ID   RELX_CAVPO              Reviewed;         160 AA.
AC   P51453;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Prorelaxin;
DE   Contains:
DE     RecName: Full=Relaxin B chain;
DE   Contains:
DE     RecName: Full=Relaxin A chain;
DE   Flags: Precursor; Fragment;
GN   Name=RLN;
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Endometrium;
RX   PubMed=1537282; DOI=10.1210/endo.130.3.1537282;
RA   Lee Y.A., Bryant-Greenwood G.D., Mandel M., Greenwood F.C.;
RT   "The complementary deoxyribonucleic acid sequence of guinea pig endometrial
RT   prorelaxin.";
RL   Endocrinology 130:1165-1172(1992).
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   -!- TISSUE SPECIFICITY: Expressed in the endometrium during pregnancy and
CC       in mammary gland during lactation.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   EMBL; S85964; AAB21586.1; -; mRNA.
DR   PIR; A49194; A49194.
DR   AlphaFoldDB; P51453; -.
DR   SMR; P51453; -.
DR   InParanoid; P51453; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
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.
FT   PEPTIDE         <1..33
FT                   /note="Relaxin B chain"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000016070"
FT   PROPEP          34..133
FT                   /note="Connecting peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000016071"
FT   PEPTIDE         137..160
FT                   /note="Relaxin A chain"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000016072"
FT   DISULFID        10..147
FT                   /note="Interchain (between B and A chains)"
FT                   /evidence="ECO:0000250"
FT   DISULFID        22..160
FT                   /note="Interchain (between B and A chains)"
FT                   /evidence="ECO:0000250"
FT   DISULFID        146..151
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   160 AA;  17892 MW;  E58DF84036467028 CRC64;
     GFLDKVIKVC GRDLVRIKID ICGKILLGDM TTGQEKQRIL GSGQSAEIMP SSINKEVDSL
     NMLESIANLP EELRAMLPEK QPSSPQLQQY VPALKNSNVA VKELNKIIRG RQEEAEDNSH
     SLLKDFNLNI YSPKKRQLDM TVSEKCCQVG CTRRFIANSC