RXFP2_MOUSE
ID RXFP2_MOUSE Reviewed; 737 AA.
AC Q91ZZ5; Q0VB90;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Relaxin receptor 2;
DE AltName: Full=G-protein coupled receptor 106;
DE AltName: Full=G-protein coupled receptor affecting testicular descent;
DE AltName: Full=Leucine-rich repeat-containing G-protein coupled receptor 8;
DE AltName: Full=Relaxin family peptide receptor 2;
GN Name=Rxfp2; Synonyms=Gpr106, Great, Lgr8;
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].
RC STRAIN=C57BL/6J;
RX PubMed=11353515; DOI=10.1002/gene.1029;
RA Overbeek P.A., Gorlov I.P., Sutherland R.W., Houston J.B., Harrison W.R.,
RA Boettger-Tong H.L., Bishop C.E., Agoulnik A.I.;
RT "A transgenic insertion causing cryptorchidism in mice.";
RL Genesis 30:26-35(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 relaxin. The activity of this receptor is
CC mediated by G proteins leading to stimulation of adenylate cyclase and
CC an increase of cAMP. May also be a receptor for Leydig insulin-like
CC peptide (INSL3) (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in embryonic and adult gonads of males
CC and females, as well in male gubernarculum. Expressed also in brain.
CC Not detected in kidney, spleen and heart.
CC -!- DISEASE: Note=Defects in Rxfp2 seems to be a cause of impaired
CC testicular descent (known as cryptorchidism).
CC {ECO:0000305|PubMed:11353515}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- CAUTION: By homology with the human sequence, it is uncertain whether
CC Met-1 is the initiator. {ECO:0000305}.
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DR EMBL; AF346501; AAL08943.1; -; mRNA.
DR EMBL; AC077689; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC120741; AAI20742.1; -; mRNA.
DR CCDS; CCDS19886.1; -.
DR RefSeq; NP_001276493.1; NM_001289564.1.
DR RefSeq; NP_001276495.1; NM_001289566.1.
DR RefSeq; NP_536716.2; NM_080468.2.
DR AlphaFoldDB; Q91ZZ5; -.
DR SMR; Q91ZZ5; -.
DR BioGRID; 228271; 1.
DR STRING; 10090.ENSMUSP00000067897; -.
DR ChEMBL; CHEMBL3714702; -.
DR GlyGen; Q91ZZ5; 6 sites.
DR iPTMnet; Q91ZZ5; -.
DR PhosphoSitePlus; Q91ZZ5; -.
DR PaxDb; Q91ZZ5; -.
DR PRIDE; Q91ZZ5; -.
DR ProteomicsDB; 256552; -.
DR Antibodypedia; 22835; 326 antibodies from 30 providers.
DR Ensembl; ENSMUST00000065745; ENSMUSP00000067897; ENSMUSG00000053368.
DR GeneID; 140498; -.
DR KEGG; mmu:140498; -.
DR UCSC; uc009ato.1; mouse.
DR CTD; 122042; -.
DR MGI; MGI:2153463; Rxfp2.
DR VEuPathDB; HostDB:ENSMUSG00000053368; -.
DR eggNOG; KOG0619; Eukaryota.
DR eggNOG; KOG2087; Eukaryota.
DR GeneTree; ENSGT00940000158948; -.
DR InParanoid; Q91ZZ5; -.
DR OMA; DNIGWAD; -.
DR OrthoDB; 559381at2759; -.
DR PhylomeDB; Q91ZZ5; -.
DR TreeFam; TF326185; -.
DR Reactome; R-MMU-418555; G alpha (s) signalling events.
DR Reactome; R-MMU-444821; Relaxin receptors.
DR BioGRID-ORCS; 140498; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Rxfp2; mouse.
DR PRO; PR:Q91ZZ5; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q91ZZ5; protein.
DR Bgee; ENSMUSG00000053368; Expressed in mesothelium and 40 other tissues.
