RXFP1_MOUSE
ID RXFP1_MOUSE Reviewed; 758 AA.
AC Q6R6I7; Q80UD3;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Relaxin receptor 1;
DE AltName: Full=Leucine-rich repeat-containing G-protein coupled receptor 7;
DE AltName: Full=Relaxin family peptide receptor 1;
GN Name=Rxfp1; Synonyms=Gm1018, Lgr7;
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 STRAIN=C57BL/6J;
RX PubMed=15566402; DOI=10.1111/j.1440-1681.2004.04075.x;
RA Scott D.J., Layfield S., Riesewijk A., Morita H., Tregear G.W.,
RA Bathgate R.A.D.;
RT "Identification and characterization of the mouse and rat relaxin receptors
RT as the novel orthologues of human leucine-rich repeat-containing G-protein-
RT coupled receptor 7.";
RL Clin. Exp. Pharmacol. Physiol. 31:828-832(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 389-420.
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: Receptor for relaxins. The activity of this receptor is
CC mediated by G proteins leading to stimulation of adenylate cyclase and
CC an increase of cAMP. Binding of the ligand may also activate a tyrosine
CC kinase pathway that inhibits the activity of a phosphodiesterase that
CC degrades cAMP. {ECO:0000269|PubMed:15566402}.
CC -!- SUBUNIT: Interacts with C1QTNF8. {ECO:0000250|UniProtKB:Q9HBX9}.
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; AY509975; AAR97515.1; -; mRNA.
DR EMBL; AY255542; AAO85054.1; -; mRNA.
DR CCDS; CCDS17420.1; -.
DR RefSeq; NP_997617.1; NM_212452.1.
DR AlphaFoldDB; Q6R6I7; -.
DR SMR; Q6R6I7; -.
DR BioGRID; 237962; 1.
DR STRING; 10090.ENSMUSP00000077611; -.
DR ChEMBL; CHEMBL3714701; -.
DR GlyGen; Q6R6I7; 6 sites.
DR PhosphoSitePlus; Q6R6I7; -.
DR MaxQB; Q6R6I7; -.
DR PaxDb; Q6R6I7; -.
DR PeptideAtlas; Q6R6I7; -.
DR PRIDE; Q6R6I7; -.
DR ProteomicsDB; 255429; -.
DR ABCD; Q6R6I7; 2 sequenced antibodies.
DR Antibodypedia; 7543; 327 antibodies from 33 providers.
DR DNASU; 381489; -.
DR Ensembl; ENSMUST00000078527; ENSMUSP00000077611; ENSMUSG00000034009.
DR GeneID; 381489; -.
DR KEGG; mmu:381489; -.
DR UCSC; uc008pnv.1; mouse.
DR CTD; 59350; -.
DR MGI; MGI:2682211; Rxfp1.
DR VEuPathDB; HostDB:ENSMUSG00000034009; -.
DR eggNOG; KOG0619; Eukaryota.
DR eggNOG; KOG2087; Eukaryota.
DR GeneTree; ENSGT00940000158241; -.
DR HOGENOM; CLU_006130_2_1_1; -.
DR InParanoid; Q6R6I7; -.
DR OMA; WITSWQC; -.
DR OrthoDB; 559381at2759; -.
DR PhylomeDB; Q6R6I7; -.
DR TreeFam; TF326185; -.
DR Reactome; R-MMU-418555; G alpha (s) signalling events.
DR Reactome; R-MMU-444821; Relaxin receptors.
DR BioGRID-ORCS; 381489; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Rxfp1; mouse.
DR PRO; PR:Q6R6I7; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q6R6I7; protein.
DR Bgee; ENSMUSG00000034009; Expressed in uterus and 26 other tissues.
DR ExpressionAtlas; Q6R6I7; baseline and differential.
DR Genevisible; Q6R6I7; MM.
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:0004930; F:G protein-coupled receptor activity; ISO:MGI.
DR GO; GO:0042562; F:hormone binding; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007190; P:activation of adenylate cyclase activity; IBA:GO_Central.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IDA:MGI.
DR GO; GO:0030198; P:extracellular matrix organization; IMP:MGI.
DR GO; GO:0009755; P:hormone-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0060427; P:lung connective tissue development; IMP:MGI.
DR GO; GO:0036446; P:myofibroblast differentiation; IMP:MGI.
DR GO; GO:0060658; P:nipple morphogenesis; IMP:MGI.
