Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9HBX9 (RXFP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Relaxin receptor 1
Alternative name(s):
Leucine-rich repeat-containing G-protein coupled receptor 7
Relaxin family peptide receptor 1
Gene names
Name:RXFP1
Synonyms:LGR7
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length757 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Receptor for relaxins. The activity of this receptor is mediated by G proteins leading to stimulation of adenylate cyclase and an increase of cAMP. Binding of the ligand may also activate a tyrosine kinase pathway that inhibits the activity of a phosphodiesterase that degrades cAMP.

Subcellular location

Cell membrane; Multi-pass membrane protein Ref.2.

Tissue specificity

Expressed in the brain, kidney, testis, placenta, uterus, ovary, adrenal, prostate, skin and heart. Not detected in spleen. Ref.2

Sequence similarities

Belongs to the G-protein coupled receptor 1 family.

Contains 1 LDL-receptor class A domain.

Contains 9 LRR (leucine-rich) repeats.

Contains 1 LRRNT domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

AKAP5P245882EBI-8088969,EBI-703640

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9HBX9-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9HBX9-2)

Also known as: LGR7.10;

The sequence of this isoform differs from the canonical sequence as follows:
     63-96: GDNNGWSLQFDKYFASYYKMTSQYPFEAETPECL → V
Isoform 3 (identifier: Q9HBX9-3)

Also known as: LGR7.1;

The sequence of this isoform differs from the canonical sequence as follows:
     180-189: YLSHNRITFL → SRAVKDGSEK
     190-757: Missing.
Isoform 4 (identifier: Q9HBX9-4)

Also known as: LGR7.2;

The sequence of this isoform differs from the canonical sequence as follows:
     300-348: LDLGSNKIENLPPLIFKDLKELSQLNLSYNPIQKIQANQFDYLVKLKSL → F

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 757757Relaxin receptor 1
PRO_0000069700

Regions

Topological domain1 – 409409Extracellular Potential
Transmembrane410 – 43021Helical; Name=1; Potential
Topological domain431 – 44313Cytoplasmic Potential
Transmembrane444 – 46421Helical; Name=2; Potential
Topological domain465 – 48622Extracellular Potential
Transmembrane487 – 50721Helical; Name=3; Potential
Topological domain508 – 52720Cytoplasmic Potential
Transmembrane528 – 54821Helical; Name=4; Potential
Topological domain549 – 57729Extracellular Potential
Transmembrane578 – 59821Helical; Name=5; Potential
Topological domain599 – 62931Cytoplasmic Potential
Transmembrane630 – 65021Helical; Name=6; Potential
Topological domain6511Extracellular Potential
Transmembrane652 – 67221Helical; Name=7; Potential
Topological domain673 – 75785Cytoplasmic Potential
Domain26 – 6338LDL-receptor class A
Domain91 – 12737LRRNT
Repeat151 – 17222LRR 1
Repeat175 – 19622LRR 2
Repeat199 – 22022LRR 3
Repeat223 – 24422LRR 4
Repeat248 – 26922LRR 5
Repeat272 – 29322LRR 6
Repeat296 – 31722LRR 7
Repeat320 – 34122LRR 8
Repeat344 – 36522LRR 9

Sites

Metal binding451Calcium; via carbonyl oxygen
Metal binding481Calcium
Metal binding501Calcium; via carbonyl oxygen
Metal binding521Calcium
Metal binding581Calcium
Metal binding591Calcium

Amino acid modifications

Glycosylation361N-linked (GlcNAc...) Ref.8
Glycosylation1271N-linked (GlcNAc...) Ref.8
Glycosylation2641N-linked (GlcNAc...) Ref.8
Glycosylation2721N-linked (GlcNAc...) Ref.8
Glycosylation3251N-linked (GlcNAc...) Ref.8
Glycosylation3681N-linked (GlcNAc...) Ref.8
Disulfide bond27 ↔ 40
Disulfide bond34 ↔ 53
Disulfide bond47 ↔ 62
Disulfide bond485 ↔ 563

Natural variations

Alternative sequence63 – 9634GDNNG…TPECL → V in isoform 2.
VSP_001984
Alternative sequence180 – 18910YLSHNRITFL → SRAVKDGSEK in isoform 3.
VSP_029877
Alternative sequence190 – 757568Missing in isoform 3.
VSP_029878
Alternative sequence300 – 34849LDLGS…KLKSL → F in isoform 4.
VSP_029879

Experimental info

Mutagenesis6371D → Y: Leads to constitutive increase of basal cAMP. Ref.1
Sequence conflict701L → M in AAG17167. Ref.1

