ID   RELX_PHODA              Reviewed;          31 AA.
AC   Q7M3C4;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   RecName: Full=Relaxin B chain;
OS   Phocoenoides dalli dalli (Dall's porpoise).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Phocoenidae; Phocoenoides.
OX   NCBI_TaxID=9745;
RN   [1]
RP   PROTEIN SEQUENCE.
RA   Woods A.S., Cotter R.J., Yoshioka M., Buellesbach E., Schwabe C.;
RT   "Enzymatic digestion on the sample foil as a method for sequence
RT   determination by plasma desorption mass spectrometry: the primary structure
RT   of porpoise relaxin.";
RL   Int. J. Mass Spectrom. Ion Process. 111:77-88(1991).
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   PIR; A58793; A58793.
DR   AlphaFoldDB; Q7M3C4; -.
DR   SMR; Q7M3C4; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR   InterPro; IPR036438; Insulin-like_sf.
DR   SUPFAM; SSF56994; Insulin-like; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Hormone;
KW   Pyrrolidone carboxylic acid; Secreted.
FT   PEPTIDE         1..31
FT                   /note="Relaxin B chain"
FT                   /id="PRO_0000044750"
FT   MOD_RES         1
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000250|UniProtKB:P11184"
SQ   SEQUENCE   31 AA;  3538 MW;  02BAA61A9F5CD896 CRC64;
     QRTNDFIKAC GRELVRVWVE ICGSVSWGRT A
//