S1PR5_MOUSE
ID S1PR5_MOUSE Reviewed; 400 AA.
AC Q91X56; Q99MN8;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 140.
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=Lysophospholipid receptor B4;
DE AltName: Full=Sphingosine 1-phosphate receptor Edg-8;
DE Short=S1P receptor Edg-8;
GN Name=S1pr5; Synonyms=Edg8, Lpb4;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 14-400.
RC STRAIN=Swiss Webster / NIH;
RA Yang A.H., Zhang G., Chun J.J.M.;
RT "Molecular cloning of the mouse sphingosine-1-phosphate receptor gene,
RT Lpb4.";
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 14-400.
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=11705398; DOI=10.1021/bi011606i;
RA Im D.-S., Clemens J., Macdonald T.L., Lynch K.R.;
RT "Characterization of the human and mouse sphingosine 1-phosphate receptor,
RT S1P5 (Edg-8): structure-activity relationship of sphingosine1-phosphate
RT receptors.";
RL Biochemistry 40:14053-14060(2001).
RN [5]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND FUNCTION.
RX PubMed=15703400; DOI=10.1523/jneurosci.4645-04.2005;
RA Jaillard C., Harrison S., Stankoff B., Aigrot M.S., Calver A.R., Duddy G.,
RA Walsh F.S., Pangalos M.N., Arimura N., Kaibuchi K., Zalc B., Lubetzki C.;
RT "Edg8/S1P5: an oligodendroglial receptor with dual function on process
RT retraction and cell survival.";
RL J. Neurosci. 25:1459-1469(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-340, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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/0)alpha and G(12) subclass of heteromeric G-proteins (By
CC similarity). S1P activation on oligodendroglial cells modulates two
CC distinct functional pathways mediating either process retraction or
CC cell survival. S1P activation on O4-positive pre-oligodendrocytes
CC induces process retraction via a Rho kinase/collapsin response-mediated
CC protein signaling pathway. The S1P-induced survival of mature
CC oligodendrocytes is mediated through a pertussis toxin-sensitive, Akt-
CC dependent pathway. S1P activation on oligodendroglial cells modulates
CC two distinct functional pathways mediating either process retraction or
CC cell survival. These effects depend on the developmental stage of the
CC cell. {ECO:0000250, ECO:0000269|PubMed:15703400}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in spleen and brain. In the CNS
CC expression is restricted to oligodendrocytes.
CC {ECO:0000269|PubMed:11705398, ECO:0000269|PubMed:15703400}.
CC -!- DEVELOPMENTAL STAGE: Expressed in 7-day and 17-day embryos, but not in
CC 11-day and 15-day embryos, implying its role in mammalian development.
CC In oligodendrocytes, expressed throughout development from the immature
CC stages to the mature myelin-froming cell.
CC {ECO:0000269|PubMed:15703400}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; BC012232; AAH12232.1; -; mRNA.
DR EMBL; AF327535; AAK15485.1; -; mRNA.
DR EMBL; AK081126; BAC38142.1; -; mRNA.
DR CCDS; CCDS22898.1; -.
DR RefSeq; NP_444420.1; NM_053190.2.
DR AlphaFoldDB; Q91X56; -.
DR SMR; Q91X56; -.
DR BioGRID; 220483; 1.
DR STRING; 10090.ENSMUSP00000113843; -.
DR GuidetoPHARMACOLOGY; 279; -.
DR GlyGen; Q91X56; 1 site.
DR iPTMnet; Q91X56; -.
DR PhosphoSitePlus; Q91X56; -.
DR PaxDb; Q91X56; -.
DR PRIDE; Q91X56; -.
DR ProteomicsDB; 256667; -.
DR Antibodypedia; 12897; 409 antibodies from 37 providers.
DR DNASU; 94226; -.
DR Ensembl; ENSMUST00000122088; ENSMUSP00000113843; ENSMUSG00000045087.
DR GeneID; 94226; -.
DR KEGG; mmu:94226; -.
DR UCSC; uc009oks.2; mouse.
DR CTD; 53637; -.
DR MGI; MGI:2150641; S1pr5.
DR VEuPathDB; HostDB:ENSMUSG00000045087; -.
DR eggNOG; ENOG502QSWN; Eukaryota.
DR GeneTree; ENSGT01050000244887; -.
DR HOGENOM; CLU_047979_1_0_1; -.
DR InParanoid; Q91X56; -.
DR OMA; LVLHYNY; -.
DR OrthoDB; 981486at2759; -.
DR PhylomeDB; Q91X56; -.
DR TreeFam; TF330052; -.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR Reactome; R-MMU-419408; Lysosphingolipid and LPA receptors.
DR BioGRID-ORCS; 94226; 3 hits in 76 CRISPR screens.
DR PRO; PR:Q91X56; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q91X56; protein.
DR Bgee; ENSMUSG00000045087; Expressed in lumbar subsegment of spinal cord and 112 other tissues.
DR Genevisible; Q91X56; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; ISO:MGI.
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:0007186; P:G protein-coupled receptor signaling pathway; TAS:MGI.
DR GO; GO:0019222; P:regulation of metabolic process; IBA:GO_Central.
DR GO; GO:0045664; P:regulation of neuron differentiation; IEA:Ensembl.
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 SMART; SM01381; 7TM_GPCR_Srsx; 1.
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_0000069437"
FT TOPO_DOM 1..41
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 42..62
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 63..68
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 69..89
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 90..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 331..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 340
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 342
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JKM5"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JKM5"
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"
SQ SEQUENCE 400 AA; 42331 MW; A4311B8E8515F3F4 CRC64;
MEPGLLRPAP VSEVIVLHYN YTGKLRGARY QPGAGLRADA AVCLAVCAFI VLENLAVLLV
LVRHPRFHAP MFLLLGSLTL SDLLAGAAYA TNILLSGPLT LRLSPALWFA REGGVFVALA
ASVLSLLAIA LERHLTMARR GPAPAASRAR TLAMAVAAWG ASLLLGLLPA LGWNCLGRLE
TCSTVLPLYA KAYVLFCVLA FLGILAAICA LYARIYCQVR ANARRLRAGP GSRRATSSSR
SRHTPRSLAL LRTLSVVLLA FVACWGPLFL LLLLDVACPA RACPVLLQAD PFLGLAMANS
LLNPIIYTFT NRDLRHALLR LLCCGRGPCN QDSSNSLQRS PSAAGPSGGG LRRCLPPTLD
RSSSPSEHLS PQQDGVDTSC STGSPGVATA NRSLVPTATD
