Q9HBX9 (RXFP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	757 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing
Domain	Leucine-rich repeat Repeat Transmembrane Transmembrane helix
Ligand	Calcium Metal-binding
Molecular function	G-protein coupled receptor Receptor Transducer
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	adenylate cyclase-modulating G-protein coupled receptor signaling pathway Inferred from electronic annotation. Source: Compara cell differentiation Inferred from electronic annotation. Source: Compara extracellular matrix organization Inferred from electronic annotation. Source: Compara lung connective tissue development Inferred from electronic annotation. Source: Compara nipple morphogenesis Inferred from electronic annotation. Source: Compara parturition Inferred from electronic annotation. Source: Compara
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Traceable author statement. Source: Reactome
Molecular_function	G-protein coupled receptor activity Inferred from direct assay PubMed 11809971. Source: MGI hormone binding Inferred from electronic annotation. Source: Compara metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 757

757

Relaxin receptor 1

PRO_0000069700

Regions

Topological domain

1 – 409

409

Extracellular Potential

Transmembrane

410 – 430

21

Helical; Name=1; Potential

Topological domain

431 – 443

13

Cytoplasmic Potential

Transmembrane

444 – 464

21

Helical; Name=2; Potential

Topological domain

465 – 486

22

Extracellular Potential

Transmembrane

487 – 507

21

Helical; Name=3; Potential

Topological domain

508 – 527

20

Cytoplasmic Potential

Transmembrane

528 – 548

21

Helical; Name=4; Potential

Topological domain

549 – 577

29

Extracellular Potential

Transmembrane

578 – 598

21

Helical; Name=5; Potential

Topological domain

599 – 629

31

Cytoplasmic Potential

Transmembrane

630 – 650

21

Helical; Name=6; Potential

Topological domain

651

1

Extracellular Potential

Transmembrane

652 – 672

21

Helical; Name=7; Potential

Topological domain

673 – 757

85

Cytoplasmic Potential

Domain

26 – 63

38

LDL-receptor class A

Domain

91 – 127

37

LRRNT

Repeat

151 – 172

22

LRR 1

Repeat

175 – 196

22

LRR 2

Repeat

199 – 220

22

LRR 3

Repeat

223 – 244

22

LRR 4

Repeat

248 – 269

22

LRR 5

Repeat

272 – 293

22

LRR 6

Repeat

296 – 317

22

LRR 7

Repeat

320 – 341

22

LRR 8

Repeat

344 – 365

22

LRR 9

Sites

Metal binding

45

1

Calcium; via carbonyl oxygen

Metal binding

48

1

Calcium

Metal binding

50

1

Calcium; via carbonyl oxygen

Metal binding

52

1

Calcium

Metal binding

58

1

Calcium

Metal binding

59

1

Calcium

Amino acid modifications

Glycosylation

36

1

N-linked (GlcNAc...) Ref.8

Glycosylation

127

1

N-linked (GlcNAc...) Ref.8

Glycosylation

264

1

N-linked (GlcNAc...) Ref.8

Glycosylation

272

1

N-linked (GlcNAc...) Ref.8

Glycosylation

325

1

N-linked (GlcNAc...) Ref.8

Glycosylation

368

1

N-linked (GlcNAc...) Ref.8

Disulfide bond

27 ↔ 40

Disulfide bond

34 ↔ 53

Disulfide bond

47 ↔ 62

Disulfide bond

485 ↔ 563

Natural variations

Alternative sequence

63 – 96

34

GDNNG…TPECL → V in isoform 2.

VSP_001984

Alternative sequence

180 – 189

10

YLSHNRITFL → SRAVKDGSEK in isoform 3.

VSP_029877

Alternative sequence

190 – 757

568

Missing in isoform 3.

VSP_029878

Alternative sequence

300 – 348

49

LDLGS…KLKSL → F in isoform 4.

