RL3R2_MOUSE
ID RL3R2_MOUSE Reviewed; 414 AA.
AC Q7TQP4; Q80UD6;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Relaxin-3 receptor 2;
DE Short=RLN3 receptor 2;
DE AltName: Full=G-protein coupled receptor 100;
DE AltName: Full=Insulin-like peptide INSL5 receptor;
DE AltName: Full=Relaxin family peptide receptor 4;
GN Name=Rxfp4; Synonyms=Gpr100, Rln3r2;
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].
RX PubMed=14623098; DOI=10.1016/s0014-5793(03)01196-7;
RA Fredriksson R., Hoeglund P.J., Gloriam D.E.I., Lagerstroem M.C.,
RA Schioeth H.B.;
RT "Seven evolutionarily conserved human rhodopsin G protein-coupled receptors
RT lacking close relatives.";
RL FEBS Lett. 554:381-388(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 41-159.
RX PubMed=12679517; DOI=10.1073/pnas.0230374100;
RA Vassilatis D.K., Hohmann J.G., Zeng H., Li F., Ranchalis J.E.,
RA Mortrud M.T., Brown A., Rodriguez S.S., Weller J.R., Wright A.C.,
RA Bergmann J.E., Gaitanaris G.A.;
RT "The G protein-coupled receptor repertoires of human and mouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:4903-4908(2003).
CC -!- FUNCTION: High affinity receptor for INSL5. Also acts as receptor for
CC RLN3/relaxin-3, as well as bradykinin and kallidin. Binding of the
CC ligand inhibit cAMP accumulation (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Detected only in bone marrow.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AY288422; AAP72131.1; -; mRNA.
DR EMBL; AY255539; AAO85051.1; -; mRNA.
DR CCDS; CCDS17482.1; -.
DR RefSeq; NP_861538.1; NM_181817.1.
DR AlphaFoldDB; Q7TQP4; -.
DR SMR; Q7TQP4; -.
DR STRING; 10090.ENSMUSP00000058732; -.
DR GuidetoPHARMACOLOGY; 354; -.
DR GlyGen; Q7TQP4; 2 sites.
DR PhosphoSitePlus; Q7TQP4; -.
DR PaxDb; Q7TQP4; -.
DR PRIDE; Q7TQP4; -.
DR Antibodypedia; 20424; 170 antibodies from 24 providers.
DR DNASU; 242093; -.
DR Ensembl; ENSMUST00000063119; ENSMUSP00000058732; ENSMUSG00000049741.
DR GeneID; 242093; -.
DR KEGG; mmu:242093; -.
DR UCSC; uc008pwc.1; mouse.
DR CTD; 339403; -.
DR MGI; MGI:2182926; Rxfp4.
DR VEuPathDB; HostDB:ENSMUSG00000049741; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01030000234534; -.
DR HOGENOM; CLU_009579_8_1_1; -.
DR InParanoid; Q7TQP4; -.
DR OMA; LWVLGNC; -.
DR OrthoDB; 880755at2759; -.
DR PhylomeDB; Q7TQP4; -.
DR TreeFam; TF330024; -.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR Reactome; R-MMU-444821; Relaxin receptors.
DR BioGRID-ORCS; 242093; 2 hits in 73 CRISPR screens.
DR PRO; PR:Q7TQP4; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q7TQP4; protein.
DR ExpressionAtlas; Q7TQP4; baseline and differential.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0008528; F:G protein-coupled peptide receptor activity; IBA:GO_Central.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central.
DR GO; GO:2000253; P:positive regulation of feeding behavior; IMP:MGI.
DR InterPro; IPR000248; ATII_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00241; ANGIOTENSINR.
DR PRINTS; PR00237; GPCRRHODOPSN.
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..414
FT /note="Relaxin-3 receptor 2"
FT /id="PRO_0000070107"
FT TOPO_DOM 1..43
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 44..64
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 65..77
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..98
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 99..116
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 117..137
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 138..155
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..176
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 177..209
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..230
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 231..255
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 256..276
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 277..293
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 294..316
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 317..414
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 5
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 17
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 114..191
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 41
FT /note="M -> L (in Ref. 2; AAO85051)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 414 AA; 45460 MW; EBB47A1C62E6DB0B CRC64;
MATSNSSASL PTLFWVNGSG DSVLSTDGAA MPVQFLVLRI MVALAYGLVG IIGLLGNLAV
LWVLGNCGQR VPGLSSDTFV FSLALADLGL ALTLPFWATE SAMDFHWPFG SALCKVVLTT
TVLSIYASTF LITALSIARY WVVAMAVGPG SHLSVFWARV VTLAVWVAAA LVTVPTAIFG
AEVELWGVCL CLLRFPSRYW LGAYQLQRVV LAFIVPLGVI TTSYLLLLAF LERQQRCRPR
QWQDSRVVAR SVRVLVASFA LCWVPNHVVT LWEILVRFDL VPWDSTFYTF HTYILPITTC
LAHSNSCLNP VIYCLLRREP QQVLVSSFRA LWSRLWPQRK ACMEQMALKE VGGRTVASTQ
ESGSSRTHTN TMEHLDEGCS LNTLLSETYQ GQSPQILGRS SCSLSQAAVS PGEV
