Q8BGE9 (RL3R1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Relaxin-3 receptor 1
Short name=RLN3 receptor 1

Alternative name(s):
G protein-coupled receptor SALPR homolog
Relaxin family peptide receptor 3

Gene names

Name:	Rxfp3
Synonyms:	Rln3r1, Salpr

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	472 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Receptor for RNL3/relaxin-3. Binding of the ligand inhibit cAMP accumulation By similarity.
Subcellular location	Cell membrane; Multi-pass membrane protein.
Sequence similarities	Belongs to the G-protein coupled receptor 1 family.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Molecular function	G-protein coupled receptor Receptor Transducer
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	elevation of cytosolic calcium ion concentration involved in G-protein signaling coupled to IP3 second messenger Inferred from direct assay. Source: MGI
Cellular component	integral to membrane Inferred by curator. Source: MGI plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	N-formyl peptide receptor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 472	472	Relaxin-3 receptor 1		PRO_0000070105
Regions
	Topological domain	1 – 81	81	Extracellular Potential
	Transmembrane	82 – 102	21	Helical; Name=1; Potential
	Topological domain	103 – 119	17	Cytoplasmic Potential
	Transmembrane	120 – 140	21	Helical; Name=2; Potential
	Topological domain	141 – 156	16	Extracellular Potential
	Transmembrane	157 – 177	21	Helical; Name=3; Potential
	Topological domain	178 – 215	38	Cytoplasmic Potential
	Transmembrane	216 – 236	21	Helical; Name=4; Potential
	Topological domain	237 – 270	34	Extracellular Potential
	Transmembrane	271 – 291	21	Helical; Name=5; Potential
	Topological domain	292 – 298	7	Cytoplasmic Potential
	Transmembrane	299 – 319	21	Helical; Name=6; Potential
	Topological domain	320 – 332	13	Extracellular Potential
	Transmembrane	333 – 353	21	Helical; Name=7; Potential
	Topological domain	354 – 472	119	Cytoplasmic Potential
	Compositional bias	67 – 70	4	Poly-Gly
	Compositional bias	308 – 311	4	Poly-Ala
Amino acid modifications
	Glycosylation	36	1	N-linked (GlcNAc...) Potential
	Glycosylation	40	1	N-linked (GlcNAc...) Potential
	Disulfide bond	155 ↔ 247		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8BGE9 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: A0688FCBE06022B1	FASTA	472	51,573
	10 20 30 40 50 60 MQVASATPAA TVRKAAAGDE LSEFFALTPD LLEVANASGN ASLQLQDLWW ELGLELPDGA 70 80 90 100 110 120 APGHPPGGGG AESTDTEARV RILISAVYWV VCALGLAGNL LVLYLMKSKQ GWRKSSINLF 130 140 150 160 170 180 VTNLALTDFQ FVLTLPFWAV ENALDFKWPF GKAMCKIVSM VTSMNMYASV FFLTAMSVAR 190 200 210 220 230 240 YHSVASALKS HRTRGRGRGD CCGQSLRESC CFSAKVLCGL IWASAALASL PNAIFSTTIR 250 260 270 280 290 300 VLGEELCLMH FPDKLLGWDR QFWLGLYHLQ KVLLGFLLPL SIISLCYLLL VRFISDRRVV 310 320 330 340 350 360 GTTDAVGAAA APGGGLSTAS ARRRSKVTKS VTIVVLSFFL CWLPNQALTT WSILIKFNAV 370 380 390 400 410 420 PFSQEYFQCQ VYAFPVSVCL AHSNSCLNPI LYCLVRREFR KALKNLLWRI ASPSLTNMRP 430 440 450 460 470 FTATTKPEPE DHGLQALAPL NAAAEPDLIY YPPGVVVYSG GRYDLLPSSS AY

References

[1]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Brain, Cerebellum and Spinal ganglion.
[2]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6. Tissue: Brain.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK043414 mRNA. Translation: BAC31542.1. AK046367 mRNA. Translation: BAC32691.1. AK084001 mRNA. Translation: BAC39091.1. BC053073 mRNA. Translation: AAH53073.1.
IPI	IPI00221590.
RefSeq	NP_848832.1. NM_178717.3.
UniGene	Mm.209312.
3D structure databases
ProteinModelPortal	Q8BGE9.
SMR	Q8BGE9. Positions 167-198, 374-408.
ModBase	Search...
Protein-protein interaction databases
STRING	Q8BGE9.
Protein family/group databases
GPCRDB	Search...
Proteomic databases
PRIDE	Q8BGE9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000058007; ENSMUSP00000062741; ENSMUSG00000060735.
GeneID	239336.
KEGG	mmu:239336.
Organism-specific databases
CTD	51289.
MGI	MGI:2441827. Rxfp3.
Phylogenomic databases
GeneTree	ENSGT00560000076900.
HOGENOM	HBG445265.
HOVERGEN	HBG101327.
InParanoid	Q8BGE9.
OMA	QGWRKSS.
OrthoDB	EOG4X3H22.
PhylomeDB	Q8BGE9.
Gene expression databases
ArrayExpress	Q8BGE9.
Bgee	Q8BGE9.
CleanEx	MM_RXFP3.
Genevestigator	Q8BGE9.
GermOnline	ENSMUSG00000060735. Mus musculus.
Family and domain databases
InterPro	IPR000276. 7TM_GPCR_Rhodpsn. IPR000826. Frt_met_rcpt. IPR017452. GPCR_Rhodpsn_supfam. [Graphical view]
KO	K08397.
Pfam	PF00001. 7tm_1. 1 hit. [Graphical view]
PRINTS	PR00526. FMETLEUPHER. PR00237. GPCRRHODOPSN.
PROSITE	PS00237. G_PROTEIN_RECEP_F1_1. False negative. PS50262. G_PROTEIN_RECEP_F1_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	384070.
SOURCE	Search...

Entry information

Entry name

RL3R1_MOUSE

Accession

Primary (citable) accession number: Q8BGE9

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 7, 2003
Last sequence update:	March 1, 2003
Last modified:	November 16, 2011
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program