Secondary structure

.......... 757
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 4, 2007. Version 2.
Checksum: B32DD71B1A5D5864

FASTA75786,975
        10         20         30         40         50         60 
MTSGSVFFYI LIFGKYFSHG GGQDVKCSLG YFPCGNITKC LPQLLHCNGV DDCGNQADED 

        70         80         90        100        110        120 
NCGDNNGWSL QFDKYFASYY KMTSQYPFEA ETPECLVGSV PVQCLCQGLE LDCDETNLRA 

       130        140        150        160        170        180 
VPSVSSNVTA MSLQWNLIRK LPPDCFKNYH DLQKLYLQNN KITSISIYAF RGLNSLTKLY 

       190        200        210        220        230        240 
LSHNRITFLK PGVFEDLHRL EWLIIEDNHL SRISPPTFYG LNSLILLVLM NNVLTRLPDK 

       250        260        270        280        290        300 
PLCQHMPRLH WLDLEGNHIH NLRNLTFISC SNLTVLVMRK NKINHLNENT FAPLQKLDEL 

       310        320        330        340        350        360 
DLGSNKIENL PPLIFKDLKE LSQLNLSYNP IQKIQANQFD YLVKLKSLSL EGIEISNIQQ 

       370        380        390        400        410        420 
RMFRPLMNLS HIYFKKFQYC GYAPHVRSCK PNTDGISSLE NLLASIIQRV FVWVVSAVTC 

       430        440        450        460        470        480 
FGNIFVICMR PYIRSENKLY AMSIISLCCA DCLMGIYLFV IGGFDLKFRG EYNKHAQLWM 

       490        500        510        520        530        540 
ESTHCQLVGS LAILSTEVSV LLLTFLTLEK YICIVYPFRC VRPGKCRTIT VLILIWITGF 

       550        560        570        580        590        600 
IVAFIPLSNK EFFKNYYGTN GVCFPLHSED TESIGAQIYS VAIFLGINLA AFIIIVFSYG 

       610        620        630        640        650        660 
SMFYSVHQSA ITATEIRNQV KKEMILAKRF FFIVFTDALC WIPIFVVKFL SLLQVEIPGT 

       670        680        690        700        710        720 
ITSWVVIFIL PINSALNPIL YTLTTRPFKE MIHRFWYNYR QRKSMDSKGQ KTYAPSFIWV 

       730        740        750 
EMWPLQEMPP ELMKPDLFTY PCEMSLISQS TRLNSYS 

« Hide

Isoform 2 (LGR7.10) [UniParc].

Checksum: 10976FE385EFEAF8
Show »

FASTA72483,060
Isoform 3 (LGR7.1) [UniParc].

Checksum: B9B3EF4D3C62778F
Show »

FASTA18921,112
Isoform 4 (LGR7.2) [UniParc].

Checksum: 18F5684D7CF67595
Show »

FASTA70981,481

References

« Hide 'large scale' references
[1]"The three subfamilies of leucine-rich repeat-containing G protein-coupled receptors (LGR): identification of LGR6 and LGR7 and the signaling mechanism for LGR7."
Hsu S.Y., Kudo M., Chen T., Nakabayashi K., Bhalla A., van der Spek P.J., van Duin M., Hsueh A.J.W.
Mol. Endocrinol. 14:1257-1271(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), MUTAGENESIS OF ASP-637.
[2]"Splice variants of the relaxin and INSL3 receptors reveal unanticipated molecular complexity."
Muda M., He C., Martini P.G.V., Ferraro T., Layfield S., Taylor D., Chevrier C., Schweickhardt R., Kelton C., Ryan P.L., Bathgate R.A.D.
Mol. Hum. Reprod. 11:591-600(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Placenta.
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain cortex.
[6]"Relaxin signalling links tyrosine phosphorylation to phosphodiesterase and adenylyl cyclase activity."
Bartsch O., Bartlick B., Ivell R.
Mol. Hum. Reprod. 7:799-809(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[7]"H3 relaxin is a specific ligand for LGR7 and activates the receptor by interacting with both the ectodomain and the exoloop 2."
Sudo S., Kumagai J., Nishi S., Layfield S., Ferraro T., Bathgate R.A.D., Hsueh A.J.W.
J. Biol. Chem. 278:7855-7862(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RLN3.
[8]"Identification of the N-linked glycosylation sites of the human relaxin receptor and effect of glycosylation on receptor function."
Yan Y., Scott D.J., Wilkinson T.N., Ji J., Tregear G.W., Bathgate R.A.
Biochemistry 47:6953-6968(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-36; ASN-127; ASN-264; ASN-272; ASN-325 AND ASN-368.
[9]"The NMR solution structure of the relaxin (RXFP1) receptor lipoprotein receptor class A module and identification of key residues in the N-terminal region of the module that mediate receptor activation."
Hopkins E.J., Layfield S., Ferraro T., Bathgate R.A.D., Gooley P.R.
J. Biol. Chem. 282:4172-4184(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 23-63 IN COMPLEX WITH CALCIUM IONS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF190500 mRNA. Translation: AAG17167.1.
AY899848 mRNA. Translation: AAX85196.1.
AY899849 mRNA. Translation: AAX85197.1.
AY899850 mRNA. Translation: AAX85198.1.
AK300379 mRNA. Translation: BAG62114.1.
CH471056 Genomic DNA. Translation: EAX04856.1.
BC112142 mRNA. Translation: AAI12143.1.
BC113617 mRNA. Translation: AAI13618.1.
RefSeqNP_001240657.1. NM_001253728.1.
NP_001240658.1. NM_001253729.1.
NP_067647.2. NM_021634.3.
UniGeneHs.591686.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2JM4NMR-A23-63[»]
2M7PNMR-A28-39[»]
ProteinModelPortalQ9HBX9.
SMRQ9HBX9. Positions 21-63, 101-681.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121891. 1 interaction.
IntActQ9HBX9. 5 interactions.
MINTMINT-231156.
STRING9606.ENSP00000303248.

