RXFP1_HUMAN
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 03-AUG-2022, entry version 185.
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}.
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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 PDBsum; 2JM4; -.
DR PDBsum; 2M7P; -.
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 GlyGen; Q9HBX9; 6 sites.
DR iPTMnet; Q9HBX9; -.
DR PhosphoSitePlus; Q9HBX9; -.
DR BioMuta; RXFP1; -.
DR DMDM; 166209887; -.
DR MassIVE; Q9HBX9; -.
DR MaxQB; Q9HBX9; -.
DR PaxDb; Q9HBX9; -.
DR PeptideAtlas; Q9HBX9; -.
DR PRIDE; Q9HBX9; -.
DR ProteomicsDB; 4211; -.
DR ProteomicsDB; 81607; -. [Q9HBX9-1]
DR ProteomicsDB; 81608; -. [Q9HBX9-2]
DR ABCD; Q9HBX9; 9 sequenced antibodies.
DR Antibodypedia; 7543; 327 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 CTD; 59350; -.
DR DisGeNET; 59350; -.
DR GeneCards; RXFP1; -.
DR HGNC; HGNC:19718; RXFP1.
DR HPA; ENSG00000171509; Tissue enhanced (adrenal gland, 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 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 Reactome; R-HSA-9660821; ADORA2B mediated anti-inflammatory cytokines production.
DR SignaLink; Q9HBX9; -.
DR SIGNOR; Q9HBX9; -.
DR BioGRID-ORCS; 59350; 9 hits in 1060 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 106 other tissues.
DR ExpressionAtlas; Q9HBX9; baseline and differential.
DR Genevisible; Q9HBX9; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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: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: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; cd00112; LDLa; 1.
DR Gene3D; 3.80.10.10; -; 2.
DR Gene3D; 4.10.400.10; -; 1.
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 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; 9.
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 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"
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
