REL1_PANTR
ID REL1_PANTR Reviewed; 166 AA.
AC P51454;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Prorelaxin H1;
DE Contains:
DE RecName: Full=Relaxin B chain;
DE Contains:
DE RecName: Full=Relaxin A chain;
DE Flags: Precursor; Fragment;
GN Name=RNL1; Synonyms=RLX1;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Placenta;
RX PubMed=8182365; DOI=10.1677/joe.0.1400385;
RA Evans B.A., Fu P., Tregear G.W.;
RT "Characterization of two relaxin genes in the chimpanzee.";
RL J. Endocrinol. 140:385-392(1994).
CC -!- FUNCTION: Relaxin is an ovarian hormone that acts with estrogen to
CC produce dilatation of the birth canal in many mammals. May be involved
CC in remodeling of connective tissues during pregnancy, promoting growth
CC of pubic ligaments and ripening of the cervix.
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 corpus luteum of pregnancy but not
CC in the placenta.
CC -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR EMBL; Z27225; CAA81739.1; -; mRNA.
DR PIR; S42783; S42783.
DR AlphaFoldDB; P51454; -.
DR SMR; P51454; -.
DR STRING; 9598.ENSPTRP00000054896; -.
DR PaxDb; P51454; -.
DR eggNOG; ENOG502TH8D; Eukaryota.
DR InParanoid; P51454; -.
DR Proteomes; UP000002277; 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; IPR022352; Insulin_family.
DR InterPro; IPR022421; Relaxin.
DR Pfam; PF00049; Insulin; 1.
DR PRINTS; PR00276; INSULINFAMLY.
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..5
FT /evidence="ECO:0000250"
FT PEPTIDE 6..34
FT /note="Relaxin B chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000016106"
FT PROPEP 37..139
FT /note="Connecting peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000016107"
FT PEPTIDE 143..166
FT /note="Relaxin A chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000016108"
FT DISULFID 16..153
FT /note="Interchain (between B and A chains)"
FT /evidence="ECO:0000250"
FT DISULFID 28..166
FT /note="Interchain (between B and A chains)"
FT /evidence="ECO:0000250"
FT DISULFID 152..157
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 166 AA; 18731 MW; 7F469B1FB9259F4F CRC64;
SRAVADSWMD EVIKLCGREL VRAQIAICGM STWSKRSLSQ EDAPQTPRPV AEIVPSFINK
DTETIIIMLE FIANLPPELK AALSERQPSL PEPQQYVPAL KDSNLSFEEF KKLIRNRQSE
AADSNPSELK YLGLDTHSQK KRQPYVALFE KCCLIGCTKR SLANYC