Chemistry

ChEMBLCHEMBL1293316.
GuidetoPHARMACOLOGY351.

Protein family/group databases

GPCRDBSearch...

PTM databases

PhosphoSiteQ9HBX9.

Polymorphism databases

DMDM166209887.

Proteomic databases

PaxDbQ9HBX9.
PRIDEQ9HBX9.

Protocols and materials databases

DNASU59350.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000307765; ENSP00000303248; ENSG00000171509. [Q9HBX9-1]
ENST00000343542; ENSP00000345889; ENSG00000171509. [Q9HBX9-4]
ENST00000423548; ENSP00000405841; ENSG00000171509. [Q9HBX9-3]
ENST00000470033; ENSP00000420712; ENSG00000171509. [Q9HBX9-2]
ENST00000471616; ENSP00000434475; ENSG00000171509. [Q9HBX9-3]
GeneID59350.
KEGGhsa:59350.
UCSCuc003ipz.3. human. [Q9HBX9-1]
uc010iqm.3. human. [Q9HBX9-2]
uc010iqo.3. human. [Q9HBX9-4]

Organism-specific databases

CTD59350.
GeneCardsGC04P159236.
H-InvDBHIX0024561.
HGNCHGNC:19718. RXFP1.
HPAHPA027067.
MIM606654. gene.
neXtProtNX_Q9HBX9.
PharmGKBPA134868312.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG4886.
HOVERGENHBG026354.
InParanoidQ9HBX9.
KOK04306.
OMATRPFKEM.
PhylomeDBQ9HBX9.
TreeFamTF326185.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.

Gene expression databases

ArrayExpressQ9HBX9.
BgeeQ9HBX9.
CleanExHS_RXFP1.
GenevestigatorQ9HBX9.

Family and domain databases

Gene3D1.20.1070.10. 1 hit.
4.10.400.10. 1 hit.
InterProIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR023415. LDLR_class-A_CS.
IPR002172. LDrepeatLR_classA_rpt.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000372. LRR-contain_N.
IPR008112. Relaxin_rcpt.
[Graphical view]
PfamPF00001. 7tm_1. 1 hit.
PF00057. Ldl_recept_a. 1 hit.
[Graphical view]
PRINTSPR00237. GPCRRHODOPSN.
PR01739. RELAXINR.
SMARTSM00192. LDLa. 1 hit.
SM00369. LRR_TYP. 2 hits.
SM00013. LRRNT. 1 hit.
[Graphical view]
SUPFAMSSF57424. SSF57424. 1 hit.
PROSITEPS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
PS01209. LDLRA_1. 1 hit.
PS50068. LDLRA_2. 1 hit.
PS51450. LRR. 10 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9HBX9.
GeneWikiRelaxin/insulin-like_family_peptide_receptor_1.
GenomeRNAi59350.
NextBio65261.
PROQ9HBX9.
SOURCESearch...

Entry information

Entry nameRXFP1_HUMAN
AccessionPrimary (citable) accession number: Q9HBX9
Secondary accession number(s): B4DTV2 expand/collapse secondary AC list , Q2M215, Q3KU24, Q3KU25, Q3KU26
Entry history
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: December 4, 2007
Last modified: April 16, 2014
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries