Entry sw:RL3R2_HUMAN

ID   RL3R2_HUMAN             Reviewed;         374 AA.
AC   Q8TDU9; B0M0L4; Q3MJB1; Q8NGZ8;
DT   07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   18-JAN-2017, entry version 132.
DE   RecName: Full=Relaxin-3 receptor 2;
DE            Short=RLN3 receptor 2;
DE   AltName: Full=G-protein coupled receptor 100;
DE   AltName: Full=G-protein coupled receptor GPCR142;
DE   AltName: Full=Insulin-like peptide INSL5 receptor;
DE   AltName: Full=Relaxin family peptide receptor 4;
GN   Name=RXFP4; Synonyms=GPR100, RLN3R2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-329, AND FUNCTION AS A
RP   RECEPTOR FOR RLN3.
RX   PubMed=14522967; DOI=10.1074/jbc.M308996200;
RA   Liu C., Chen J., Sutton S., Roland B., Kuei C., Farmer N., Sillard R.,
RA   Lovenberg T.W.;
RT   "Identification of relaxin-3/INSL7 as a ligand for GPCR142.";
RL   J. Biol. Chem. 278:50765-50770(2003).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INTERACTION WITH
RP   BRADYKININ AND KALLIDIN.
RC   TISSUE=Pancreatic carcinoma;
RX   PubMed=14530218; DOI=10.1038/sj.bjp.0705521;
RA   Boels K., Schaller H.C.;
RT   "Identification and characterisation of GPR100 as a novel human G-
RT   protein-coupled bradykinin receptor.";
RL   Br. J. Pharmacol. 140:932-938(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Suwa M., Sato T., Okouchi I., Arita M., Futami K., Matsumoto S.,
RA   Tsutsumi S., Aburatani H., Asai K., Akiyama Y.;
RT   "Genome-wide discovery and analysis of human seven transmembrane helix
RT   receptor genes.";
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12044878; DOI=10.1016/S0014-5793(02)02775-8;
RA   Takeda S., Kadowaki S., Haga T., Takaesu H., Mitaku S.;
RT   "Identification of G protein-coupled receptor genes from the human
RT   genome sequence.";
RL   FEBS Lett. 520:97-101(2002).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA   Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA   Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA   McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA   Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA   Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA   Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA   Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA   Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA   Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA   Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA   Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA   Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA   Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA   Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA   Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA   Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA   Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA   Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA   Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA   Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA   Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA   Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT SER-329.
RC   TISSUE=Testis;
RA   Kaighin V.A., Martin A.L., Aronstam R.S.;
RL   Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-329.
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [9]
RP   FUNCTION AS A RECEPTOR FOR INSL5.
RX   PubMed=15525639; DOI=10.1074/jbc.M409916200;
RA   Liu C., Kuei C., Sutton S., Chen J., Bonaventure P., Wu J.,
RA   Nepomuceno D., Kamme F., Tran D.T., Zhu J., Wilkinson T., Bathgate R.,
RA   Eriste E., Sillard R., Lovenberg T.W.;
RT   "INSL5 is a high affinity specific agonist for GPCR142 (GPR100).";
RL   J. Biol. Chem. 280:292-300(2005).
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.
CC       {ECO:0000269|PubMed:14522967, ECO:0000269|PubMed:15525639}.
CC   -!- INTERACTION:
CC       Q8WXF3:RLN3; NbExp=9; IntAct=EBI-9519524, EBI-9519546;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Expressed in a broader range of tissues
CC       including brain, kidney, testis, thymus, placenta, prostate,
CC       salivary gland, thyroid and colon. {ECO:0000269|PubMed:14530218}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC05844.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; AY394502; AAQ92316.1; -; mRNA.
DR   EMBL; AY288415; AAP72124.1; -; mRNA.
DR   EMBL; AY170824; AAO17676.1; -; mRNA.
DR   EMBL; AB065617; BAC05844.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AB083593; BAB89306.1; -; Genomic_DNA.
DR   EMBL; AL355388; CAH72626.1; -; Genomic_DNA.
DR   EMBL; EU432129; ABY87928.1; -; mRNA.
DR   EMBL; BC101507; AAI01508.1; -; mRNA.
DR   EMBL; BC101509; AAI01510.1; -; mRNA.
DR   CCDS; CCDS1124.1; -.
DR   RefSeq; NP_871001.1; NM_181885.2.
DR   UniGene; Hs.449914; -.
DR   ProteinModelPortal; Q8TDU9; -.
DR   BioGrid; 130880; 3.
DR   IntAct; Q8TDU9; 1.
DR   STRING; 9606.ENSP00000357301; -.
DR   BindingDB; Q8TDU9; -.
DR   ChEMBL; CHEMBL1628473; -.
DR   GuidetoPHARMACOLOGY; 354; -.
DR   iPTMnet; Q8TDU9; -.
DR   PhosphoSitePlus; Q8TDU9; -.
DR   BioMuta; RXFP4; -.
DR   DMDM; 38258194; -.