DR ExpressionAtlas; Q91ZZ5; baseline and differential.
DR Genevisible; Q91ZZ5; MM.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0008528; F:G protein-coupled peptide receptor activity; IBA:GO_Central.
DR GO; GO:0017046; F:peptide hormone binding; ISO:MGI.
DR GO; GO:0016500; F:protein-hormone receptor activity; IMP:MGI.
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:MGI.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0009755; P:hormone-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0008584; P:male gonad development; IMP:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0001556; P:oocyte maturation; ISO:MGI.
DR GO; GO:0043950; P:positive regulation of cAMP-mediated signaling; ISO: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 Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Leucine-rich repeat; Membrane; Receptor; Reference proteome; Repeat;
KW Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..737
FT /note="Relaxin receptor 2"
FT /id="PRO_0000069703"
FT TOPO_DOM 1..399
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 400..420
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 421..438
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 439..459
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 460..478
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 479..501
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 502..520
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 521..541
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 542..575
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 576..596
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 597..622
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 623..643
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 644..653
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 654..674
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 675..737
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 27..64
FT /note="LDL-receptor class A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT REPEAT 121..142
FT /note="LRR 1"
FT REPEAT 145..166
FT /note="LRR 2"
FT REPEAT 169..190
FT /note="LRR 3"
FT REPEAT 193..214
FT /note="LRR 4"
FT REPEAT 217..238
FT /note="LRR 5"
FT REPEAT 241..262
FT /note="LRR 6"
FT REPEAT 265..286
FT /note="LRR 7"
FT REPEAT 289..310
FT /note="LRR 8"
FT REPEAT 313..334
FT /note="LRR 9"
FT REPEAT 337..358
FT /note="LRR 10"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 318
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 350
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 361
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 28..41
FT /evidence="ECO:0000250"
FT DISULFID 35..54
FT /evidence="ECO:0000250"
FT DISULFID 48..63
FT /evidence="ECO:0000250"
FT DISULFID 478..556
FT /evidence="ECO:0000250"
FT CONFLICT 222
FT /note="S -> P (in Ref. 1; AAL08943)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 737 AA; 82934 MW; AF60F63538061E49 CRC64;
MWLLLHVILL TEVKDFALAD SSMVAPLCPK GYFPCGNLTK CLPRAFHCDG VDDCGNGADE
DNCGDTSGWT TIFGTVHGNV NKVTLTQECF LSQYPQHCYC RENELECVKA DLKAVPKVSS
NVTLLSLKKN KIHRLPVKVF SRYTELRKIY LQHNCITHIS RRAFLGLHNL QILYLSHNCI
TSLRPGIFKD LHQLAWLILD DNPITRISQK SFMGLNSLFF LSMVGNRLEA LPETLCAQMP
QLNWVDLANN GIKYITNSTF LTCDSLTVLF LPRNQIGFVP EKTFSSLKNL GELDLSSNMI
TKLPVHLFSD LHLLQKLNLS SNPLLYVHKN QFGSLKQLQS LDLERIEIPN ISTGMFQPMK
NLSHIYLKTF RYCSYVPHVR ICMPSTDGIS SSEDLLANGI LRVSVWVIAF ITCVGNFLVI
AVRSLIKAEN TTHAMSIKIL CCADCLMGVY LFSVGVFDIK YRGQYQKYAL LWMESVPCRL
LGFLATLSTE VSVLLLTFLT LEKFLVIVFP FSNLRLGKRQ TAVALASIWV VGFLIAAVPF
TREDYFGNFY GKNGVCFPLH YDQAEDFGSR GYSLGIFLGV NLLAFLVIVI SYVTMFCSIH
KTALQTAEVR SHIGKEVAVA NRFFFIVFSD AICWIPVFVV KILSLLQVEI PGTITSWIVV
FFLPVNSALN PILYTLTTSF FKDKLKQLLH KHRRKPIFKV KKKSLSASIV WTDESSLKLG
VLSKIALGDS IMKPVSP
