S1PR5_RAT
ID S1PR5_RAT Reviewed; 400 AA.
AC Q9JKM5; Q9QY79;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Sphingosine 1-phosphate receptor 5;
DE Short=S1P receptor 5;
DE Short=S1P5;
DE AltName: Full=Endothelial differentiation G-protein-coupled receptor 8;
DE AltName: Full=Nerve growth factor-regulated G-protein-coupled receptor 1;
DE Short=NRG-1;
DE AltName: Full=Sphingosine 1-phosphate receptor Edg-8;
DE Short=S1P receptor Edg-8;
GN Name=S1pr5; Synonyms=Edg8, Nrg1;
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], TISSUE SPECIFICITY, AND INDUCTION.
RC TISSUE=Adrenal gland;
RX PubMed=10532805; DOI=10.1006/mcne.1999.0776;
RA Glickman M., Malek R.L., Kwitek-Black A.E., Jacob H.J., Lee N.H.;
RT "Molecular cloning, tissue-specific expression, and chromosomal
RT localization of a novel nerve growth factor-regulated G-protein-coupled
RT receptor, nrg-1.";
RL Mol. Cell. Neurosci. 14:141-152(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND POSSIBLE FUNCTION.
RC TISSUE=Brain;
RX PubMed=10799507; DOI=10.1074/jbc.275.19.14281;
RA Im D.-S., Heise C.E., Ancellin N., O'Dowd B.F., Shei G.-J., Heavens R.P.,
RA Rigby M.R., Hla T., Mandala S., McAllister G., George S.R., Lynch K.R.;
RT "Characterization of a novel sphingosine 1-phosphate receptor, Edg-8.";
RL J. Biol. Chem. 275:14281-14286(2000).
RN [3]
RP SIGNAL TRANSDUCTION PATHWAY EXAMINATION.
RX PubMed=11069896; DOI=10.1074/jbc.m003964200;
RA Malek R.L., Toman R.E., Edsall L.C., Wong S., Chiu J., Letterle C.A.,
RA Van Brocklyn J.R., Milstien S., Spiegel S., Lee N.H.;
RT "Nrg-1 belongs to the endothelial differentiation gene family of G protein-
RT coupled sphingosine-1-phosphate receptors.";
RL J. Biol. Chem. 276:5692-5699(2001).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=12234605; DOI=10.1016/s0006-2952(02)01289-3;
RA Niedernberg A., Scherer C.R., Busch A.E., Kostenis E.;
RT "Comparative analysis of human and rat S1P(5) (edg8): differential
RT expression profiles and sensitivities to antagonists.";
RL Biochem. Pharmacol. 64:1243-1250(2002).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-340; SER-342 AND SER-384, AND
RP IDENTIFICATION BY 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 the lysosphingolipid sphingosine 1-phosphate
CC (S1P). S1P is a bioactive lysophospholipid that elicits diverse
CC physiological effect on most types of cells and tissues. Is coupled to
CC both the G(i/O)alpha and G(12) subclass of heteromeric G-proteins.
CC Displays antiproliferative effects in transfected CHO-K1 and HEK293
CC cells.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Found almost exclusively in brain and skin.
CC Ubiquitously detected in different brain regions with very prominent
CC expression in lower brain regions such as the midbrain, pons, medulla,
CC and spinal cord. Expressed predominantly within white matter tracts of
CC the brain. Corpus callosum, optic nerve, olfactory tract, anterior
CC commissure, internal and external capsules, fimbra of the hippocampus,
CC mammillary tract, stria medullaris, and white matter of the cerebellum
CC and brain stem all express the receptor. Within the striatum itself
CC white matter fascicles express the receptor. Detected also in spleen
CC and lung. Not observed in heart, liver, skeletal muscle, kidney, or
CC testes. {ECO:0000269|PubMed:10532805, ECO:0000269|PubMed:10799507,
CC ECO:0000269|PubMed:12234605}.
CC -!- INDUCTION: In PC-12 cells, nerve growth factor induces neuronal
CC differentiation and represses expression of the receptor. Down-
CC regulated also by fibroblast growth factor and dibutyryl cAMP.
CC Epidermal growth factor, an agent that does not induce differentiation,
CC does not repress expression. Protein kinase A appears to be an
CC obligatory cellular component in regulation.
CC {ECO:0000269|PubMed:10532805}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AF115249; AAF15395.1; -; mRNA.