DR   PaxDb; Q8TDU9; -.
DR   PeptideAtlas; Q8TDU9; -.
DR   PRIDE; Q8TDU9; -.
DR   Ensembl; ENST00000368318; ENSP00000357301; ENSG00000173080.
DR   GeneID; 339403; -.
DR   KEGG; hsa:339403; -.
DR   UCSC; uc010pgs.3; human.
DR   CTD; 339403; -.
DR   GeneCards; RXFP4; -.
DR   HGNC; HGNC:14666; RXFP4.
DR   MIM; 609043; gene.
DR   neXtProt; NX_Q8TDU9; -.
DR   OpenTargets; ENSG00000173080; -.
DR   PharmGKB; PA28848; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   eggNOG; ENOG410XRW9; LUCA.
DR   GeneTree; ENSGT00760000119055; -.
DR   HOGENOM; HOG000230485; -.
DR   HOVERGEN; HBG101327; -.
DR   InParanoid; Q8TDU9; -.
DR   KO; K08398; -.
DR   OMA; LWVLGNC; -.
DR   OrthoDB; EOG091G0CM0; -.
DR   PhylomeDB; Q8TDU9; -.
DR   TreeFam; TF330024; -.
DR   BioCyc; ZFISH:ENSG00000173080-MONOMER; -.
DR   Reactome; R-HSA-418594; G alpha (i) signalling events.
DR   Reactome; R-HSA-444821; Relaxin receptors.
DR   GeneWiki; Relaxin/insulin-like_family_peptide_receptor_4; -.
DR   GenomeRNAi; 339403; -.
DR   PRO; PR:Q8TDU9; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   Bgee; ENSG00000173080; -.
DR   CleanEx; HS_RXFP4; -.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0008528; F:G-protein coupled peptide receptor activity; IBA:GO_Central.
DR   GO; GO:0007218; P:neuropeptide 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; IEA:Ensembl.
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   1: Evidence at protein level;
KW   Cell membrane; Complete proteome; Disulfide bond;
KW   G-protein coupled receptor; Glycoprotein; Membrane; Polymorphism;
KW   Receptor; Reference proteome; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    374       Relaxin-3 receptor 2.
FT                                /FTId=PRO_0000070106.
FT   TOPO_DOM      1     43       Extracellular. {ECO:0000255}.
FT   TRANSMEM     44     64       Helical; Name=1. {ECO:0000255}.
FT   TOPO_DOM     65     78       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM     79     99       Helical; Name=2. {ECO:0000255}.
FT   TOPO_DOM    100    116       Extracellular. {ECO:0000255}.
FT   TRANSMEM    117    137       Helical; Name=3. {ECO:0000255}.
FT   TOPO_DOM    138    154       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    155    175       Helical; Name=4. {ECO:0000255}.
FT   TOPO_DOM    176    209       Extracellular. {ECO:0000255}.
FT   TRANSMEM    210    230       Helical; Name=5. {ECO:0000255}.
FT   TOPO_DOM    231    249       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    250    270       Helical; Name=6. {ECO:0000255}.
FT   TOPO_DOM    271    281       Extracellular. {ECO:0000255}.
FT   TRANSMEM    282    302       Helical; Name=7. {ECO:0000255}.
FT   TOPO_DOM    303    374       Cytoplasmic. {ECO:0000255}.
FT   CARBOHYD      5      5       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD     17     17       N-linked (GlcNAc...). {ECO:0000255}.
FT   DISULFID    114    191       {ECO:0000255|PROSITE-ProRule:PRU00521}.
FT   VARIANT     329    329       L -> S (in dbSNP:rs2152051).
FT                                {ECO:0000269|PubMed:14522967,
FT                                ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|Ref.7}.
FT                                /FTId=VAR_021516.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT        56    309       ipfam:7tm_1 [T]
FT   MYHIT        56    309       iprf:G_PROTEIN_RECEP_F1_2 [T]
SQ   SEQUENCE   374 AA;  41141 MW;  1929EA812C0804DA CRC64;
     MPTLNTSASP PTFFWANASG GSVLSADDAP MPVKFLALRL MVALAYGLVG AIGLLGNLAV
     LWVLSNCARR APGPPSDTFV FNLALADLGL ALTLPFWAAE SALDFHWPFG GALCKMVLTA
     TVLNVYASIF LITALSVARY WVVAMAAGPG THLSLFWARI ATLAVWAAAA LVTVPTAVFG
     VEGEVCGVRL CLLRFPSRYW LGAYQLQRVV LAFMVPLGVI TTSYLLLLAF LQRRQRRRQD
     SRVVARSVRI LVASFFLCWF PNHVVTLWGV LVKFDLVPWN STFYTIQTYV FPVTTCLAHS
     NSCLNPVLYC LLRREPRQAL AGTFRDLRLR LWPQGGGWVQ QVALKQVGRR WVASNPRESR
     PSTLLTNLDR GTPG
//