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 24-JAN-2024, entry version 213. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 7WU9; EM; 3.38 A; R=47-359. DR PDBsum; 6AK3; -. DR PDBsum; 6M9T; -. DR PDBsum; 7WU9; -. DR AlphaFoldDB; P43115; -. DR EMDB; EMD-32824; -. 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 DrugBank; DB16315; Rivenprost. DR DrugBank; DB04297; Trichostatin A. DR DrugCentral; P43115; -. DR GuidetoPHARMACOLOGY; 342; -. DR TCDB; 9.A.14.9.2; the g-protein-coupled receptor (gpcr) family. DR GlyCosmos; P43115; 2 sites, No reported glycans. DR GlyGen; P43115; 2 sites. DR iPTMnet; P43115; -. DR PhosphoSitePlus; P43115; -. DR BioMuta; PTGER3; -. DR DMDM; 1172071; -. DR MassIVE; P43115; -. DR PaxDb; 9606-ENSP00000349003; -. DR PeptideAtlas; 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; 528 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; ENST00000370924.5; 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 AGR; HGNC:9595; -. 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; 5355693at2759; -. 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; 23 hits in 1174 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 204 other cell types or tissues. DR ExpressionAtlas; P43115; baseline and differential. DR GO; GO:0016020; C:membrane; NAS:UniProtKB. 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 Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1. 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; G-PROTEIN COUPLED RECEPTOR FAMILY 1 MEMBER; 1. DR PANTHER; PTHR11866:SF10; PROSTAGLANDIN E2 RECEPTOR EP3 SUBTYPE; 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 SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. DR Genevisible; P43115; HS. 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 //