MQMADAATIATMNKAAGGDKLAELFSLVPDLLEAANTSGNASLQLPDLWWELGLELPDGA PPGHPPGSGGAESADTEARVRILISVVYWVVCALGLAGNLLVLYLMKSMQGWRKSSINLF VTNLALTDFQFVLTLPFWAVENALDFKWPFGKAMCKIVSMVTSMNMYASVFFLTAMSVTR YHSVASALKSHRTRGHGRGDCCGRSLGDSCCFSAKALCVWIWALAALASLPSAIFSTTVK VMGEELCLVRFPDKLLGRDRQFWLGLYHSQKVLLGFVLPLGIIILCYLLLVRFIADRRAA GTKGGAAVAGGRPTGASARRLSKVTKSVTIVVLSFFLCWLPNQALTTWSILIKFNAVPFS QEYFLCQVYAFPVSVCLAHSNSCLNPVLYCLVRREFRKALKSLLWRIASPSITSMRPFTA TTKPEHEDQGLQAPAPPHAAAEPDLLYYPPGVVVYSGGRYDLLPSSSAY
Note: The complete
sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is
translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application,
please explicitly request the full and complete sequence of this protein before ordering.
Protein Length
full length protein
Tag Info
N-terminal 10xHis-tagged
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Receptor for RNL3/relaxin-3. Binding of the ligand inhibit cAMP accumulation.
Gene References into Functions
This study indicated that RXFP3 mainly localised in the post-acrosomal region of sperm head and neck.PMID:29159832
The role of these four INSL5 determinants in distinguishing RXFP4 from RXFP3.PMID:27404393
Therefore, we conclude that stapling of the relaxin3 B chain does not compromise its ability to activate RXFP3 and is a promising method for developing stable peptide agonists and antagonists of RXFP3 to aid relaxin-3/RXFP3 research.PMID:27498038
the negatively charged transmembrane aspartate residue controls activation of the relaxin-3 receptor RXFP3PMID:27353281
we demonstrated distinct patterns of signalling for H3 and H2 relaxin and R3(BDelta23-27)R/I5 at the RXFP3 receptorPMID:24641548
Glu141 and Asp145 of the RXFP3 interact with the highly conserved arginine residues of relaxin-3.PMID:24615237
demonstrate the existence of an allosteric site for modulation of RXFP3PMID:22347403
H3 relaxin potently activates all signaling pathways coupled to RXFP3, whereas H2 relaxin is an AP-1-biased ligand relative to H3 relaxin.PMID:20159943
GPCR135 (SALPR) is the receptor for relaxin-3PMID:14522968
Substitution of the relaxin-3 A-chain with the A-chain from insulin-like peptide 5 results in a chimeric peptide that selectively activates GPCR135 and GPCR142.PMID:15465925
functional response to H3 relaxin and other relaxin/insulin peptides of GPCR135 expressed in CHO-K1 cells was measured in the cytosensor microphysiometer and analyzed using inhibitors of signal transduction proteinsPMID:15956730
analysis of truncated human relaxin-2 and -3 (H2 and H3) relaxin peptides and their binding and cAMP activities on RXFP1, RXFP2, and RXFP3PMID:18434306
the N-terminus and EL2 domains of RXFP3 and RXFP4 are involved in ligand binding while TM2, 3, and 5 are critical for receptor activation.PMID:18582868
Results decribe the structural and functional aspects of the interaction between relaxin-3 and its receptor, RXFP3.PMID:19152634
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Subcellular Location
Cell membrane; Multi-pass membrane protein.
Protein Families
G-protein coupled receptor 1 family
Tissue Specificity
Expressed predominantly in brain regions. Highest expression in substantia nigra and pituitary, followed by hippocampus, spinal cord, amygdala, caudate nucleus and corpus callosum, quite low level in cerebellum. In peripheral tissues, relatively high leve