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PI2R_RAT
ID   PI2R_RAT                Reviewed;         416 AA.
AC   P43253;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 158.
DE   RecName: Full=Prostacyclin receptor;
DE   AltName: Full=Prostaglandin I2 receptor;
DE            Short=PGI receptor;
DE            Short=PGI2 receptor;
DE   AltName: Full=Prostanoid IP receptor;
DE   Flags: Precursor;
GN   Name=Ptgir;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Lung;
RX   PubMed=7803522; DOI=10.1016/0167-4889(94)90300-x;
RA   Sasaki Y., Usui T., Tanaka I., Nakagawa O., Sando T., Takahashi T.,
RA   Namba T., Narumiya S., Nakao K.;
RT   "Cloning and expression of a cDNA for rat prostacyclin receptor.";
RL   Biochim. Biophys. Acta 1224:601-605(1994).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Receptor for prostacyclin (prostaglandin I2 or PGI2). The
CC       activity of this receptor is mediated by G(s) proteins which activate
CC       adenylate cyclase.
CC   -!- SUBUNIT: Interacts (non-isoprenylated C-terminus) with PDZK1.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- PTM: Isoprenylation does not influence ligand binding but is required
CC       for efficient coupling to the effectors adenylyl cyclase and
CC       phospholipase C. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; D28966; BAA06091.1; -; mRNA.
DR   PIR; S52078; S52078.
DR   RefSeq; NP_001071112.1; NM_001077644.1.
DR   AlphaFoldDB; P43253; -.
DR   SMR; P43253; -.
DR   STRING; 10116.ENSRNOP00000022461; -.
DR   BindingDB; P43253; -.
DR   ChEMBL; CHEMBL3322; -.
DR   DrugCentral; P43253; -.
DR   GuidetoPHARMACOLOGY; 345; -.
DR   GlyGen; P43253; 1 site.
DR   iPTMnet; P43253; -.
DR   PhosphoSitePlus; P43253; -.
DR   PaxDb; P43253; -.
DR   PRIDE; P43253; -.
DR   Ensembl; ENSRNOT00000022461; ENSRNOP00000022461; ENSRNOG00000016756.
DR   GeneID; 292661; -.
DR   KEGG; rno:292661; -.
DR   UCSC; RGD:1310890; rat.
DR   CTD; 5739; -.
DR   RGD; 1310890; Ptgir.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT01050000244902; -.
DR   HOGENOM; CLU_045991_0_1_1; -.
DR   InParanoid; P43253; -.
DR   OMA; IHPFCGD; -.
DR   OrthoDB; 972015at2759; -.
DR   PhylomeDB; P43253; -.
DR   Reactome; R-RNO-391908; Prostanoid ligand receptors.
DR   Reactome; R-RNO-392851; Prostacyclin signalling through prostacyclin receptor.
DR   PRO; PR:P43253; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000016756; Expressed in lung and 16 other tissues.
DR   GO; GO:0005829; C:cytosol; ISO:RGD.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR   GO; GO:0016501; F:prostacyclin receptor activity; IBA:GO_Central.
DR   GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; ISO:RGD.
DR   GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR   GO; GO:0010642; P:negative regulation of platelet-derived growth factor receptor signaling pathway; ISO:RGD.
DR   GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; ISO:RGD.
DR   GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR   GO; GO:0051239; P:regulation of multicellular organismal process; IEA:UniProt.
DR   GO; GO:0032496; P:response to lipopolysaccharide; ISO:RGD.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   InterPro; IPR008365; Prostanoid_rcpt.
DR   InterPro; IPR000370; Prostglndn_IP_rcpt.
DR   PANTHER; PTHR11866; PTHR11866; 1.
DR   PANTHER; PTHR11866:SF7; PTHR11866:SF7; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR01788; PROSTANOIDR.
DR   PRINTS; PR00856; PRSTNOIDIPR.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW   Lipoprotein; Membrane; Methylation; Phosphoprotein; Prenylation; Receptor;
KW   Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN           1..413
FT                   /note="Prostacyclin receptor"
FT                   /id="PRO_0000070077"
FT   PROPEP          414..416
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000240006"
FT   TOPO_DOM        1..45
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        46..67
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        68..80
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        81..105
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        106..123
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        124..144
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        145..163
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        164..187
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        188..215
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        216..237
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        238..264
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        265..289
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        290..302
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        303..323
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        324..416
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         366
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         413
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250"
FT   LIPID           413
FT                   /note="S-farnesyl cysteine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        36
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        34..194
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   DISULFID        121..199
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   416 AA;  44662 MW;  03171B5ED21C4171 CRC64;
     MVASGGRPDG PPSITPESPL IVGGREWQGM AGSCWNITYV QDSVGPATST LMFVAGVVGN
     GLALGILGAR RRSHPSAFAV LVTGLAVTDL LGTCFLSPAV FVAYARNSSL LGLAHGGTML
     CDTFAFAMTF FGLASTLILF AMAVERCLAL SHPYLYAQLD GPRCARLALP AIYAFCCLFC
     SLPLLGLGEH QQYCPGSWCF IRMRSPQPGG CAFSLAYASL MALLVTSIFF CNGSVTLSLC
     HMYRQQRRHH GSFVPTSRAR EDEVYHLILL ALMTGIMAVC SLPLTIRGFT QAIAPDSREM
     GDLHAFRFNA FNPILDPWVF ILFRKAVFQR LKFWLCCLCA RSVHGDLQTP LSRPVSGRRD
     TLAPDSLQAK EGNWVPLSTW GTGQVAPLTA VPLSGGDGCS VGMPSKTEAV VACSLC
 
 
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