RXFP1_RAT
ID RXFP1_RAT Reviewed; 758 AA.
AC Q6R6I6;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 112.
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=Lgr7;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
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).
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 (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:15566402}.
CC -!- SUBUNIT: Interacts with C1QTNF8. {ECO:0000250|UniProtKB:Q9HBX9}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15566402};
CC Multi-pass membrane protein {ECO:0000269|PubMed:15566402}.
CC -!- TISSUE SPECIFICITY: Detected in brain cortex, and at low levels in
CC testis. {ECO:0000269|PubMed:15566402}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AY509976; AAR97516.1; -; mRNA.
DR RefSeq; NP_958820.1; NM_201417.1.
DR AlphaFoldDB; Q6R6I6; -.
DR SMR; Q6R6I6; -.
DR STRING; 10116.ENSRNOP00000033541; -.
DR BindingDB; Q6R6I6; -.
DR ChEMBL; CHEMBL4739859; -.
DR GlyGen; Q6R6I6; 6 sites.
DR PhosphoSitePlus; Q6R6I6; -.
DR PaxDb; Q6R6I6; -.
DR PRIDE; Q6R6I6; -.
DR GeneID; 295144; -.
DR KEGG; rno:295144; -.
DR UCSC; RGD:1302973; rat.
DR CTD; 59350; -.
DR RGD; 1302973; Rxfp1.
DR eggNOG; KOG0619; Eukaryota.
DR eggNOG; KOG2087; Eukaryota.
DR InParanoid; Q6R6I6; -.
DR OrthoDB; 559381at2759; -.
DR PhylomeDB; Q6R6I6; -.
DR Reactome; R-RNO-444821; Relaxin receptors.
DR PRO; PR:Q6R6I6; -.
DR Proteomes; UP000002494; Unplaced.
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; IDA:RGD.
DR GO; GO:0042562; F:hormone binding; ISO:RGD.
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; IMP:RGD.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; ISO:RGD.
DR GO; GO:0030154; P:cell differentiation; ISO:RGD.
DR GO; GO:0030198; P:extracellular matrix organization; ISO:RGD.
DR GO; GO:0009755; P:hormone-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0060427; P:lung connective tissue development; ISO:RGD.
DR GO; GO:0060658; P:nipple morphogenesis; ISO:RGD.
DR GO; GO:0007567; P:parturition; ISO:RGD.
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_0000312669"
FT TOPO_DOM 1..408
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 409..429
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 430..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..660
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 661..681
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 682..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 105..125
FT /note="LRR 1"
FT REPEAT 126..148
FT /note="LRR 2"
FT REPEAT 149..172
FT /note="LRR 3"
FT REPEAT 173..196
FT /note="LRR 4"
FT REPEAT 198..220
FT /note="LRR 5"
FT REPEAT 221..244
FT /note="LRR 6"
FT REPEAT 246..269
FT /note="LRR 7"
FT REPEAT 270..293
FT /note="LRR 8"
FT REPEAT 294..317
FT /note="LRR 9"
FT REPEAT 319..341
FT /note="LRR 10"
FT REPEAT 342..365
FT /note="LRR 11"
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; 87183 MW; 85C2A295A5C0195B CRC64;
MTSGPFFFCV FIIGRYFTLG NAQDVSCPLG SFPCGNISKC LPQLLHCNGV DDCGNQADED
NCGDNNGWSL QLDKYFANYY KLTSTNSIEA ETSECLVGSV PMHCLCRDLE LDCDEANLRA
VPSVSSNVTV MSLQWNFIRT LPPNSFRKYH DLQKLCLQNN KIRSVSVSAF RGLHSLTKLY
LSHNRITFLK PGVFEDLHRL EWLIIEDNHL SRISPLTFYG LNSLILLVLM NNALTRLPDK
PLCQHMPRLH WLDFEGNRIH NLRNLTFISC NNLTVLVMRK NKINHLNEHA FTHLQKLDEL
DLGSNKIENL PPNIFKDLKE LSQLNISYNP IQKIEVNQFD YLAKLKSLSL EGIEISNIQQ
RMFRPLINLS HIYFKKFQYC GYAPHVRSCK PNTDGISSLE NLLASIIQRV FVWVVSAITC
FGNIFVICMR PYIRSENKLH AMSIMSLCCA DCLMGVYLFV IGAFDLKFRG EYRKHAQPWM
ESVHCQFMGS LAVLSTEVSV LLLTFLTLEK YICIVYPFRC LRPRKCRTVA VLIFIWITGF
IVAFAPLGNK EFFKNYYGTN GVCFPLHSED TGSTGAQIYS VVIFLGINLV AFIIIVFSYG
SMFYSVHQST ITATEIQKQV KKEMILAKRF FFIVFTDALC WIPIFILKFL SLIRVEIPDT
ITSWVVIFIL PINSALNPII YTLTTRPFKE MIHQLWYNYR QRRSVDRKGT QKAYTPSFIW
VEMWPLQEMS TEFMKPDAFT DPCDLSLVSR SSRLNSYS
