LOCUS NP_997617 758 aa linear ROD 08-AUG-2023
DEFINITION relaxin receptor 1 precursor [Mus musculus].
ACCESSION NP_997617 XP_355441
VERSION NP_997617.1
DBSOURCE REFSEQ: accession NM_212452.3
KEYWORDS RefSeq; RefSeq Select.
SOURCE Mus musculus (house mouse)
ORGANISM Mus musculus
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE 1 (residues 1 to 758)
AUTHORS Ye Q, Bhojwani A and Hu JK.
TITLE Understanding the development of oral epithelial organs through
single cell transcriptomic analysis
JOURNAL Development 149 (16) (2022)
PUBMED 35831953
REFERENCE 2 (residues 1 to 758)
AUTHORS Ng HH, Soula M, Rivas B, Wilson KJ, Marugan JJ and Agoulnik AI.
TITLE Anti-apoptotic and Matrix Remodeling Actions of a Small Molecule
Agonist of the Human Relaxin Receptor, ML290 in Mice With
Unilateral Ureteral Obstruction
JOURNAL Front Physiol 12, 650769 (2021)
PUBMED 34305630
REMARK Publication Status: Online-Only
REFERENCE 3 (residues 1 to 758)
AUTHORS Hu M, Wang Y, Liu Z, Yu Z, Guan K, Liu M, Wang M, Tan J and Huang
L.
TITLE Hepatic macrophages act as a central hub for relaxin-mediated
alleviation of liver fibrosis
JOURNAL Nat Nanotechnol 16 (4), 466-477 (2021)
PUBMED 33495618
REMARK GeneRIF: Hepatic macrophages act as a central hub for
relaxin-mediated alleviation of liver fibrosis.
REFERENCE 4 (residues 1 to 758)
AUTHORS Patil NA, Rosengren KJ, Separovic F, Wade JD, Bathgate RAD and
Hossain MA.
TITLE Relaxin family peptides: structure-activity relationship studies
JOURNAL Br J Pharmacol 174 (10), 950-961 (2017)
PUBMED 27922185
REMARK Review article
Erratum:[Br J Pharmacol. 2017 Dec;174(24):4836. PMID: 29235105]
REFERENCE 5 (residues 1 to 758)
AUTHORS Petrie EJ, Lagaida S, Sethi A, Bathgate RA and Gooley PR.
TITLE In a Class of Their Own - RXFP1 and RXFP2 are Unique Members of the
LGR Family
JOURNAL Front Endocrinol (Lausanne) 6, 137 (2015)
PUBMED 26441827
REMARK Review article
Publication Status: Online-Only
REFERENCE 6 (residues 1 to 758)
AUTHORS Ortinau S, Lin F, Wade JD, Tregear GW, Bathgate RA and Gundlach AL.
TITLE Insulin-relaxin family peptide signaling and receptors in mouse
brain membranes and neuronal cells
JOURNAL Ann N Y Acad Sci 1041, 211-215 (2005)
PUBMED 15956710
REMARK GeneRIF: expression of lgr7 in mouse brain membranes and neurons
REFERENCE 7 (residues 1 to 758)
AUTHORS Siebel AL, Gehring HM, Reytomas IG and Parry LJ.
TITLE Inhibition of oxytocin receptor and estrogen receptor-alpha
expression, but not relaxin receptors (LGR7), in the myometrium of
late pregnant relaxin gene knockout mice
JOURNAL Endocrinology 144 (10), 4272-4275 (2003)
PUBMED 12959965
REFERENCE 8 (residues 1 to 758)
AUTHORS Vassilatis DK, Hohmann JG, Zeng H, Li F, Ranchalis JE, Mortrud MT,
Brown A, Rodriguez SS, Weller JR, Wright AC, Bergmann JE and
Gaitanaris GA.
TITLE The G protein-coupled receptor repertoires of human and mouse
JOURNAL Proc Natl Acad Sci U S A 100 (8), 4903-4908 (2003)
PUBMED 12679517
REFERENCE 9 (residues 1 to 758)
AUTHORS Hsu SY, Nakabayashi K, Nishi S, Kumagai J, Kudo M, Sherwood OD and
Hsueh AJ.
TITLE Activation of orphan receptors by the hormone relaxin
JOURNAL Science 295 (5555), 671-674 (2002)
PUBMED 11809971
REFERENCE 10 (residues 1 to 758)
AUTHORS Hsu SY, Kudo M, Chen T, Nakabayashi K, Bhalla A, van der Spek PJ,
van Duin M and Hsueh AJ.
TITLE The three subfamilies of leucine-rich repeat-containing G
protein-coupled receptors (LGR): identification of LGR6 and LGR7
and the signaling mechanism for LGR7
JOURNAL Mol Endocrinol 14 (8), 1257-1271 (2000)
PUBMED 10935549
COMMENT VALIDATED REFSEQ: This record has undergone validation or
preliminary review. The reference sequence was derived from
AC159281.3 and AC122462.5.
On Aug 30, 2004 this sequence version replaced XP_355441.1.
