ID REL3_RAT Reviewed; 140 AA. AC Q8BFS3; DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 24-JAN-2024, entry version 120. DE RecName: Full=Relaxin-3; DE AltName: Full=Insulin-like peptide INSL7; DE Short=Insulin-like peptide 7; DE AltName: Full=Prorelaxin R3; DE Contains: DE RecName: Full=Relaxin-3 B chain; DE Contains: DE RecName: Full=Relaxin-3 A chain; DE Flags: Precursor; GN Name=Rln3; Synonyms=Insl7; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RC STRAIN=Sprague-Dawley; TISSUE=Brain; RX PubMed=12354304; DOI=10.1046/j.1471-4159.2002.01114.x; RA Burazin T.C.D., Bathgate R.A.D., Macris M., Layfield S., Gundlach A.L., RA Tregear G.W.; RT "Restricted, but abundant, expression of the novel rat gene-3 (R3) relaxin RT in the dorsal tegmental region of brain."; RL J. Neurochem. 82:1553-1557(2002). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=12686464; DOI=10.1016/s0167-0115(02)00304-x; RA Kizawa H., Nishi K., Ishibashi Y., Harada M., Asano T., Ito Y., Suzuki N., RA Hinuma S., Fujisawa Y., Onda H., Nishimura O., Fujino M.; RT "Production of recombinant human relaxin 3 in AtT20 cells."; RL Regul. Pept. 113:79-84(2003). CC -!- FUNCTION: May play a role in neuropeptide signaling processes. Ligand CC for LGR7, relaxin-3 receptor-1 and relaxin-3 receptor-2 (By CC similarity). {ECO:0000250}. CC -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two CC disulfide bonds. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- TISSUE SPECIFICITY: Highly abundant expression is detected in neurons CC within the ventomedial dorsal tegmental nucleus and the laterally CC central gray alpha of the pons. Also detected at much lower levels CC within the hippocampus. {ECO:0000269|PubMed:12354304}. CC -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY112741; AAM56033.1; -; mRNA. DR EMBL; AB076564; BAC53759.1; -; mRNA. DR RefSeq; NP_733767.1; NM_170667.2. DR AlphaFoldDB; Q8BFS3; -. DR SMR; Q8BFS3; -. DR STRING; 10116.ENSRNOP00000007775; -. DR PhosphoSitePlus; Q8BFS3; -. DR PaxDb; 10116-ENSRNOP00000007775; -. DR Ensembl; ENSRNOT00000007775.5; ENSRNOP00000007775.1; ENSRNOG00000005911.5. DR Ensembl; ENSRNOT00055014014; ENSRNOP00055011237; ENSRNOG00055008295. DR Ensembl; ENSRNOT00060022858; ENSRNOP00060018087; ENSRNOG00060013425. DR Ensembl; ENSRNOT00065015744; ENSRNOP00065011911; ENSRNOG00065009789. DR GeneID; 266997; -. DR KEGG; rno:266997; -. DR AGR; RGD:628745; -. DR CTD; 117579; -. DR RGD; 628745; Rln3. DR eggNOG; ENOG502S2C4; Eukaryota. DR GeneTree; ENSGT00940000154396; -. DR HOGENOM; CLU_120043_0_0_1; -. DR InParanoid; Q8BFS3; -. DR OMA; SSTCCKW; -. DR OrthoDB; 4255151at2759; -. DR PhylomeDB; Q8BFS3; -. DR TreeFam; TF333404; -. DR Reactome; R-RNO-418594; G alpha (i) signalling events. DR Reactome; R-RNO-444821; Relaxin receptors. DR PRO; PR:Q8BFS3; -. DR Proteomes; UP000002494; Chromosome 19. DR Bgee; ENSRNOG00000005911; Expressed in thymus and 9 other cell types or tissues. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0001664; F:G protein-coupled receptor binding; IMP:RGD. DR GO; GO:0005179; F:hormone activity; TAS:RGD. DR CDD; cd04365; IlGF_relaxin_like; 1. DR InterPro; IPR016179; Insulin-like. DR InterPro; IPR036438; Insulin-like_sf. DR InterPro; IPR022353; Insulin_CS. DR InterPro; IPR022352; Insulin_family. DR PANTHER; PTHR20968; ILGF DOMAIN-CONTAINING PROTEIN; 1. DR PANTHER; PTHR20968:SF0; RELAXIN-3; 1. DR Pfam; PF00049; Insulin; 1. DR PRINTS; PR00276; INSULINFAMLY. DR SMART; SM00078; IlGF; 1. DR SUPFAM; SSF56994; Insulin-like; 1. DR PROSITE; PS00262; INSULIN; 1. PE 2: Evidence at transcript level; KW Cleavage on pair of basic residues; Disulfide bond; Hormone; KW Reference proteome; Secreted; Signal. FT SIGNAL 1..23 FT /evidence="ECO:0000250" FT PEPTIDE 24..50 FT /note="Relaxin-3 B chain" FT /evidence="ECO:0000250" FT /id="PRO_0000016094" FT PROPEP 53..116 FT /note="Connecting peptide" FT /evidence="ECO:0000250" FT /id="PRO_0000016095" FT PEPTIDE 117..140 FT /note="Relaxin-3 A chain" FT /evidence="ECO:0000250" FT /id="PRO_0000016096" FT DISULFID 33..127 FT /note="Interchain (between B and A chains)" FT /evidence="ECO:0000250" FT DISULFID 45..140 FT /note="Interchain (between B and A chains)" FT /evidence="ECO:0000250" FT DISULFID 126..131 FT /evidence="ECO:0000250" SQ SEQUENCE 140 AA; 14922 MW; F4B6979756122EDA CRC64; MATRGLLLAS WALLGALVLQ AEARPAPYGV KLCGREFIRA VIFTCGGSRW RRADILAHDP LGEFFADGEA NTDHLASELD EAVGSSEWLA LTKSPQVFYG GRSSWQGSPG VVRGSRDVLA GLSSSCCEWG CSKSQISSLC //