MyHits has reached its end of life and no longer provides data or services. Thank you for your support and trust for more than 23 years!
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
- MyHits
| Description | RecName: Full=Relaxin-3 receptor 2; Short=RLN3 receptor 2; AltName: Full=G-protein coupled receptor 100; AltName: Full=Insulin-like peptide INSL5 receptor; AltName: Full=Relaxin family peptide receptor 4; |
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| MyHits synonyms | RL3R2_MOUSE , Q7TQP4 , Q80UD6 , EBB47A1C62E6DB0B |
 Legends: 1, N-linked (GlcNAc...) asparagine. {ECO:0000255}; 2, CONFLICT M -> L (in Ref. 2; AAO85051). {ECO:0000305}; 3, TOPO_DOM Extracellular. {ECO:0000255}; 4, TRANSMEM Helical; Name=1. {ECO:0000255}; 5, TOPO_DOM Cytoplasmic. {ECO:0000255}; 6, TRANSMEM Helical; Name=2. {ECO:0000255}; 7, TRANSMEM Helical; Name=3. {ECO:0000255}; 8, TRANSMEM Helical; Name=4. {ECO:0000255}; 9, TRANSMEM Helical; Name=5. {ECO:0000255}; 10, TRANSMEM Helical; Name=6. {ECO:0000255}; 11, TRANSMEM Helical; Name=7. {ECO:0000255}; 12, COMPBIAS Poly-Leu.
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ID RL3R2_MOUSE Reviewed; 414 AA.
AC Q7TQP4; Q80UD6;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 10-MAY-2017, entry version 115.
DE RecName: Full=Relaxin-3 receptor 2;
DE Short=RLN3 receptor 2;
DE AltName: Full=G-protein coupled receptor 100;
DE AltName: Full=Insulin-like peptide INSL5 receptor;
DE AltName: Full=Relaxin family peptide receptor 4;
GN Name=Rxfp4; Synonyms=Gpr100, Rln3r2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC Muroidea; Muridae; Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=14623098; DOI=10.1016/S0014-5793(03)01196-7;
RA Fredriksson R., Hoeglund P.J., Gloriam D.E.I., Lagerstroem M.C.,
RA Schioeth H.B.;
RT "Seven evolutionarily conserved human rhodopsin G protein-coupled
RT receptors lacking close relatives.";
RL FEBS Lett. 554:381-388(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 41-159.
RX PubMed=12679517; DOI=10.1073/pnas.0230374100;
RA Vassilatis D.K., Hohmann J.G., Zeng H., Li F., Ranchalis J.E.,
RA Mortrud M.T., Brown A., Rodriguez S.S., Weller J.R., Wright A.C.,
RA Bergmann J.E., Gaitanaris G.A.;
RT "The G protein-coupled receptor repertoires of human and mouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:4903-4908(2003).
CC -!- FUNCTION: High affinity receptor for INSL5. Also acts as receptor
CC for RLN3/relaxin-3, as well as bradykinin and kallidin. Binding of
CC the ligand inhibit cAMP accumulation (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Detected only in bone marrow.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AY288422; AAP72131.1; -; mRNA.
DR EMBL; AY255539; AAO85051.1; -; mRNA.
DR CCDS; CCDS17482.1; -.
DR RefSeq; NP_861538.1; NM_181817.1.
DR UniGene; Mm.269130; -.
DR ProteinModelPortal; Q7TQP4; -.
DR STRING; 10090.ENSMUSP00000058732; -.
DR GuidetoPHARMACOLOGY; 354; -.
DR PhosphoSitePlus; Q7TQP4; -.
DR PaxDb; Q7TQP4; -.
DR PRIDE; Q7TQP4; -.
DR Ensembl; ENSMUST00000063119; ENSMUSP00000058732; ENSMUSG00000049741.
DR GeneID; 242093; -.
DR KEGG; mmu:242093; -.
DR UCSC; uc008pwc.1; mouse.
DR CTD; 339403; -.
DR MGI; MGI:2182926; Rxfp4.
DR eggNOG; KOG3656; Eukaryota.
DR eggNOG; ENOG410XRW9; LUCA.
