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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
 
 
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