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Database: UniProt
Entry: Q6R6I7
LinkDB: Q6R6I7
Original site: Q6R6I7 
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   08-MAY-2019, entry version 120.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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
RT   receptors as the novel orthologues of human leucine-rich repeat-
RT   containing G-protein-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
CC       and an increase of cAMP. Binding of the ligand may also activate a
CC       tyrosine kinase pathway that inhibits the activity of a
CC       phosphodiesterase that degrades cAMP.
CC       {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}.
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   STRING; 10090.ENSMUSP00000077611; -.
DR   ChEMBL; CHEMBL3714701; -.
DR   PhosphoSitePlus; Q6R6I7; -.
DR   MaxQB; Q6R6I7; -.
DR   PaxDb; Q6R6I7; -.
DR   PeptideAtlas; Q6R6I7; -.
DR   PRIDE; Q6R6I7; -.
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   eggNOG; KOG0619; Eukaryota.
DR   eggNOG; KOG2087; Eukaryota.
DR   eggNOG; COG4886; LUCA.
DR   GeneTree; ENSGT00940000158241; -.
DR   HOGENOM; HOG000049056; -.
DR   InParanoid; Q6R6I7; -.
DR   KO; K04306; -.
DR   OMA; HAQLWMD; -.
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   ChiTaRS; Rxfp1; mouse.
DR   PRO; PR:Q6R6I7; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   Bgee; ENSMUSG00000034009; Expressed in 27 organ(s), highest expression level in uterus.
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:0030154; P:cell differentiation; IMP: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: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; Complete proteome; Disulfide bond;
KW   G-protein coupled receptor; Glycoprotein; Leucine-rich repeat;
KW   Membrane; Metal-binding; Receptor; Reference proteome; Repeat;
KW   Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN         1    758       Relaxin receptor 1.
FT                                /FTId=PRO_0000303887.
FT   TOPO_DOM      1    409       Extracellular. {ECO:0000255}.
FT   TRANSMEM    410    430       Helical; Name=1. {ECO:0000255}.
FT   TOPO_DOM    431    443       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    444    464       Helical; Name=2. {ECO:0000255}.
FT   TOPO_DOM    465    486       Extracellular. {ECO:0000255}.
FT   TRANSMEM    487    507       Helical; Name=3. {ECO:0000255}.
FT   TOPO_DOM    508    527       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    528    548       Helical; Name=4. {ECO:0000255}.
FT   TOPO_DOM    549    577       Extracellular. {ECO:0000255}.
FT   TRANSMEM    578    598       Helical; Name=5. {ECO:0000255}.
FT   TOPO_DOM    599    629       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    630    650       Helical; Name=6. {ECO:0000255}.
FT   TOPO_DOM    651    651       Extracellular. {ECO:0000255}.
FT   TRANSMEM    652    672       Helical; Name=7. {ECO:0000255}.
FT   TOPO_DOM    673    758       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       26     63       LDL-receptor class A.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   REPEAT      127    148       LRR 1.
FT   REPEAT      151    172       LRR 2.
FT   REPEAT      175    196       LRR 3.
FT   REPEAT      199    220       LRR 4.
FT   REPEAT      223    244       LRR 5.
FT   REPEAT      248    269       LRR 6.
FT   REPEAT      272    293       LRR 7.
FT   REPEAT      296    317       LRR 8.
FT   REPEAT      320    341       LRR 9.
FT   REPEAT      344    365       LRR 10.
FT   METAL        45     45       Calcium; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL        48     48       Calcium. {ECO:0000250}.
FT   METAL        50     50       Calcium; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL        52     52       Calcium. {ECO:0000250}.
FT   METAL        58     58       Calcium. {ECO:0000250}.
FT   METAL        59     59       Calcium. {ECO:0000250}.
FT   CARBOHYD     36     36       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    127    127       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    264    264       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    272    272       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    325    325       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    368    368       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     27     40       {ECO:0000250}.
FT   DISULFID     34     53       {ECO:0000250}.
FT   DISULFID     47     62       {ECO:0000250}.
FT   DISULFID    485    563       {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
//
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