PE2R3_RABIT
ID PE2R3_RABIT Reviewed; 411 AA.
AC P46069;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=Prostaglandin E2 receptor EP3 subtype;
DE Short=PGE receptor EP3 subtype;
DE Short=PGE2 receptor EP3 subtype;
DE AltName: Full=Prostanoid EP3 receptor;
GN Name=PTGER3;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 77A; 72A; 74A AND 80A), FUNCTION,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=New Zealand white; TISSUE=Kidney cortex;
RX PubMed=8119961; DOI=10.1016/s0021-9258(17)37583-x;
RA Breyer R.M., Emeson R.B., Tarng J.L., Breyer M.D., Davis L.S.,
RA Abromson R.M., Ferrenbach S.M.;
RT "Alternative splicing generates multiple isoforms of a rabbit prostaglandin
RT E2 receptor.";
RL J. Biol. Chem. 269:6163-6169(1994).
CC -!- FUNCTION: Receptor for prostaglandin E2 (PGE2) (PubMed:8119961).
CC Required for normal development of fever in response to pyrinogens,
CC including IL1B, prostaglandin E2 and bacterial lipopolysaccharide
CC (LPS). Required for normal potentiation of platelet aggregation by
CC prostaglandin E2, and thus plays a role in the regulation of blood
CC coagulation. Required for increased HCO3(-) secretion in the duodenum
CC in response to mucosal acidification, and thereby contributes to the
CC protection of the mucosa against acid-induced ulceration. Not required
CC for normal kidney function, normal urine volume and osmolality (By
CC similarity). {ECO:0000250|UniProtKB:P30557,
CC ECO:0000269|PubMed:8119961}.
CC -!- SUBUNIT: Interacts (via C-terminus) with MKLN1.
CC {ECO:0000250|UniProtKB:P34980}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:8119961};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Additional isoforms seem to exist.;
CC Name=77A;
CC IsoId=P46069-1; Sequence=Displayed;
CC Name=72A;
CC IsoId=P46069-2; Sequence=VSP_001943, VSP_001944;
CC Name=74A;
CC IsoId=P46069-3; Sequence=VSP_001945, VSP_001946;
CC Name=80A;
CC IsoId=P46069-4; Sequence=VSP_001947, VSP_001948;
CC -!- TISSUE SPECIFICITY: In the kidney cortex and medulla, adrenal gland and
CC stomach. In kidney, expression is higher in tubules in the outer
CC medulla, with lower levels in cortex. In kidney cortex, expression is
CC restricted to distal tubules. {ECO:0000269|PubMed:8119961}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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; U04274; AAA17413.1; -; mRNA.
DR EMBL; U04273; AAA17412.1; -; mRNA.
DR EMBL; U04275; AAA17414.1; -; mRNA.
DR EMBL; U04276; AAA17415.1; -; mRNA.
DR PIR; A53216; A53216.
DR PIR; B53216; B53216.
DR PIR; D53216; D53216.
DR RefSeq; NP_001076140.1; NM_001082671.1.
DR RefSeq; NP_001116407.1; NM_001122935.1. [P46069-1]
DR AlphaFoldDB; P46069; -.
DR SMR; P46069; -.
DR STRING; 9986.ENSOCUP00000017018; -.
DR GeneID; 100009389; -.
DR KEGG; ocu:100009389; -.
DR CTD; 5733; -.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; P46069; -.
DR OrthoDB; 972015at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0004957; F:prostaglandin E receptor activity; IEA:InterPro.
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 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..411
FT /note="Prostaglandin E2 receptor EP3 subtype"
FT /id="PRO_0000070061"
FT TOPO_DOM 1..49
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 50..74
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 75..87
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..108
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 109..127
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 128..149
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 150..171
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..193
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 194..223
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 224..249
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 250..279
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 280..303
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 304..323
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 324..345
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 346..411
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 367..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..389
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 18
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 126..204
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VAR_SEQ 356..389
FT /note="VIHENNEQKDEIQRENRNVSHSGQHEEARDSEKS -> HSPAIGDLQISTHI
FT SKTNKYFEGLMKTFHSLAYL (in isoform 80A)"
FT /evidence="ECO:0000303|PubMed:8119961"
FT /id="VSP_001947"
FT VAR_SEQ 356..377
FT /note="VIHENNEQKDEIQRENRNVSHS -> IRYHTNNYASSSTSLTHQCSST (in
FT isoform 74A)"
FT /evidence="ECO:0000303|PubMed:8119961"
FT /id="VSP_001945"
FT VAR_SEQ 356..361
FT /note="VIHENN -> EEFWEK (in isoform 72A)"
FT /evidence="ECO:0000303|PubMed:8119961"
FT /id="VSP_001943"
FT VAR_SEQ 362..411
FT /note="Missing (in isoform 72A)"
FT /evidence="ECO:0000303|PubMed:8119961"
FT /id="VSP_001944"
FT VAR_SEQ 378..411
FT /note="Missing (in isoform 74A)"
FT /evidence="ECO:0000303|PubMed:8119961"
FT /id="VSP_001946"
FT VAR_SEQ 390..411
FT /note="Missing (in isoform 80A)"
FT /evidence="ECO:0000303|PubMed:8119961"
FT /id="VSP_001948"
FT VARIANT 243
FT /note="T -> A"
SQ SEQUENCE 411 AA; 45600 MW; 1A0265AFBDDD0CD5 CRC64;
MKETRGDGGS APFCTRLNHS YPGMWAPEAR GNLTRPPGPG EDCGSVSVAF PITMLITGFV
GNALAMLLVS RSYRRRESKR KKSFLLCIGW LALTDLVGQL LTSPVVILVY LSKQRWEQLD
PSGRLCTFFG LTMTVFGLSS LFIASAMAVE RALAIRAPHW YASHMKTRAT RAVLLGVWLA
VLAFALLPVL GVGQYTIQWP GTWCFISTGR GDNGTSSSHN WGNLFFASTF AFLGLLALAI
TFTCNLATIK ALVSRCRAKA AASQSSAQWG RITTETAIQL MGIMCVLSVC WSPLLIMMLK
MIFNQTSVEH CKTDTGKQKE CNFFLIAVRL ASLNQILDPW VYLLLRKILL RKFCQVIHEN
NEQKDEIQRE NRNVSHSGQH EEARDSEKSK TIPGLFSILL QADPGARPYQ Q