VSP_029879

Experimental info

Mutagenesis

637

1

D → Y: Leads to constitutive increase of basal cAMP. Ref.1

Sequence conflict

70

1

L → M in AAG17167. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

757

Helix Strand Turn

Details...

Beta strand

31 – 33

3

Beta strand

35 – 38

4

Beta strand

40 – 42

3

Helix

43 – 45

3

Beta strand

53 – 55

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 4, 2007. Version 2. Checksum: B32DD71B1A5D5864	FASTA	757	86,975
	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
	Isoform 2 (LGR7.10) [UniParc]. Checksum: 10976FE385EFEAF8	FASTA	724	83,060
	10 20 30 40 50 60 MTSGSVFFYI LIFGKYFSHG GGQDVKCSLG YFPCGNITKC LPQLLHCNGV DDCGNQADED 70 80 90 100 110 120 NCVVGSVPVQ CLCQGLELDC DETNLRAVPS VSSNVTAMSL QWNLIRKLPP DCFKNYHDLQ 130 140 150 160 170 180 KLYLQNNKIT SISIYAFRGL NSLTKLYLSH NRITFLKPGV FEDLHRLEWL IIEDNHLSRI 190 200 210 220 230 240 SPPTFYGLNS LILLVLMNNV LTRLPDKPLC QHMPRLHWLD LEGNHIHNLR NLTFISCSNL 250 260 270 280 290 300 TVLVMRKNKI NHLNENTFAP LQKLDELDLG SNKIENLPPL IFKDLKELSQ LNLSYNPIQK 310 320 330 340 350 360 IQANQFDYLV KLKSLSLEGI EISNIQQRMF RPLMNLSHIY FKKFQYCGYA PHVRSCKPNT 370 380 390 400 410 420 DGISSLENLL ASIIQRVFVW VVSAVTCFGN IFVICMRPYI RSENKLYAMS IISLCCADCL 430 440 450 460 470 480 MGIYLFVIGG FDLKFRGEYN KHAQLWMEST HCQLVGSLAI LSTEVSVLLL TFLTLEKYIC 490 500 510 520 530 540 IVYPFRCVRP GKCRTITVLI LIWITGFIVA FIPLSNKEFF KNYYGTNGVC FPLHSEDTES 550 560 570 580 590 600 IGAQIYSVAI FLGINLAAFI IIVFSYGSMF YSVHQSAITA TEIRNQVKKE MILAKRFFFI 610 620 630 640 650 660 VFTDALCWIP IFVVKFLSLL QVEIPGTITS WVVIFILPIN SALNPILYTL TTRPFKEMIH 670 680 690 700 710 720 RFWYNYRQRK SMDSKGQKTY APSFIWVEMW PLQEMPPELM KPDLFTYPCE MSLISQSTRL NSYS
	Isoform 3 (LGR7.1) [UniParc]. Checksum: B9B3EF4D3C62778F	FASTA	189	21,112
	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 RGLNSLTKLS RAVKDGSEK
	Isoform 4 (LGR7.2) [UniParc]. Checksum: 18F5684D7CF67595	FASTA	709	81,481
	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 FAPLQKLDEF 310 320 330 340 350 360 SLEGIEISNI QQRMFRPLMN LSHIYFKKFQ YCGYAPHVRS CKPNTDGISS LENLLASIIQ 370 380 390 400 410 420 RVFVWVVSAV TCFGNIFVIC MRPYIRSENK LYAMSIISLC CADCLMGIYL FVIGGFDLKF 430 440 450 460 470 480 RGEYNKHAQL WMESTHCQLV GSLAILSTEV SVLLLTFLTL EKYICIVYPF RCVRPGKCRT 490 500 510 520 530 540 ITVLILIWIT GFIVAFIPLS NKEFFKNYYG TNGVCFPLHS EDTESIGAQI YSVAIFLGIN 550 560 570 580 590 600 LAAFIIIVFS YGSMFYSVHQ SAITATEIRN QVKKEMILAK RFFFIVFTDA LCWIPIFVVK 610 620 630 640 650 660 FLSLLQVEIP GTITSWVVIF ILPINSALNP ILYTLTTRPF KEMIHRFWYN YRQRKSMDSK 670 680 690 700 GQKTYAPSFI WVEMWPLQEM PPELMKPDLF TYPCEMSLIS QSTRLNSYS

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.

