ID   RELX_CANLF              Reviewed;         177 AA.
AC   Q9TRM8; Q9N0Z7; Q9TRM9;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   29-AUG-2001, sequence version 3.
DT   25-MAY-2022, entry version 99.
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   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Placenta;
RX   PubMed=10026098; DOI=10.1095/biolreprod60.3.551;
RA   Klonisch T., Hombach-Klonisch S., Froehlich C., Kauffold J., Steger K.,
RA   Steinetz B.G., Fischer B.;
RT   "Canine preprorelaxin: nucleic acid sequence and localization within the
RT   canine placenta.";
RL   Biol. Reprod. 60:551-557(1999).
RN   [2]
RP   PROTEIN SEQUENCE OF 26-60 AND 154-177.
RC   TISSUE=Placenta;
RX   PubMed=1388669; DOI=10.1007/bf01024863;
RA   Stewart D.R., Henzel W.J., Vandlen R.;
RT   "Purification and sequence determination of canine relaxin.";
RL   J. Protein Chem. 11:247-253(1992).
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   -!- TISSUE SPECIFICITY: Placenta; syncytiotrophoblast.
CC       {ECO:0000269|PubMed:10026098}.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   EMBL; AF233687; AAF60302.1; -; mRNA.
DR   RefSeq; NP_001003132.1; NM_001003132.1.
DR   AlphaFoldDB; Q9TRM8; -.
DR   STRING; 9612.ENSCAFP00000031075; -.
DR   PaxDb; Q9TRM8; -.
DR   PRIDE; Q9TRM8; -.
DR   GeneID; 403742; -.
DR   KEGG; cfa:403742; -.
DR   CTD; 6019; -.
DR   eggNOG; ENOG502TH8D; Eukaryota.
DR   InParanoid; Q9TRM8; -.
DR   OrthoDB; 1331287at2759; -.
DR   Proteomes; UP000002254; 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   1: Evidence at protein level;
KW   Cleavage on pair of basic residues; Direct protein sequencing;
KW   Disulfide bond; Hormone; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000269|PubMed:1388669"
FT   PEPTIDE         26..60
FT                   /note="Relaxin B chain"
FT                   /id="PRO_0000016067"
FT   PROPEP          63..149
FT                   /note="Connecting peptide"
FT                   /id="PRO_0000016068"
FT   PEPTIDE         154..177
FT                   /note="Relaxin A chain"
FT                   /id="PRO_0000016069"
FT   DISULFID        34..164
FT                   /note="Interchain (between B and A chains)"
FT   DISULFID        46..177
FT                   /note="Interchain (between B and A chains)"
FT   DISULFID        163..168
FT   CONFLICT        49
FT                   /note="I -> S (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   177 AA;  20563 MW;  220BB0EC99DD302A CRC64;
     MLRWFLSHLL GVWLLLSQLP REIPATDDKK LKACGRDYVR LQIEVCGSIW WGRKAGQLRE
     RRQISEPLAE VVPSSIINDP EILSLMLQSI PGMPQELRIA TRSGKEKLLR ELHFVLEDSN
     LNLEEMKKTF LNTQFEAEDK SLSKLDKHPR KKRDNYIKMS DKCCNVGCTR RELASRC