RXFP2_CANLF
ID RXFP2_CANLF Reviewed; 737 AA.
AC Q5XM32;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Relaxin receptor 2;
DE AltName: Full=INSL3 receptor;
DE AltName: Full=Leucine-rich repeat-containing G-protein coupled receptor 8;
DE AltName: Full=Relaxin family peptide receptor 2;
GN Name=RXFP2; Synonyms=LGR8;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=White shepherd;
RA Agoulnik A.I.;
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AY749634; AAU95071.1; -; mRNA.
DR RefSeq; NP_001005870.1; NM_001005870.1.
DR AlphaFoldDB; Q5XM32; -.
DR SMR; Q5XM32; -.
DR STRING; 9612.ENSCAFP00000009735; -.
DR PaxDb; Q5XM32; -.
DR Ensembl; ENSCAFT00000010501; ENSCAFP00000009735; ENSCAFG00000006501.
DR Ensembl; ENSCAFT00845035419; ENSCAFP00845027726; ENSCAFG00845019902.
DR GeneID; 450220; -.
DR KEGG; cfa:450220; -.
DR CTD; 122042; -.
DR VEuPathDB; HostDB:ENSCAFG00845019902; -.
DR VGNC; VGNC:54989; RXFP2.
DR eggNOG; KOG0619; Eukaryota.
DR eggNOG; KOG2087; Eukaryota.
DR GeneTree; ENSGT00940000158948; -.
DR InParanoid; Q5XM32; -.
DR OrthoDB; 559381at2759; -.
DR Proteomes; UP000002254; Chromosome 25.
DR Bgee; ENSCAFG00000006501; Expressed in thymus and 3 other tissues.
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:0016500; F:protein-hormone receptor activity; IEA:Ensembl.
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; IBA:GO_Central.
DR GO; GO:0009755; P:hormone-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0008584; P:male gonad development; IEA:Ensembl.
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; 3.
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; 9.
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_0000069701"
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 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"
SQ SEQUENCE 737 AA; 84109 MW; 2FC61629E851132D CRC64;
MFPLLHFIVL IDVKDFPLTE GSTITPLCQK GYFPCGNLTK CLPRAFHCDG VDDCGNGADE
DNCGDTSGWA TIFGTVHGNA NNVALTQECF LNQYPQPCDC KGTELECINA DLRAVPVISS
NTTLLSLKKN KIHSLPDKVF TKYTQLKQIF LQHNCITHIS RKAFFGLHNL QILYLSHNCI
TTLRPGVFKD LHQLTWLILD DNPITRISQQ LFTGLKSLFF LSMVNNYLEA LPKQMCAQMP
QLNWMDLEGN GIKYLTNSSF LSCNSLTVLF LPRNQIDFVP EKTFSSLKNL GELDLSSNMI
MELPPEIFKD LKLLQKLNLS SNPLLYLHKN QFESLKQLQS LDLERIEIPN INTRMFQPMM
NLSHIYFKNF RYCSYAPHVR ICMPLTDGIS SFEDLLANNI LRIFVWVIAF ITCFGNLFVI
GMRSFIKAEN TTHATSIKIL CCADCLMGVY LFFIGFFDIK YRGQYQKYAL LWMESLQCRL
MGFLAMLSTE VSVLLLTYLT LEKFLAIVFP FSNIRPGKWQ TMVILICIWI VGFLIAVIPF
WKEDYFGNFY GKNGVCFPLY YDQTEDIGSK GYSLGIFLGV NLLAFLIIVF SYTIMFCSIK
KTALQTSEVR NPIGREVAVA NRFFFIVFSD AICWIPVFVI KILSLFRVEI PGTITSWIVI
FFLPVNSALN PILYTLTTSF FKDKLKQLLH KHRRKSIFKT KKKSLSTSIV WTDDSSSLKL
GVLNKITLGD SIVKPIS