PSYR_MOUSE
ID PSYR_MOUSE Reviewed; 337 AA.
AC Q61038; Q921N3;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2003, sequence version 2.
DT 25-MAY-2022, entry version 150.
DE RecName: Full=Psychosine receptor;
DE AltName: Full=G-protein coupled receptor 65;
DE AltName: Full=T-cell death-associated gene 8 protein;
GN Name=Gpr65; Synonyms=Gpcr25, Tdag8;
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 [MRNA], AND FUNCTION.
RC TISSUE=Thymocyte;
RX PubMed=8599842; DOI=10.1006/cimm.1996.0051;
RA Choi J.-W., Lee S.Y., Choi Y.;
RT "Identification of a putative G protein-coupled receptor induced during
RT activation-induced apoptosis of T cells.";
RL Cell. Immunol. 168:78-84(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27287411; DOI=10.1016/j.immuni.2016.05.007;
RA Lassen K.G., McKenzie C.I., Mari M., Murano T., Begun J., Baxt L.A.,
RA Goel G., Villablanca E.J., Kuo S.Y., Huang H., Macia L., Bhan A.K.,
RA Batten M., Daly M.J., Reggiori F., Mackay C.R., Xavier R.J.;
RT "Genetic coding variant in GPR65 alters lysosomal pH and links lysosomal
RT dysfunction with colitis risk.";
RL Immunity 44:1392-1405(2016).
CC -!- FUNCTION: Receptor for the glycosphingolipid psychosine (PSY) and
CC several related glycosphingolipids (By similarity). Plays a role in
CC immune response by maintaining lysosome function and supporting
CC phagocytosis-mediated intracellular bacteria clearance
CC (PubMed:27287411). May have a role in activation-induced cell death or
CC differentiation of T-cells (PubMed:8599842).
CC {ECO:0000250|UniProtKB:Q8IYL9, ECO:0000269|PubMed:27287411,
CC ECO:0000269|PubMed:8599842}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Detected in thymus and at low levels in spleen.
CC -!- INDUCTION: By glucocorticoids, during apoptosis of immature thymocytes.
CC -!- DISRUPTION PHENOTYPE: Mutant mice are healthy with no signs of
CC spontaneous colitis or inflammation, however are more susceptible to
CC bacteria-induced colitis in comparison to the wild type.
CC {ECO:0000269|PubMed:27287411}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U39827; AAB02188.1; -; mRNA.
DR EMBL; BC011332; AAH11332.1; -; mRNA.
DR CCDS; CCDS26096.1; -.
DR RefSeq; NP_032178.1; NM_008152.3.
DR AlphaFoldDB; Q61038; -.
DR SMR; Q61038; -.
DR STRING; 10090.ENSMUSP00000074581; -.
DR GlyGen; Q61038; 2 sites.
DR iPTMnet; Q61038; -.
DR PhosphoSitePlus; Q61038; -.
DR PaxDb; Q61038; -.
DR PRIDE; Q61038; -.
DR ProteomicsDB; 301868; -.
DR DNASU; 14744; -.
DR GeneID; 14744; -.
DR KEGG; mmu:14744; -.
DR CTD; 8477; -.
DR MGI; MGI:108031; Gpr65.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; Q61038; -.
DR OrthoDB; 987208at2759; -.
DR PhylomeDB; Q61038; -.
DR TreeFam; TF331803; -.
DR Reactome; R-MMU-373076; Class A/1 (Rhodopsin-like receptors).
DR Reactome; R-MMU-416476; G alpha (q) signalling events.
DR BioGRID-ORCS; 14744; 2 hits in 71 CRISPR screens.
DR PRO; PR:Q61038; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q61038; protein.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0004930; F:G protein-coupled receptor activity; ISO:MGI.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; ISO:MGI.
DR GO; GO:0090630; P:activation of GTPase activity; ISO:MGI.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0006915; P:apoptotic process; TAS:BHF-UCL.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0051482; P:positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G protein-coupled signaling pathway; IBA:GO_Central.
DR GO; GO:0035025; P:positive regulation of Rho protein signal transduction; IBA:GO_Central.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; ISO:MGI.
DR GO; GO:0010447; P:response to acidic pH; ISO:MGI.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR005464; Psych_rcpt.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR01649; PSYCHOSINER.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..337
FT /note="Psychosine receptor"
FT /id="PRO_0000070088"
FT TOPO_DOM 1..17
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 18..38
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 39..52
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 53..73
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 74..91
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 113..131
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..152
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 153..182
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 204..229
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 230..250
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 251..273
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..294
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 295..337
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 89..172
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 12
FT /note="H -> R (in Ref. 1; AAB02188)"
FT /evidence="ECO:0000305"
FT CONFLICT 318
FT /note="Q -> K (in Ref. 1; AAB02188)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 337 AA; 39388 MW; 61A1ADE6E0D09273 CRC64;
MAMNSMCIEE QHHLEHYLFP VVYIIVFIVS VPANIGSLCV SFLQAKKENE LGIYLFSLSL
SDLLYALTLP LWINYTWNKD NWTFSPTLCK GSVFFTYMNF YSSTAFLTCI ALDRYLAVVY
PLKFSFLRTR RFAFITSLSI WILESFFNSM LLWKDETSVE YCDSDKSNFT LCYDKYPLEK
WQINLNLFRT CMGYAIPLIT IMICNHKVYR AVRHNQATEN SEKRRIIKLL ASITLTFVLC
FTPFHVMVLI RCVLERDMNV NDKSGWQTFT VYRVTVALTS LNCVADPILY CFVTETGRAD
MWNILKLCTR KHNRHQGQKR DILSVSTRDA VELEIID
