="ECO:0007829|PDB:6M9T"
FT HELIX 276..306
FT /evidence="ECO:0007829|PDB:6M9T"
FT HELIX 324..346
FT /evidence="ECO:0007829|PDB:6M9T"
FT HELIX 348..352
FT /evidence="ECO:0007829|PDB:6M9T"
SQ SEQUENCE 390 AA; 43310 MW; BC76EAC78FDF5420 CRC64;
MKETRGYGGD APFCTRLNHS YTGMWAPERS AEARGNLTRP PGSGEDCGSV SVAFPITMLL
TGFVGNALAM LLVSRSYRRR ESKRKKSFLL CIGWLALTDL VGQLLTTPVV IVVYLSKQRW
EHIDPSGRLC TFFGLTMTVF GLSSLFIASA MAVERALAIR APHWYASHMK TRATRAVLLG
VWLAVLAFAL LPVLGVGQYT VQWPGTWCFI STGRGGNGTS SSHNWGNLFF ASAFAFLGLL
ALTVTFSCNL ATIKALVSRC RAKATASQSS AQWGRITTET AIQLMGIMCV LSVCWSPLLI
MMLKMIFNQT SVEHCKTHTE KQKECNFFLI AVRLASLNQI LDPWVYLLLR KILLRKFCQI
RYHTNNYASS STSLPCQCSS TLMWSDHLER