DR GO; GO:0007567; P:parturition; IMP:MGI.
DR CDD; cd00112; LDLa; 1.
DR Gene3D; 3.80.10.10; -; 2.
DR Gene3D; 4.10.400.10; -; 1.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR008112; Relaxin_rcpt.
DR Pfam; PF00001; 7tm_1; 1.
DR Pfam; PF00057; Ldl_recept_a; 1.
DR Pfam; PF13855; LRR_8; 2.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR01739; RELAXINR.
DR SMART; SM00192; LDLa; 1.
DR SMART; SM00369; LRR_TYP; 10.
DR SUPFAM; SSF57424; SSF57424; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR PROSITE; PS01209; LDLRA_1; 1.
DR PROSITE; PS50068; LDLRA_2; 1.
DR PROSITE; PS51450; LRR; 10.
PE 2: Evidence at transcript level;
KW Calcium; Cell membrane; Disulfide bond; G-protein coupled receptor;
KW Glycoprotein; Leucine-rich repeat; Membrane; Metal-binding; Receptor;
KW Reference proteome; Repeat; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..758
FT /note="Relaxin receptor 1"
FT /id="PRO_0000303887"
FT TOPO_DOM 1..409
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 410..430
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 431..443
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 444..464
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 465..486
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 487..507
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 508..527
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 528..548
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 549..577
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 578..598
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 599..629
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 630..650
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 651
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 652..672
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 673..758
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 26..63
FT /note="LDL-receptor class A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT REPEAT 127..148
FT /note="LRR 1"
FT REPEAT 151..172
FT /note="LRR 2"
FT REPEAT 175..196
FT /note="LRR 3"
FT REPEAT 199..220
FT /note="LRR 4"
FT REPEAT 223..244
FT /note="LRR 5"
FT REPEAT 248..269
FT /note="LRR 6"
FT REPEAT 272..293
FT /note="LRR 7"
FT REPEAT 296..317
FT /note="LRR 8"
FT REPEAT 320..341
FT /note="LRR 9"
FT REPEAT 344..365
FT /note="LRR 10"
FT BINDING 45
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 48
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 50
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 52
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 58
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 59
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT CARBOHYD 36
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 264
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 272
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 325
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 27..40
FT /evidence="ECO:0000250"
FT DISULFID 34..53
FT /evidence="ECO:0000250"
FT DISULFID 47..62
FT /evidence="ECO:0000250"
FT DISULFID 485..563
FT /evidence="ECO:0000250"
SQ SEQUENCE 758 AA; 86957 MW; 10D62BE70EC336E6 CRC64;
MTSGPFFFCI FIIGKYFTLG SAQDVSCPLG SFPCGNMSRC LPQLLHCNGV DDCGNRADED
HCGDNNGWSL QLDKYFANYY KLASTNSFEA ETSECLVGSV PMHCLCRDLE LDCDEANLRA
VPSVSSNVTV MSLQRNFIRT LPPNGFRKYH ELQKLCLQNN RIHSVSVSAF RGLRSLTKLY
LSHNRITFLK PGVFEDLHRL EWLIIEDNHL SRISPLTFYG LNSLILLVLM NNALTRLPDK
PLCQHMPRLH WLDFEGNRIH NLRNLTFISC NNLTVLVMRK NKINYLNEHA FTHLQKLDEL
DLGSNKIENL PPNIFKDLKE LSQLNISYNP IQKIEVNQFD CLAKLKSLSL EGIEISNIQQ
RMFRPLINLS HIYFKKFQYC GYAPHVRSCK PNTDGISSLE NLLASIIQRV FVWVVSAITC
FGNIFVICMR PYIRSENKLH AMSIISLCCA DCLMGVYLFV IGAFDLKFRG EYNKHAQPWM
ESVHCQFMGS LAILSTEVSV LLLTFLTLEK YICIVYPFRC LRPRKCRTIT VLIFIWIIGF
IVAFAPLGNK EFFKNYYGTN GVCFPLHSED TGSTGAQIYS VVIFLGINLV AFIIIVFSYG
SMFYSVHQSS VTVTEIQKQV KKEVVLAKRF FFIVFTDALC WIPIFILKFL SLLQVEIPDS
ITSWVVIFIL PINSALNPII YTLTTRPFKE MIHQLWHNYR QRRSVDRKET QKAYAPSFIW
VEMWPLQEMS SGFMKPGAFT DPCDLSLVSQ SSRLNSYS
