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PE2R3_PIG
ID   PE2R3_PIG               Reviewed;         373 AA.
AC   P50131; Q28967;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 130.
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   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Heart;
RA   Meyer J., Schroer K.;
RL   Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 323-365 (ISOFORM SHORT).
RC   TISSUE=Heart;
RA   Meyer J., Schroer K.;
RL   Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Receptor for prostaglandin E2 (PGE2). Required for normal
CC       development of fever in response to pyrinogens, including IL1B,
CC       prostaglandin E2 and bacterial lipopolysaccharide (LPS). Required for
CC       normal potentiation of platelet aggregation by prostaglandin E2, and
CC       thus plays a role in the regulation of blood coagulation. Required for
CC       increased HCO3(-) secretion in the duodenum in response to mucosal
CC       acidification, and thereby contributes to the protection of the mucosa
CC       against acid-induced ulceration. Not required for normal kidney
CC       function, normal urine volume and osmolality.
CC       {ECO:0000250|UniProtKB:P30557}.
CC   -!- SUBUNIT: Interacts (via C-terminus) with MKLN1.
CC       {ECO:0000250|UniProtKB:P34980}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P30557};
CC       Multi-pass membrane protein {ECO:0000250|UniProtKB:P30557}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Long;
CC         IsoId=P50131-1; Sequence=Displayed;
CC       Name=Short;
CC         IsoId=P50131-2; Sequence=VSP_001942;
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; U27083; AAC63408.1; -; mRNA.
DR   EMBL; U30374; AAA75308.1; -; mRNA.
DR   RefSeq; NP_998999.1; NM_213834.1. [P50131-1]
DR   AlphaFoldDB; P50131; -.
DR   SMR; P50131; -.
DR   STRING; 9823.ENSSSCP00000004097; -.
DR   PaxDb; P50131; -.
DR   PRIDE; P50131; -.
DR   Ensembl; ENSSSCT00015008308; ENSSSCP00015003345; ENSSSCG00015006184. [P50131-1]
DR   Ensembl; ENSSSCT00050026947; ENSSSCP00050011152; ENSSSCG00050019943. [P50131-1]
DR   GeneID; 396811; -.
DR   KEGG; ssc:396811; -.
DR   CTD; 5733; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   HOGENOM; CLU_045991_3_1_1; -.
DR   InParanoid; P50131; -.
DR   OrthoDB; 972015at2759; -.
DR   TreeFam; TF324982; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   Genevisible; P50131; SS.
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; IBA:GO_Central.
DR   GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
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   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..373
FT                   /note="Prostaglandin E2 receptor EP3 subtype"
FT                   /id="PRO_0000070060"
FT   TOPO_DOM        1..30
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        31..55
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        56..68
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        69..89
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        90..108
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        109..130
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        131..152
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        153..174
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        175..204
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        205..230
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        231..260
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        261..284
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        285..304
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        305..326
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        327..373
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        13
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        194
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        107..185
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   VAR_SEQ         337..373
FT                   /note="AVSQKQREEAATLIFTHLSISRTEPGEARVLFSKSKC -> VANAVCSCSKN
FT                   GQKVQTISLSHEITQTEA (in isoform Short)"
FT                   /evidence="ECO:0000303|Ref.2"
FT                   /id="VSP_001942"
SQ   SEQUENCE   373 AA;  41417 MW;  4CB7CC14B6C68186 CRC64;
     MWAPERSAEE QGNLTRSLGS SEDCGSVSVV FPMTMLITGF VGNALAMLLV SQSYRRRESK
     RKKSFLLCIG WLALTDMVGQ LLTSPVVIVL YLSHQRWEQL DPSGRLCTFF GLTMTAFGLS
     SLFIASAMAV ERALAIRAPH WYSSHMKTSA TRAVLLGVWL AVLAFALLPV LGVGQYTIQW
     PGTWCFISTR TGGNETSSEN NWGNIFFASA FSFLGLSALV VTFACNLATI KALVSRCRAK
     ATASQSSAQW GRITTETAIQ LMGIMCVLSV CWSPLLIMML KTIFNQTSVE YCKVYTEKQN
     ECNFFLIAVR LASLNQILDP WVYLLLRKIL LQKFCQAVSQ KQREEAATLI FTHLSISRTE
     PGEARVLFSK SKC
 
 
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