RL3R1_HUMAN
ID RL3R1_HUMAN Reviewed; 469 AA.
AC Q9NSD7; Q14DA5;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Relaxin-3 receptor 1;
DE Short=RLN3 receptor 1;
DE AltName: Full=G protein-coupled receptor SALPR;
DE AltName: Full=G-protein coupled receptor GPCR135;
DE AltName: Full=Relaxin family peptide receptor 3;
DE AltName: Full=Somatostatin- and angiotensin-like peptide receptor;
GN Name=RXFP3; Synonyms=GPCR135, RLN3R1, SALPR;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain cortex;
RX PubMed=10806363; DOI=10.1016/s0378-1119(00)00123-2;
RA Matsumoto M., Kamohara M., Sugimoto T., Hidaka K., Takasaki J., Saito T.,
RA Okada M., Yamaguchi T., Furuichi K.;
RT "The novel G-protein coupled receptor SALPR shares sequence similarity with
RT somatostatin and angiotensin receptors.";
RL Gene 248:183-189(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kopatz S.A., Aronstam R.S., Sharma S.V.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION AS A RECEPTOR FOR RLN3.
RX PubMed=14522968; DOI=10.1074/jbc.m308995200;
RA Liu C., Eriste E., Sutton S., Chen J., Roland B., Kuei C., Farmer N.,
RA Joernvall H., Sillard R., Lovenberg T.W.;
RT "Identification of relaxin-3/INSL7 as an endogenous ligand for the orphan
RT G-protein coupled receptor GPCR135.";
RL J. Biol. Chem. 278:50754-50764(2003).
RN [4]
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).
CC -!- FUNCTION: Receptor for RNL3/relaxin-3. Binding of the ligand inhibit
CC cAMP accumulation. {ECO:0000269|PubMed:14522968}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in brain regions. Highest
CC expression in substantia nigra and pituitary, followed by hippocampus,
CC spinal cord, amygdala, caudate nucleus and corpus callosum, quite low
CC level in cerebellum. In peripheral tissues, relatively high levels in
CC adrenal glands, low levels in pancreas, salivary gland, placenta,
CC mammary gland and testis.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; D88437; BAA93001.1; -; mRNA.
DR EMBL; AY236541; AAO92063.1; -; Genomic_DNA.
DR EMBL; AY394501; AAQ92315.1; -; mRNA.
DR EMBL; BC113438; AAI13439.1; -; mRNA.
DR EMBL; BC113440; AAI13441.1; -; mRNA.
DR CCDS; CCDS3900.1; -.
DR RefSeq; NP_057652.1; NM_016568.3.
DR AlphaFoldDB; Q9NSD7; -.
DR SMR; Q9NSD7; -.
DR BioGRID; 119440; 10.
DR IntAct; Q9NSD7; 8.
DR MINT; Q9NSD7; -.
DR STRING; 9606.ENSP00000328708; -.
DR BindingDB; Q9NSD7; -.
DR ChEMBL; CHEMBL1628472; -.
DR GuidetoPHARMACOLOGY; 353; -.
DR TCDB; 9.A.14.13.21; the g-protein-coupled receptor (gpcr) family.
DR GlyGen; Q9NSD7; 2 sites.
DR iPTMnet; Q9NSD7; -.
DR PhosphoSitePlus; Q9NSD7; -.
DR BioMuta; RXFP3; -.
DR DMDM; 20455271; -.
DR jPOST; Q9NSD7; -.
DR PaxDb; Q9NSD7; -.
DR PRIDE; Q9NSD7; -.
DR ProteomicsDB; 82537; -.
DR Antibodypedia; 9933; 279 antibodies from 30 providers.
DR DNASU; 51289; -.
DR Ensembl; ENST00000330120.5; ENSP00000328708.3; ENSG00000182631.7.
DR Ensembl; ENST00000616205.2; ENSP00000480733.1; ENSG00000277069.2.
DR GeneID; 51289; -.
DR KEGG; hsa:51289; -.
DR MANE-Select; ENST00000330120.5; ENSP00000328708.3; NM_016568.3; NP_057652.1.
DR UCSC; uc003jic.3; human.
DR CTD; 51289; -.
DR DisGeNET; 51289; -.
DR GeneCards; RXFP3; -.
DR HGNC; HGNC:24883; RXFP3.
DR HPA; ENSG00000182631; Tissue enhanced (brain).
DR MIM; 609445; gene.
DR neXtProt; NX_Q9NSD7; -.
DR OpenTargets; ENSG00000182631; -.
DR PharmGKB; PA134868535; -.
DR VEuPathDB; HostDB:ENSG00000182631; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01030000234518; -.
DR HOGENOM; CLU_009579_8_1_1; -.
DR InParanoid; Q9NSD7; -.
DR OMA; IVTSMNM; -.
DR OrthoDB; 880755at2759; -.
DR PhylomeDB; Q9NSD7; -.
DR TreeFam; TF330024; -.
DR PathwayCommons; Q9NSD7; -.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR Reactome; R-HSA-444821; Relaxin receptors.
DR SignaLink; Q9NSD7; -.
DR BioGRID-ORCS; 51289; 9 hits in 1060 CRISPR screens.
DR GeneWiki; Relaxin/insulin-like_family_peptide_receptor_3; -.
DR GenomeRNAi; 51289; -.
DR Pharos; Q9NSD7; Tchem.
DR PRO; PR:Q9NSD7; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9NSD7; protein.
DR Bgee; ENSG00000182631; Expressed in adrenal tissue and 11 other tissues.
DR Genevisible; Q9NSD7; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0008528; F:G protein-coupled peptide receptor activity; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; TAS:ProtInc.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central.
DR GO; GO:0032467; P:positive regulation of cytokinesis; IMP:UniProtKB.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..469
FT /note="Relaxin-3 receptor 1"
FT /id="PRO_0000070104"
FT TOPO_DOM 1..81
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..102
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 103..119
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 120..140
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 141..156
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 178..215
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..236
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 237..270
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 271..291
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 292..329
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 330..350
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 351..356
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 357..377
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 378..469
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 36
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 40
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 155..247
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 469 AA; 51124 MW; 932E7B3001689F7B CRC64;
MQMADAATIA TMNKAAGGDK LAELFSLVPD LLEAANTSGN ASLQLPDLWW ELGLELPDGA
PPGHPPGSGG AESADTEARV RILISVVYWV VCALGLAGNL LVLYLMKSMQ GWRKSSINLF
VTNLALTDFQ FVLTLPFWAV ENALDFKWPF GKAMCKIVSM VTSMNMYASV FFLTAMSVTR
YHSVASALKS HRTRGHGRGD CCGRSLGDSC CFSAKALCVW IWALAALASL PSAIFSTTVK
VMGEELCLVR FPDKLLGRDR QFWLGLYHSQ KVLLGFVLPL GIIILCYLLL VRFIADRRAA
GTKGGAAVAG GRPTGASARR LSKVTKSVTI VVLSFFLCWL PNQALTTWSI LIKFNAVPFS
QEYFLCQVYA FPVSVCLAHS NSCLNPVLYC LVRREFRKAL KSLLWRIASP SITSMRPFTA
TTKPEHEDQG LQAPAPPHAA AEPDLLYYPP GVVVYSGGRY DLLPSSSAY