IPI

IPI00012456.
IPI00219888.
IPI00654878.
IPI00876893.

RefSeq

NP_001240657.1. NM_001253728.1.
NP_001240658.1. NM_001253729.1.
NP_067647.2. NM_021634.3.

UniGene

Hs.591686.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2JM4	NMR	-	A	23-63	[»]

ProteinModelPortal

Q9HBX9.

ModBase

Search...

Protein-protein interaction databases

MINT

MINT-231156.

STRING

9606.ENSP00000303248.

Protein family/group databases

GPCRDB

Search...

PTM databases

PhosphoSite

Q9HBX9.

Polymorphism databases

DMDM

166209887.

Proteomic databases

PaxDb

Q9HBX9.

PRIDE

Q9HBX9.

Protocols and materials databases

DNASU

59350.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000307765; ENSP00000303248; ENSG00000171509.
ENST00000343542; ENSP00000345889; ENSG00000171509.
ENST00000423548; ENSP00000405841; ENSG00000171509.
ENST00000470033; ENSP00000420712; ENSG00000171509.
ENST00000471616; ENSP00000434475; ENSG00000171509.

GeneID

59350.

KEGG

hsa:59350.

UCSC

uc003ipz.3. human.
uc010iqm.3. human.
uc010iqo.3. human.

Organism-specific databases

CTD

59350.

GeneCards

GC04P159236.

H-InvDB

HIX0024561.

HGNC

HGNC:19718. RXFP1.

HPA

HPA027067.

MIM

606654. gene.

neXtProt

NX_Q9HBX9.

PharmGKB

PA134868312.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG4886.

HOVERGEN

HBG026354.

InParanoid

Q9HBX9.

KO

K04306.

OMA

YTLTTRP.

PhylomeDB

Q9HBX9.

Enzyme and pathway databases

Reactome

REACT_111102. Signal Transduction.

Gene expression databases

ArrayExpress

Q9HBX9.

Bgee

Q9HBX9.

CleanEx

HS_RXFP1.

Genevestigator

Q9HBX9.

GermOnline

ENSG00000171509. Homo sapiens.

Family and domain databases

Gene3D

4.10.400.10. 1 hit.

InterPro

IPR000276. 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]

Pfam

PF00001. 7tm_1. 1 hit.
PF00057. Ldl_recept_a. 1 hit.
[Graphical view]

PRINTS

PR00237. GPCRRHODOPSN.
PR01739. RELAXINR.

SMART

SM00192. LDLa. 1 hit.
SM00369. LRR_TYP. 2 hits.
SM00013. LRRNT. 1 hit.
[Graphical view]

SUPFAM

SSF57424. LDL_rcpt_classA_cys-rich. 1 hit.

PROSITE

PS00237. G_PROTEIN_RECEP_F1_1. False negative.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
PS01209. LDLRA_1. 1 hit.
PS50068. LDLRA_2. 1 hit.
PS51450. LRR. 10 hits.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL1293316.

EvolutionaryTrace

Q9HBX9.

GenomeRNAi

59350.

NextBio

65261.

SOURCE

Search...

Entry information

Entry name

RXFP1_HUMAN

Accession

Primary (citable) accession number: Q9HBX9
Secondary accession number(s): B4DTV2 , Q2M215, Q3KU24, Q3KU25, Q3KU26

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 6, 2002
Last sequence update:	December 4, 2007
Last modified:	May 1, 2013
This is version 113 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.