ID RXFP1_HUMAN Reviewed; 757 AA. AC Q9HBX9; B4DHD1; B4DTV2; Q2M215; Q3KU24; Q3KU25; Q3KU26; DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot. DT 04-DEC-2007, sequence version 2. DT 24-JAN-2024, entry version 193. 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 Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND MUTAGENESIS OF ASP-637. RX PubMed=10935549; DOI=10.1210/mend.14.8.0510; RA Hsu S.Y., Kudo M., Chen T., Nakabayashi K., Bhalla A., van der Spek P.J., RA van Duin M., Hsueh A.J.W.; RT "The three subfamilies of leucine-rich repeat-containing G protein-coupled RT receptors (LGR): identification of LGR6 and LGR7 and the signaling RT mechanism for LGR7."; RL Mol. Endocrinol. 14:1257-1271(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4), SUBCELLULAR LOCATION, AND RP TISSUE SPECIFICITY. RX PubMed=16051677; DOI=10.1093/molehr/gah205; RA Muda M., He C., Martini P.G.V., Ferraro T., Layfield S., Taylor D., RA Chevrier C., Schweickhardt R., Kelton C., Ryan P.L., Bathgate R.A.D.; RT "Splice variants of the relaxin and INSL3 receptors reveal unanticipated RT molecular complexity."; RL Mol. Hum. Reprod. 11:591-600(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 5). RC TISSUE=Brain, and Placenta; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain cortex; 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). RN [7] RP CHARACTERIZATION. RX PubMed=11517286; DOI=10.1093/molehr/7.9.799; RA Bartsch O., Bartlick B., Ivell R.; RT "Relaxin signalling links tyrosine phosphorylation to phosphodiesterase and RT adenylyl cyclase activity."; RL Mol. Hum. Reprod. 7:799-809(2001). RN [8] RP INTERACTION WITH RLN3. RX PubMed=12506116; DOI=10.1074/jbc.m212457200; RA Sudo S., Kumagai J., Nishi S., Layfield S., Ferraro T., Bathgate R.A.D., RA Hsueh A.J.W.; RT "H3 relaxin is a specific ligand for LGR7 and activates the receptor by RT interacting with both the ectodomain and the exoloop 2."; RL J. Biol. Chem. 278:7855-7862(2003). RN [9] RP GLYCOSYLATION AT ASN-36; ASN-127; ASN-264; ASN-272; ASN-325 AND ASN-368. RX PubMed=18533687; DOI=10.1021/bi800535b; RA Yan Y., Scott D.J., Wilkinson T.N., Ji J., Tregear G.W., Bathgate R.A.; RT "Identification of the N-linked glycosylation sites of the human relaxin RT receptor and effect of glycosylation on receptor function."; RL Biochemistry 47:6953-6968(2008). RN [10] RP INTERACTION WITH C1QTNF8. RX PubMed=24014093; DOI=10.1002/path.4257; RA Glogowska A., Kunanuvat U., Stetefeld J., Patel T.R., Thanasupawat T., RA Krcek J., Weber E., Wong G.W., Del Bigio M.R., Hoang-Vu C., RA Hombach-Klonisch S., Klonisch T.; RT "C1q-tumour necrosis factor-related protein 8 (CTRP8) is a novel RT interaction partner of relaxin receptor RXFP1 in human brain cancer RT cells."; RL J. Pathol. 231:466-479(2013). RN [11] RP STRUCTURE BY NMR OF 23-63 IN COMPLEX WITH CALCIUM IONS. RX PubMed=17148455; DOI=10.1074/jbc.m609526200; RA Hopkins E.J., Layfield S., Ferraro T., Bathgate R.A.D., Gooley P.R.; RT "The NMR solution structure of the relaxin (RXFP1) receptor lipoprotein RT receptor class A module and identification of key residues in the N- RT terminal region of the module that mediate receptor activation."; RL J. Biol. Chem. 282:4172-4184(2007). 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. CC -!- SUBUNIT: Interacts with C1QTNF8. {ECO:0000269|PubMed:24014093}. CC -!- INTERACTION: CC Q9HBX9; P24588: AKAP5; NbExp=2; IntAct=EBI-8088969, EBI-703640; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16051677}; CC Multi-pass membrane protein {ECO:0000269|PubMed:16051677}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; CC IsoId=Q9HBX9-1; Sequence=Displayed; CC Name=2; Synonyms=LGR7.10; CC IsoId=Q9HBX9-2; Sequence=VSP_001984; CC Name=3; Synonyms=LGR7.1; CC IsoId=Q9HBX9-3; Sequence=VSP_029877, VSP_029878; CC Name=4; Synonyms=LGR7.2; CC IsoId=Q9HBX9-4; Sequence=VSP_029879; CC Name=5; CC IsoId=Q9HBX9-5; Sequence=VSP_054375, VSP_054376; CC -!- TISSUE SPECIFICITY: Expressed in the brain, kidney, testis, placenta, CC uterus, ovary, adrenal, prostate, skin and heart. Not detected in CC spleen. {ECO:0000269|PubMed:16051677}. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC {ECO:0000255|PROSITE-ProRule:PRU00521}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF190500; AAG17167.1; -; mRNA. DR EMBL; AY899848; AAX85196.1; -; mRNA. DR EMBL; AY899849; AAX85197.1; -; mRNA. DR EMBL; AY899850; AAX85198.1; -; mRNA. DR EMBL; AK295040; BAG58092.1; -; mRNA. DR EMBL; AK300379; BAG62114.1; -; mRNA. DR EMBL; AC019341; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC107056; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC107219; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC108017; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC121161; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC125489; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471056; EAX04856.1; -; Genomic_DNA. DR EMBL; BC112142; AAI12143.1; -; mRNA. DR EMBL; BC113617; AAI13618.1; -; mRNA. DR CCDS; CCDS43276.1; -. [Q9HBX9-1] DR CCDS; CCDS58929.1; -. [Q9HBX9-4] DR CCDS; CCDS58930.1; -. [Q9HBX9-2] DR RefSeq; NP_001240657.1; NM_001253728.1. [Q9HBX9-2] DR RefSeq; NP_001240658.1; NM_001253729.1. [Q9HBX9-4] DR RefSeq; NP_067647.2; NM_021634.3. [Q9HBX9-1] DR PDB; 2JM4; NMR; -; A=23-63. DR PDB; 2M7P; NMR; -; A=28-39. DR PDB; 7TMW; EM; 3.20 A; R=23-737. DR PDBsum; 2JM4; -. DR PDBsum; 2M7P; -. DR PDBsum; 7TMW; -. DR AlphaFoldDB; Q9HBX9; -. DR SASBDB; Q9HBX9; -. DR SMR; Q9HBX9; -. DR BioGRID; 121891; 86. DR IntAct; Q9HBX9; 5. DR MINT; Q9HBX9; -. DR STRING; 9606.ENSP00000405841; -. DR BindingDB; Q9HBX9; -. DR ChEMBL; CHEMBL1293316; -. DR GuidetoPHARMACOLOGY; 351; -. DR TCDB; 9.A.14.1.19; the g-protein-coupled receptor (gpcr) family. DR GlyCosmos; Q9HBX9; 6 sites, No reported glycans. DR GlyGen; Q9HBX9; 6 sites. DR iPTMnet; Q9HBX9; -. DR PhosphoSitePlus; Q9HBX9; -. DR BioMuta; RXFP1; -. DR DMDM; 166209887; -. DR MassIVE; Q9HBX9; -. DR MaxQB; Q9HBX9; -. DR PaxDb; 9606-ENSP00000405841; -. DR PeptideAtlas; Q9HBX9; -. DR ABCD; Q9HBX9; 9 sequenced antibodies. DR Antibodypedia; 7543; 377 antibodies from 33 providers. DR DNASU; 59350; -. DR Ensembl; ENST00000307765.10; ENSP00000303248.5; ENSG00000171509.16. [Q9HBX9-1] DR Ensembl; ENST00000343542.9; ENSP00000345889.5; ENSG00000171509.16. [Q9HBX9-4] DR Ensembl; ENST00000470033.2; ENSP00000420712.1; ENSG00000171509.16. [Q9HBX9-2] DR Ensembl; ENST00000471616.5; ENSP00000434475.1; ENSG00000171509.16. [Q9HBX9-3] DR GeneID; 59350; -. DR KEGG; hsa:59350; -. DR MANE-Select; ENST00000307765.10; ENSP00000303248.5; NM_021634.4; NP_067647.2. DR UCSC; uc003ipz.4; human. [Q9HBX9-1] DR AGR; HGNC:19718; -. DR CTD; 59350; -. DR DisGeNET; 59350; -. DR GeneCards; RXFP1; -. DR HGNC; HGNC:19718; RXFP1. DR HPA; ENSG00000171509; Tissue enhanced (brain, endometrium). DR MIM; 606654; gene. DR neXtProt; NX_Q9HBX9; -. DR OpenTargets; ENSG00000171509; -. DR PharmGKB; PA134868312; -. DR VEuPathDB; HostDB:ENSG00000171509; -. DR eggNOG; KOG0619; Eukaryota. DR eggNOG; KOG2087; Eukaryota. DR GeneTree; ENSGT00940000158241; -. DR HOGENOM; CLU_1431019_0_0_1; -. DR InParanoid; Q9HBX9; -. DR OrthoDB; 2913881at2759; -. DR PhylomeDB; Q9HBX9; -. DR TreeFam; TF326185; -. DR PathwayCommons; Q9HBX9; -. DR Reactome; R-HSA-418555; G alpha (s) signalling events. DR Reactome; R-HSA-444821; Relaxin receptors. DR SignaLink; Q9HBX9; -. DR SIGNOR; Q9HBX9; -. DR BioGRID-ORCS; 59350; 10 hits in 1138 CRISPR screens. DR ChiTaRS; RXFP1; human. DR EvolutionaryTrace; Q9HBX9; -. DR GeneWiki; Relaxin/insulin-like_family_peptide_receptor_1; -. DR GenomeRNAi; 59350; -. DR Pharos; Q9HBX9; Tchem. DR PRO; PR:Q9HBX9; -. DR Proteomes; UP000005640; Chromosome 4. DR RNAct; Q9HBX9; Protein. DR Bgee; ENSG00000171509; Expressed in decidua and 108 other cell types or tissues. DR ExpressionAtlas; Q9HBX9; baseline and differential. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. 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:MGI. DR GO; GO:0042562; F:hormone binding; IEA:Ensembl. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central. DR GO; GO:0030198; P:extracellular matrix organization; IEA:Ensembl. DR GO; GO:0009755; P:hormone-mediated signaling pathway; IBA:GO_Central. DR GO; GO:0060427; P:lung connective tissue development; IEA:Ensembl. DR GO; GO:0036446; P:myofibroblast differentiation; IEA:Ensembl. DR GO; GO:0060658; P:nipple morphogenesis; IEA:Ensembl. DR GO; GO:0007567; P:parturition; IEA:Ensembl. DR CDD; cd15965; 7tmA_RXFP1_LGR7; 1. DR CDD; cd00112; LDLa; 1. DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 1. DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1. DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2. DR IDEAL; IID00681; -. 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 PANTHER; PTHR24372; GLYCOPROTEIN HORMONE RECEPTOR; 1. DR PANTHER; PTHR24372:SF68; RELAXIN RECEPTOR 1; 1. 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; SM00365; LRR_SD22; 4. DR SMART; SM00369; LRR_TYP; 9. DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1. DR SUPFAM; SSF52058; L domain-like; 1. DR SUPFAM; SSF57424; LDL receptor-like module; 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. DR Genevisible; Q9HBX9; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Calcium; Cell membrane; Disulfide bond; KW G-protein coupled receptor; Glycoprotein; Leucine-rich repeat; Membrane; KW Metal-binding; Receptor; Reference proteome; Repeat; Transducer; KW Transmembrane; Transmembrane helix. FT CHAIN 1..757 FT /note="Relaxin receptor 1" FT /id="PRO_0000069700" 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..757 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 DOMAIN 91..127 FT /note="LRRNT" FT REPEAT 151..172 FT /note="LRR 1" FT REPEAT 175..196 FT /note="LRR 2" FT REPEAT 199..220 FT /note="LRR 3" FT REPEAT 223..244 FT /note="LRR 4" FT REPEAT 248..269 FT /note="LRR 5" FT REPEAT 272..293 FT /note="LRR 6" FT REPEAT 296..317 FT /note="LRR 7" FT REPEAT 320..341 FT /note="LRR 8" FT REPEAT 344..365 FT /note="LRR 9" FT BINDING 45 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT BINDING 48 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT BINDING 50 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT BINDING 52 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT BINDING 58 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT BINDING 59 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT CARBOHYD 36 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:18533687" FT CARBOHYD 127 