Publication Note: This RefSeq record includes a subset of the
publications that are available for this gene. Please see the Gene
record to access additional publications.
##Evidence-Data-START##
Transcript exon combination :: SRR9219379.20980.1, AY509975.1
[ECO:0000332]
RNAseq introns :: mixed sample support SAMN00849374,
SAMN00849375 [ECO:0006172]
##Evidence-Data-END##
##RefSeq-Attributes-START##
RefSeq Select criteria :: based on conservation, expression,
longest protein
##RefSeq-Attributes-END##
FEATURES Location/Qualifiers
source 1..758
/organism="Mus musculus"
/strain="C57BL/6"
/db_xref="taxon:10090"
/chromosome="3"
/map="3 34.94 cM"
Protein 1..758
/product="relaxin receptor 1 precursor"
/note="relaxin receptor 1; leucine-rich repeat-containing
7; leucine-rich repeat-containing G-protein coupled
receptor 7; relaxin family peptide receptor 1"
/calculated_mol_wt=84527
sig_peptide 1..22
/inference="COORDINATES: ab initio prediction:SignalP:4.0"
/calculated_mol_wt=2448
Region 27..62
/region_name="LDLa"
/note="Low Density Lipoprotein Receptor Class A domain, a
cysteine-rich repeat that plays a central role in
mammalian cholesterol metabolism; the receptor protein
binds LDL and transports it into cells by endocytosis; 7
successive cysteine-rich repeats of about...; cd00112"
/db_xref="CDD:238060"
Site order(32,41,52..53)
/site_type="active"
/note="putative binding surface [active]"
/db_xref="CDD:238060"
Site 36
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000255; propagated from
UniProtKB/Swiss-Prot (Q6R6I7.1)"
Site order(45,48,52,58..59)
/site_type="other"
/note="calcium-binding site [ion binding]"
/db_xref="CDD:238060"
Site 55..59
/site_type="other"
/note="D-X-S-D-E motif"
/db_xref="CDD:238060"
Region 110..127
/region_name="leucine-rich repeat"
/note="leucine-rich repeat [structural motif]"
/db_xref="CDD:275378"
Region 111..281
/region_name="PPP1R42"
/note="protein phosphatase 1 regulatory subunit 42;
cl42388"
/db_xref="CDD:455733"
Region 127..148
/region_name="LRR 1"
/note="propagated from UniProtKB/Swiss-Prot (Q6R6I7.1)"
Site 127
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000255; propagated from
UniProtKB/Swiss-Prot (Q6R6I7.1)"
Region 128..151
/region_name="leucine-rich repeat"
/note="leucine-rich repeat [structural motif]"
/db_xref="CDD:275380"
Region 151..172
/region_name="LRR 2"
/note="propagated from UniProtKB/Swiss-Prot (Q6R6I7.1)"
Region 152..175
/region_name="leucine-rich repeat"
/note="leucine-rich repeat [structural motif]"
/db_xref="CDD:275380"
Region 175..196
/region_name="LRR 3"
/note="propagated from UniProtKB/Swiss-Prot (Q6R6I7.1)"
Region 176..199
/region_name="leucine-rich repeat"
/note="leucine-rich repeat [structural motif]"
/db_xref="CDD:275380"
Region 199..220
/region_name="LRR 4"
/note="propagated from UniProtKB/Swiss-Prot (Q6R6I7.1)"
Region 200..223
/region_name="leucine-rich repeat"
/note="leucine-rich repeat [structural motif]"
/db_xref="CDD:275380"
Region 223..244
/region_name="LRR 5"
/note="propagated from UniProtKB/Swiss-Prot (Q6R6I7.1)"
Region 224..248
/region_name="leucine-rich repeat"
/note="leucine-rich repeat [structural motif]"
/db_xref="CDD:275380"
Region 248..269
/region_name="LRR 6"
/note="propagated from UniProtKB/Swiss-Prot (Q6R6I7.1)"
Region 249..272
/region_name="leucine-rich repeat"
/note="leucine-rich repeat [structural motif]"
/db_xref="CDD:275380"
Site 264
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000255; propagated from
UniProtKB/Swiss-Prot (Q6R6I7.1)"
Region 272..331
/region_name="LRR_8"
/note="Leucine rich repeat; pfam13855"
/db_xref="CDD:404697"
Region 272..293
/region_name="LRR 7"
/note="propagated from UniProtKB/Swiss-Prot (Q6R6I7.1)"
Site 272
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000255; propagated from
UniProtKB/Swiss-Prot (Q6R6I7.1)"
Region 273..296
/region_name="leucine-rich repeat"
/note="leucine-rich repeat [structural motif]"
