ID   REL1_MOUSE              Reviewed;         185 AA.
AC   P47932;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   25-MAY-2022, entry version 124.
DE   RecName: Full=Prorelaxin 1;
DE   Contains:
DE     RecName: Full=Relaxin B chain;
DE   Contains:
DE     RecName: Full=Relaxin A chain;
DE   Flags: Precursor;
GN   Name=Rln1; Synonyms=Rln, Rlx;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=SWR/J; TISSUE=Ovary;
RX   PubMed=8452637; DOI=10.1677/jme.0.0100015;
RA   Evans B.A., John M., Fowler K.J., Summers R.J., Cronk M., Shine J.,
RA   Tregear G.W.;
RT   "The mouse relaxin gene: nucleotide sequence and expression.";
RL   J. Mol. Endocrinol. 10:15-23(1993).
RN   [2]
RP   DISULFIDE BONDS.
RX   PubMed=8216305; DOI=10.1006/bbrc.1993.2250;
RA   Bullesbach E.E., Schwabe C.;
RT   "Mouse relaxin: synthesis and biological activity of the first relaxin with
RT   an unusual crosslinking pattern.";
RL   Biochem. Biophys. Res. Commun. 196:311-319(1993).
CC   -!- FUNCTION: Relaxin is an ovarian hormone that acts with estrogen to
CC       produce dilatation of the birth canal in many mammals.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   EMBL; Z27088; CAA81611.1; -; mRNA.
DR   CCDS; CCDS29733.1; -.
DR   PIR; S48082; S48082.
DR   AlphaFoldDB; P47932; -.
DR   SMR; P47932; -.
DR   STRING; 10090.ENSMUSP00000043376; -.
DR   PaxDb; P47932; -.
DR   PRIDE; P47932; -.
DR   MGI; MGI:97931; Rln1.
DR   eggNOG; ENOG502TH8D; Eukaryota.
DR   InParanoid; P47932; -.
DR   PhylomeDB; P47932; -.
DR   Reactome; R-MMU-418555; G alpha (s) signalling events.
DR   Reactome; R-MMU-444821; Relaxin receptors.
DR   PRO; PR:P47932; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; P47932; protein.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR   GO; GO:0005102; F:signaling receptor binding; IDA:MGI.
DR   GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; ISO:MGI.
DR   GO; GO:0048589; P:developmental growth; IMP:MGI.
DR   GO; GO:0060443; P:mammary gland morphogenesis; IMP:CACAO.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR   GO; GO:0060618; P:nipple development; IMP:CACAO.
DR   GO; GO:0060736; P:prostate gland growth; IMP:MGI.
DR   GO; GO:0042981; P:regulation of apoptotic process; IMP:CACAO.
DR   GO; GO:0042127; P:regulation of cell population proliferation; ISO:MGI.
DR   GO; GO:0010749; P:regulation of nitric oxide mediated signal transduction; IMP:MGI.
DR   GO; GO:0007283; P:spermatogenesis; IMP:CACAO.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR036438; Insulin-like_sf.
DR   InterPro; IPR022421; Relaxin.
DR   Pfam; PF00049; Insulin; 1.
DR   PRINTS; PR02004; RELAXIN.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
PE   1: Evidence at protein level;
KW   Cleavage on pair of basic residues; Disulfide bond; Hormone;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000250"
FT   PEPTIDE         23..57
FT                   /note="Relaxin B chain"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000016103"
FT   PROPEP          58..156
FT                   /note="Connecting peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000016104"
FT   PEPTIDE         161..185
FT                   /note="Relaxin A chain"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000016105"
FT   REGION          135..161
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        36..171
FT                   /note="Interchain (between B and A chains)"
FT                   /evidence="ECO:0000269|PubMed:8216305"
FT   DISULFID        48..185
FT                   /note="Interchain (between B and A chains)"
FT                   /evidence="ECO:0000269|PubMed:8216305"
FT   DISULFID        170..175
FT                   /evidence="ECO:0000269|PubMed:8216305"
SQ   SEQUENCE   185 AA;  20571 MW;  2B9E753E8B85087B CRC64;
     MSSRFLLQLL GFWLLLSQPC RTRVSEEWMD GFIRMCGREY ARELIKICGA SVGRLALSQE
     EPALLARQAT EVVPSFINKD AEPFDTTLKC LPNLSEELKA VLSEAQASLP ELQHAPVLSD
     SVVSLEGFKK TLHDRLGEAE DGSPPGLKYL QSDTHSRKKR ESGGLMSQQC CHVGCSRRSI
     AKLYC