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:18533687" FT CARBOHYD 264 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:18533687" FT CARBOHYD 272 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:18533687" FT CARBOHYD 325 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:18533687" FT CARBOHYD 368 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:18533687" FT DISULFID 27..40 FT DISULFID 34..53 FT DISULFID 47..62 FT DISULFID 485..563 FT VAR_SEQ 1..81 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_054375" FT VAR_SEQ 63..96 FT /note="GDNNGWSLQFDKYFASYYKMTSQYPFEAETPECL -> V (in isoform FT 2)" FT /evidence="ECO:0000303|PubMed:10935549, FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:16051677" FT /id="VSP_001984" FT VAR_SEQ 180..189 FT /note="YLSHNRITFL -> SRAVKDGSEK (in isoform 3)" FT /evidence="ECO:0000303|PubMed:16051677" FT /id="VSP_029877" FT VAR_SEQ 190..757 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:16051677" FT /id="VSP_029878" FT VAR_SEQ 252..275 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_054376" FT VAR_SEQ 300..348 FT /note="LDLGSNKIENLPPLIFKDLKELSQLNLSYNPIQKIQANQFDYLVKLKSL -> FT F (in isoform 4)" FT /evidence="ECO:0000303|PubMed:16051677" FT /id="VSP_029879" FT MUTAGEN 637 FT /note="D->Y: Leads to constitutive increase of basal cAMP." FT /evidence="ECO:0000269|PubMed:10935549" FT CONFLICT 70 FT /note="L -> M (in Ref. 1; AAG17167)" FT /evidence="ECO:0000305" FT STRAND 31..33 FT /evidence="ECO:0007829|PDB:2JM4" FT STRAND 35..38 FT /evidence="ECO:0007829|PDB:2JM4" FT STRAND 40..42 FT /evidence="ECO:0007829|PDB:2JM4" FT HELIX 43..45 FT /evidence="ECO:0007829|PDB:2JM4" FT STRAND 53..55 FT /evidence="ECO:0007829|PDB:2JM4" FT HELIX 406..429 FT /evidence="ECO:0007829|PDB:7TMW" FT HELIX 438..467 FT /evidence="ECO:0007829|PDB:7TMW" FT STRAND 468..470 FT /evidence="ECO:0007829|PDB:7TMW" FT TURN 472..475 FT /evidence="ECO:0007829|PDB:7TMW" FT HELIX 476..481 FT /evidence="ECO:0007829|PDB:7TMW" FT HELIX 483..514 FT /evidence="ECO:0007829|PDB:7TMW" FT HELIX 525..548 FT /evidence="ECO:0007829|PDB:7TMW" FT HELIX 550..553 FT /evidence="ECO:0007829|PDB:7TMW" FT HELIX 574..583 FT /evidence="ECO:0007829|PDB:7TMW" FT TURN 584..587 FT /evidence="ECO:0007829|PDB:7TMW" FT HELIX 588..607 FT /evidence="ECO:0007829|PDB:7TMW" FT HELIX 625..652 FT /evidence="ECO:0007829|PDB:7TMW" FT HELIX 659..667 FT /evidence="ECO:0007829|PDB:7TMW" FT TURN 668..671 FT /evidence="ECO:0007829|PDB:7TMW" FT HELIX 672..680 FT /evidence="ECO:0007829|PDB:7TMW" FT TURN 681..683 FT /evidence="ECO:0007829|PDB:7TMW" FT HELIX 686..698 FT /evidence="ECO:0007829|PDB:7TMW" SQ SEQUENCE 757 AA; 86975 MW; B32DD71B1A5D5864 CRC64; MTSGSVFFYI LIFGKYFSHG GGQDVKCSLG YFPCGNITKC LPQLLHCNGV DDCGNQADED NCGDNNGWSL QFDKYFASYY KMTSQYPFEA ETPECLVGSV PVQCLCQGLE LDCDETNLRA VPSVSSNVTA MSLQWNLIRK LPPDCFKNYH DLQKLYLQNN KITSISIYAF RGLNSLTKLY LSHNRITFLK PGVFEDLHRL EWLIIEDNHL SRISPPTFYG LNSLILLVLM NNVLTRLPDK PLCQHMPRLH WLDLEGNHIH NLRNLTFISC SNLTVLVMRK NKINHLNENT FAPLQKLDEL DLGSNKIENL PPLIFKDLKE LSQLNLSYNP IQKIQANQFD YLVKLKSLSL EGIEISNIQQ RMFRPLMNLS HIYFKKFQYC GYAPHVRSCK PNTDGISSLE NLLASIIQRV FVWVVSAVTC FGNIFVICMR PYIRSENKLY AMSIISLCCA DCLMGIYLFV IGGFDLKFRG EYNKHAQLWM ESTHCQLVGS LAILSTEVSV LLLTFLTLEK YICIVYPFRC VRPGKCRTIT VLILIWITGF IVAFIPLSNK EFFKNYYGTN GVCFPLHSED TESIGAQIYS VAIFLGINLA AFIIIVFSYG SMFYSVHQSA ITATEIRNQV KKEMILAKRF FFIVFTDALC WIPIFVVKFL SLLQVEIPGT ITSWVVIFIL PINSALNPIL YTLTTRPFKE MIHRFWYNYR QRKSMDSKGQ KTYAPSFIWV EMWPLQEMPP ELMKPDLFTY PCEMSLISQS TRLNSYS //