DR GeneTree; ENSGT00760000119055; -.
DR HOGENOM; HOG000230485; -.
DR HOVERGEN; HBG101327; -.
DR InParanoid; Q7TQP4; -.
DR KO; K08398; -.
DR OMA; LWVLGNC; -.
DR OrthoDB; EOG091G0CM0; -.
DR PhylomeDB; Q7TQP4; -.
DR TreeFam; TF330024; -.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR Reactome; R-MMU-444821; Relaxin receptors.
DR PRO; PR:Q7TQP4; -.
DR Proteomes; UP000000589; Chromosome 3.
DR CleanEx; MM_RXFP4; -.
DR ExpressionAtlas; Q7TQP4; baseline and differential.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0004966; F:galanin receptor activity; IBA:GO_Central.
DR GO; GO:0007188; P:adenylate cyclase-modulating G-protein coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007200; P:phospholipase C-activating G-protein coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:2000253; P:positive regulation of feeding behavior; IMP:MGI.
DR InterPro; IPR000248; ATII_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00241; ANGIOTENSINR.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Complete proteome; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1 414 Relaxin-3 receptor 2.
FT /FTId=PRO_0000070107.
FT TOPO_DOM 1 43 Extracellular. {ECO:0000255}.
FT TRANSMEM 44 64 Helical; Name=1. {ECO:0000255}.
FT TOPO_DOM 65 77 Cytoplasmic. {ECO:0000255}.
FT TRANSMEM 78 98 Helical; Name=2. {ECO:0000255}.
FT TOPO_DOM 99 116 Extracellular. {ECO:0000255}.
FT TRANSMEM 117 137 Helical; Name=3. {ECO:0000255}.
FT TOPO_DOM 138 155 Cytoplasmic. {ECO:0000255}.
FT TRANSMEM 156 176 Helical; Name=4. {ECO:0000255}.
FT TOPO_DOM 177 209 Extracellular. {ECO:0000255}.
FT TRANSMEM 210 230 Helical; Name=5. {ECO:0000255}.
FT TOPO_DOM 231 255 Cytoplasmic. {ECO:0000255}.
FT TRANSMEM 256 276 Helical; Name=6. {ECO:0000255}.
FT TOPO_DOM 277 293 Extracellular. {ECO:0000255}.
FT TRANSMEM 294 316 Helical; Name=7. {ECO:0000255}.
FT TOPO_DOM 317 414 Cytoplasmic. {ECO:0000255}.
FT COMPBIAS 225 228 Poly-Leu.
FT CARBOHYD 5 5 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 17 17 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT DISULFID 114 191 {ECO:0000255|PROSITE-ProRule:PRU00521}.
FT CONFLICT 41 41 M -> L (in Ref. 2; AAO85051).
FT {ECO:0000305}.
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CC The following FT lines are automated annotations from the MyHits database.
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FT MYHIT 56 313 iprf:G_PROTEIN_RECEP_F1_2 [T]
FT MYHIT 56 313 ipfam:7tm_1 [T]
SQ SEQUENCE 414 AA; 45460 MW; EBB47A1C62E6DB0B CRC64;
MATSNSSASL PTLFWVNGSG DSVLSTDGAA MPVQFLVLRI MVALAYGLVG IIGLLGNLAV
LWVLGNCGQR VPGLSSDTFV FSLALADLGL ALTLPFWATE SAMDFHWPFG SALCKVVLTT
TVLSIYASTF LITALSIARY WVVAMAVGPG SHLSVFWARV VTLAVWVAAA LVTVPTAIFG
AEVELWGVCL CLLRFPSRYW LGAYQLQRVV LAFIVPLGVI TTSYLLLLAF LERQQRCRPR
QWQDSRVVAR SVRVLVASFA LCWVPNHVVT LWEILVRFDL VPWDSTFYTF HTYILPITTC
LAHSNSCLNP VIYCLLRREP QQVLVSSFRA LWSRLWPQRK ACMEQMALKE VGGRTVASTQ
ESGSSRTHTN TMEHLDEGCS LNTLLSETYQ GQSPQILGRS SCSLSQAAVS PGEV
//
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