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   03-AUG-2022, entry version 114.
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}.
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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   PaxDb; Q8BFS3; -.
DR   Ensembl; ENSRNOT00000007775; ENSRNOP00000007775; ENSRNOG00000005911.
DR   GeneID; 266997; -.
DR   KEGG; rno:266997; -.
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; CEWGCSK; -.
DR   OrthoDB; 1354498at2759; -.
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 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   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR036438; Insulin-like_sf.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   Pfam; PF00049; Insulin; 1.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 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