S1PR5_PIG
ID S1PR5_PIG Reviewed; 398 AA.
AC Q684M3;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 71.
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=Sphingosine 1-phosphate receptor Edg-8;
DE Short=S1P receptor Edg-8;
GN Name=S1PR5; Synonyms=EDG8;
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 [GENOMIC DNA].
RA Leeb T.;
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AJ632303; CAG15152.1; -; Genomic_DNA.
DR RefSeq; NP_001116581.1; NM_001123109.1.
DR AlphaFoldDB; Q684M3; -.
DR SMR; Q684M3; -.
DR STRING; 9823.ENSSSCP00000025031; -.
DR PaxDb; Q684M3; -.
DR PRIDE; Q684M3; -.
DR Ensembl; ENSSSCT00015101812; ENSSSCP00015042195; ENSSSCG00015075560.
DR Ensembl; ENSSSCT00030037813; ENSSSCP00030017343; ENSSSCG00030027044.
DR Ensembl; ENSSSCT00045007194; ENSSSCP00045004936; ENSSSCG00045004317.
DR Ensembl; ENSSSCT00050025619; ENSSSCP00050010642; ENSSSCG00050018947.
DR Ensembl; ENSSSCT00060048513; ENSSSCP00060020770; ENSSSCG00060035801.
DR GeneID; 100141401; -.
DR KEGG; ssc:100141401; -.
DR CTD; 53637; -.
DR eggNOG; ENOG502QSWN; Eukaryota.
DR InParanoid; Q684M3; -.
DR OrthoDB; 981486at2759; -.
DR Reactome; R-SSC-418594; G alpha (i) signalling events.
DR Reactome; R-SSC-419408; Lysosphingolipid and LPA receptors.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0038036; F:sphingosine-1-phosphate receptor activity; IEA:InterPro.
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; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 3: Inferred from homology;
KW Cell membrane; G-protein coupled receptor; Glycoprotein; Lipoprotein;
KW Membrane; Palmitate; Phosphoprotein; Receptor; Reference proteome;
KW Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..398
FT /note="Sphingosine 1-phosphate receptor 5"
FT /id="PRO_0000069438"
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..70
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 71..91
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 92..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..191
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 192..212
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 213..252
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 253..273
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 274..287
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 288..308
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 309..398
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 332..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 337
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91X56"
FT MOD_RES 381
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JKM5"
FT LIPID 323
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 20
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 398 AA; 41861 MW; 37172AFB6EF06125 CRC64;
MEPGLLRPAP VSEVIVLHYN YTGKLRGARY QPGAGLRADA VVCLAVCALI VLENLAVLVV
LGRHPRFHAP MFLLLGSLTL SDLLAGAAYA ANILLSGPLT LRLSPALWFA REGGVFVALA
ASVLSLLAIA LERLLTMERR GPAPAARRGR TLALAAGAWG VSLLLGLLPA LGWNCLGRLE
ACSTVLPLYA KAYVLFCVLA FVGILAAICG LYARIYCQVR AKAQRLRARP GAGEGTSARA
RGTPRSLALL RTLSVVLVAF VACWGPLFLL LLLDVACPAR ACPVLLQADP FLGLAMANSL
LNPIIYTFTN RDLRHALLRL ICCGRRPCWG GSGTSRSPGS TLGASGGLHR WLPPGMDRSS
SRSERSSPQR DGLDTSGSTG SPAAPTAAQT LVPPPAAD
