ID   RELX_MESAU              Reviewed;         177 AA.
AC   Q64171;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Prorelaxin;
DE   Contains:
DE     RecName: Full=Relaxin B chain;
DE   Contains:
DE     RecName: Full=Relaxin A chain;
DE   Flags: Precursor;
GN   Name=RLN;
OS   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Placenta;
RX   PubMed=7492700; DOI=10.1095/biolreprod53.2.454;
RA   McCaslin R.B., Renegar R.H.;
RT   "Determination of the prorelaxin nucleotide sequence and expression of
RT   prorelaxin messenger ribonucleic acid in the golden hamster.";
RL   Biol. Reprod. 53:454-461(1995).
CC   -!- FUNCTION: Relaxin is an ovarian hormone that acts with estrogen to
CC       produce dilatation of the birth canal in many mammals. It bears mature
CC       young, and allows separation of the pelvic bones.
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; S79879; AAB35655.1; -; mRNA.
DR   RefSeq; NP_001297483.1; NM_001310554.1.
DR   AlphaFoldDB; Q64171; -.
DR   SMR; Q64171; -.
DR   STRING; 10036.XP_005063768.1; -.
DR   GeneID; 101831439; -.
DR   eggNOG; ENOG502TH8D; Eukaryota.
DR   OrthoDB; 1331287at2759; -.
DR   Proteomes; UP000189706; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR036438; Insulin-like_sf.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022421; Relaxin.
DR   Pfam; PF00049; Insulin; 1.
DR   PRINTS; PR02004; RELAXIN.
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..22
FT                   /evidence="ECO:0000250"
FT   PEPTIDE         23..59
FT                   /note="Relaxin B chain"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000016100"
FT   PROPEP          64..149
FT                   /note="Connecting peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000016101"
FT   PEPTIDE         154..177
FT                   /note="Relaxin A chain"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000016102"
FT   REGION          80..114
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        36..164
FT                   /note="Interchain (between B and A chains)"
FT                   /evidence="ECO:0000250"
FT   DISULFID        48..177
FT                   /note="Interchain (between B and A chains)"
FT                   /evidence="ECO:0000250"
FT   DISULFID        163..168
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   177 AA;  20007 MW;  6925562BD8C66CCD CRC64;
     MSCKFVLQLL GFWLLLSQPC RARVTKEWLD EVIHVCGREY VRAILDICAA TVGLEAPPLR
     RRRMTEEAVS SFIKEDAEPF DTMPNLSEKP KTALPEGHPS LPEQQQYVPV SSDSVGSLDD
     FKKSFHATQG EAEDSSLPEL KSLYLDTLSR KKRYTSIYMS HQCCFRGCSR RSLTAAC