ID   RELX_FELCA              Reviewed;         180 AA.
AC   Q9MYK8;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Prorelaxin;
DE            Short=RXN;
DE   Contains:
DE     RecName: Full=Relaxin B chain;
DE   Contains:
DE     RecName: Full=Relaxin A chain;
DE   Flags: Precursor;
GN   Name=RLN;
OS   Felis catus (Cat) (Felis silvestris catus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX   NCBI_TaxID=9685;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Placenta;
RX   PubMed=9915995; DOI=10.1095/biolreprod60.2.305;
RA   Klonisch T., Hombach-Klonisch S., Froehlich C., Kauffold J., Steger K.,
RA   Huppertz B., Fischer B.;
RT   "Nucleic acid sequence of feline preprorelaxin and its localization within
RT   the feline placenta.";
RL   Biol. Reprod. 60:305-311(1999).
CC   -!- FUNCTION: Relaxin is an ovarian hormone that acts with estrogen to
CC       produce dilatation of the birth canal in many mammals. {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the placenta. Exclusively detected in
CC       cells located in the lamellar placental labyrinth and absent from other
CC       placental and non-placental uterine parts.
CC       {ECO:0000269|PubMed:9915995}.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   EMBL; AF233688; AAF60303.1; -; mRNA.
DR   RefSeq; NP_001009317.1; NM_001009317.1.
DR   AlphaFoldDB; Q9MYK8; -.
DR   SMR; Q9MYK8; -.
DR   STRING; 9685.ENSFCAP00000010657; -.
DR   GeneID; 493883; -.
DR   KEGG; fca:493883; -.
DR   CTD; 100329416; -.
DR   eggNOG; ENOG502TH8D; Eukaryota.
DR   InParanoid; Q9MYK8; -.
DR   OrthoDB; 1331287at2759; -.
DR   TreeFam; TF333404; -.
DR   Proteomes; UP000011712; 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..25
FT                   /evidence="ECO:0000250"
FT   PEPTIDE         26..51
FT                   /note="Relaxin B chain"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000250468"
FT   PROPEP          53..154
FT                   /note="Connecting peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000250469"
FT   PEPTIDE         157..180
FT                   /note="Relaxin A chain"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000250470"
FT   DISULFID        33..167
FT                   /note="Interchain (between B and A chains)"
FT                   /evidence="ECO:0000250"
FT   DISULFID        45..180
FT                   /note="Interchain (between B and A chains)"
FT                   /evidence="ECO:0000250"
FT   DISULFID        166..171
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   180 AA;  20360 MW;  4C2CF371C698AF9F CRC64;
     MLRLFLSHLL GVWLLLSLRA RKIPAQEEVL KACGREFVRL QIRICGSLSW GKSSQQHREP
     RQAPAALPEI VSSSITSGAE ALNGMLEYIP DLPQELKATL SEREPSFREL QPSLKDSNLN
     LEEVEKSILG RQNEAEDQSL SQLGRSRLDA HSRIKRSDYI RYSDRCCNVG CTRKELADLC