/db_xref="CDD:275380"
Region 296..317
/region_name="LRR 8"
/note="propagated from UniProtKB/Swiss-Prot (Q6R6I7.1)"
Region 297..320
/region_name="leucine-rich repeat"
/note="leucine-rich repeat [structural motif]"
/db_xref="CDD:275380"
Region 320..341
/region_name="LRR 9"
/note="propagated from UniProtKB/Swiss-Prot (Q6R6I7.1)"
Region 321..344
/region_name="leucine-rich repeat"
/note="leucine-rich repeat [structural motif]"
/db_xref="CDD:275380"
Site 325
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000255; propagated from
UniProtKB/Swiss-Prot (Q6R6I7.1)"
Region 344..365
/region_name="LRR 10"
/note="propagated from UniProtKB/Swiss-Prot (Q6R6I7.1)"
Region 345..366
/region_name="leucine-rich repeat"
/note="leucine-rich repeat [structural motif]"
/db_xref="CDD:275380"
Site 368
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000255; propagated from
UniProtKB/Swiss-Prot (Q6R6I7.1)"
Region 406..692
/region_name="7tmA_RXFP1_LGR7"
/note="relaxin receptor 1 (or LGR7), member of the class A
family of seven-transmembrane G protein-coupled receptors;
cd15965"
/db_xref="CDD:320631"
Region 407..433
/region_name="TM helix 1"
/note="TM helix 1 [structural motif]"
/db_xref="CDD:320631"
Site 410..430
/site_type="transmembrane region"
/note="propagated from UniProtKB/Swiss-Prot (Q6R6I7.1)"
Region 440..465
/region_name="TM helix 2"
/note="TM helix 2 [structural motif]"
/db_xref="CDD:320631"
Site 444..464
/site_type="transmembrane region"
/note="propagated from UniProtKB/Swiss-Prot (Q6R6I7.1)"
Site order(461,464..465,485..490,492..493,496,540,542..546,576,
579..581,583..585,587..588,641,644..645,647..648,651,
659..660,662..664,667,670..671)
/site_type="other"
/note="putative peptide ligand binding pocket [polypeptide
binding]"
/db_xref="CDD:320631"
Region 485..515
/region_name="TM helix 3"
/note="TM helix 3 [structural motif]"
/db_xref="CDD:320631"
Site 487..507
/site_type="transmembrane region"
/note="propagated from UniProtKB/Swiss-Prot (Q6R6I7.1)"
Region 526..548
/region_name="TM helix 4"
/note="TM helix 4 [structural motif]"
/db_xref="CDD:320631"
Site 528..548
/site_type="transmembrane region"
/note="propagated from UniProtKB/Swiss-Prot (Q6R6I7.1)"
Region 576..605
/region_name="TM helix 5"
/note="TM helix 5 [structural motif]"
/db_xref="CDD:320631"
Site 578..598
/site_type="transmembrane region"
/note="propagated from UniProtKB/Swiss-Prot (Q6R6I7.1)"
Region 621..651
/region_name="TM helix 6"
/note="TM helix 6 [structural motif]"
/db_xref="CDD:320631"
Site 630..650
/site_type="transmembrane region"
/note="propagated from UniProtKB/Swiss-Prot (Q6R6I7.1)"
Site 652..672
/site_type="transmembrane region"
/note="propagated from UniProtKB/Swiss-Prot (Q6R6I7.1)"
Region 660..685
/region_name="TM helix 7"
/note="TM helix 7 [structural motif]"
/db_xref="CDD:320631"
CDS 1..758
/gene="Rxfp1"
/gene_synonym="Gm1018; Lgr7"
/coded_by="NM_212452.3:87..2363"
/db_xref="CCDS:CCDS17420.1"
/db_xref="GeneID:381489"
/db_xref="MGI:MGI:2682211"
ORIGIN
1 mtsgpfffci fiigkyftlg saqdvscplg sfpcgnmsrc lpqllhcngv ddcgnraded
61 hcgdnngwsl qldkyfanyy klastnsfea etseclvgsv pmhclcrdle ldcdeanlra
121 vpsvssnvtv mslqrnfirt lppngfrkyh elqklclqnn rihsvsvsaf rglrsltkly
181 lshnritflk pgvfedlhrl ewliiednhl srispltfyg lnslillvlm nnaltrlpdk
241 plcqhmprlh wldfegnrih nlrnltfisc nnltvlvmrk nkinylneha fthlqkldel
301 dlgsnkienl ppnifkdlke lsqlnisynp iqkievnqfd claklkslsl egieisniqq
361 rmfrplinls hiyfkkfqyc gyaphvrsck pntdgissle nllasiiqrv fvwvvsaitc
421 fgnifvicmr pyirsenklh amsiislcca dclmgvylfv igafdlkfrg eynkhaqpwm
481 esvhcqfmgs lailstevsv llltfltlek yicivypfrc lrprkcrtit vlifiwiigf
541 ivafaplgnk effknyygtn gvcfplhsed tgstgaqiys vviflginlv afiiivfsyg
601 smfysvhqss vtvteiqkqv kkevvlakrf ffivftdalc wipifilkfl sllqveipds
661 itswvvifil pinsalnpii ytlttrpfke mihqlwhnyr qrrsvdrket qkayapsfiw
721 vemwplqems sgfmkpgaft dpcdlslvsq ssrlnsys
//