DR EMBL; AF233649; AAF35912.1; -; mRNA.
DR RefSeq; NP_068543.2; NM_021775.2.
DR RefSeq; XP_006242725.1; XM_006242663.3.
DR RefSeq; XP_006242726.1; XM_006242664.3.
DR RefSeq; XP_006242727.1; XM_006242665.3.
DR AlphaFoldDB; Q9JKM5; -.
DR SMR; Q9JKM5; -.
DR BioGRID; 248819; 1.
DR STRING; 10116.ENSRNOP00000028380; -.
DR GuidetoPHARMACOLOGY; 279; -.
DR GlyGen; Q9JKM5; 1 site.
DR iPTMnet; Q9JKM5; -.
DR PhosphoSitePlus; Q9JKM5; -.
DR PaxDb; Q9JKM5; -.
DR Ensembl; ENSRNOT00000028380; ENSRNOP00000028380; ENSRNOG00000020901.
DR Ensembl; ENSRNOT00000098087; ENSRNOP00000090421; ENSRNOG00000020901.
DR GeneID; 60399; -.
DR KEGG; rno:60399; -.
DR UCSC; RGD:620566; rat.
DR CTD; 53637; -.
DR RGD; 620566; S1pr5.
DR eggNOG; ENOG502QSWN; Eukaryota.
DR GeneTree; ENSGT01050000244887; -.
DR HOGENOM; CLU_047979_1_0_1; -.
DR InParanoid; Q9JKM5; -.
DR OMA; LVLHYNY; -.
DR OrthoDB; 981486at2759; -.
DR PhylomeDB; Q9JKM5; -.
DR TreeFam; TF330052; -.
DR Reactome; R-RNO-418594; G alpha (i) signalling events.
DR Reactome; R-RNO-419408; Lysosphingolipid and LPA receptors.
DR PRO; PR:Q9JKM5; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000020901; Expressed in cerebellum and 12 other tissues.
DR Genevisible; Q9JKM5; RN.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IDA:RGD.
DR GO; GO:0038036; F:sphingosine-1-phosphate receptor activity; IEA:InterPro.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0019222; P:regulation of metabolic process; IBA:GO_Central.
DR GO; GO:0045664; P:regulation of neuron differentiation; IEP:RGD.
DR InterPro; IPR005386; EDG8_S1P_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR004061; S1P_rcpt.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR01561; EDG8RECEPTOR.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR01523; S1PRECEPTOR.
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; G-protein coupled receptor; Glycoprotein; Lipoprotein;
KW Membrane; Palmitate; Phosphoprotein; Receptor; Reference proteome;
KW Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..400
FT /note="Sphingosine 1-phosphate receptor 5"
FT /id="PRO_0000069439"
FT TOPO_DOM 1..40
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 41..61
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 62..69
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 70..90
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 91..111
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 112..132
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 133..151
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 152..172
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 173..192
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 193..213
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 214..253
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 254..274
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 275..288
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 289..309
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 310..400
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 330..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 340
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 342
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT LIPID 324
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 20
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 131
FT /note="L -> I (in Ref. 1; AAF15395)"
FT /evidence="ECO:0000305"
FT CONFLICT 162..164
FT /note="SLL -> LLT (in Ref. 1; AAF15395)"
FT /evidence="ECO:0000305"
FT CONFLICT 188
FT /note="L -> V (in Ref. 1; AAF15395)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 400 AA; 42369 MW; 71B398DC4DEE0FEB CRC64;
MESGLLRPAP VSEVIVLHYN YTGKLRGARY QPGAGLRADA AVCLAVCAFI VLENLAVLLV
LGRHPRFHAP MFLLLGSLTL SDLLAGAAYA TNILLSGPLT LRLSPALWFA REGGVFVALA
ASVLSLLAIA LERHLTMARR GPAPAASRAR TLAMAVAAWG LSLLLGLLPA LGWNCLGRLE
ACSTVLPLYA KAYVLFCVLA FLGILAAICA LYARIYCQVR ANARRLRAGP GSRRATSSSR
SRHTPRSLAL LRTLSVVLLA FVACWGPLFL LLLLDVACPA RACPVLLQAD PFLGLAMANS
LLNPIIYTFT NRDLRHALLR LLCCGRGPCN QDSSNSLQRS PSAVGPSGGG LRRCLPPTLD
RSSSPSEHSC PQRDGMDTSC STGSPGAATA NRTLVPDATD
