RELX_PIG
ID RELX_PIG Reviewed; 182 AA.
AC P01348;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 25-MAY-2022, entry version 130.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6897721; DOI=10.1089/dna.1.1982.1.155;
RA Haley J., Hudson P., Scanlon D., John M., Cronk M., Shine J., Tregear G.,
RA Niall H.;
RT "Porcine relaxin: molecular cloning and cDNA structure.";
RL DNA 1:155-162(1982).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2442155; DOI=10.1016/s0021-9258(18)45299-4;
RA Haley J., Crawford R., Hudson P., Scanlon D., Tregear G., Shine J.,
RA Niall H.;
RT "Porcine relaxin. Gene structure and expression.";
RL J. Biol. Chem. 262:11940-11946(1987).
RN [3]
RP PRELIMINARY PROTEIN SEQUENCE OF 25-54 AND 161-182.
RX PubMed=876374; DOI=10.1038/267544a0;
RA James R., Niall H., Kwok S., Bryant-Greenwood G.;
RT "Primary structure of porcine relaxin: homology with insulin and related
RT growth factors.";
RL Nature 267:544-546(1977).
RN [4]
RP PROTEIN SEQUENCE OF 25-51.
RX PubMed=851452; DOI=10.1016/0006-291x(77)91070-1;
RA Schwabe C., McDonald J.K., Steinetz B.G.;
RT "Primary structure of the B-chain of porcine relaxin.";
RL Biochem. Biophys. Res. Commun. 75:503-510(1977).
RN [5]
RP PYROGLUTAMATE FORMATION AT GLN-25.
RX PubMed=843375; DOI=10.1016/0006-291x(77)90612-x;
RA Schwabe C., McDonald J.K.;
RT "Demonstration of a pyroglutamyl residue at the N-terminus of the B-chain
RT of porcine relaxin.";
RL Biochem. Biophys. Res. Commun. 74:1501-1504(1977).
RN [6]
RP PROTEIN SEQUENCE OF 161-182.
RX PubMed=938497; DOI=10.1016/0006-291x(76)91059-7;
RA Schwabe C., McDonald J.K., Steinetz B.G.;
RT "Primary structure of the A chain of porcine relaxin.";
RL Biochem. Biophys. Res. Commun. 70:397-405(1976).
RN [7]
RP DISULFIDE BONDS.
RX PubMed=887933; DOI=10.1126/science.887933;
RA Schwabe C., McDonald J.K.;
RT "Relaxin: a disulfide homolog of insulin.";
RL Science 197:914-915(1977).
RN [8]
RP 3D-STRUCTURE MODELING.
RX PubMed=622170; DOI=10.1038/271278a0;
RA Isaacs N.W., James R., Niall H., Bryant-Greenwood G., Dodson G.G.,
RA Evans A., North A.C.T.;
RT "Relaxin and its structural relationship to insulin.";
RL Nature 271:278-281(1978).
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 EMBL; K01088; AAA31114.1; -; mRNA.
DR EMBL; J02792; AAA31115.1; -; Genomic_DNA.
DR PIR; A90934; RXPG.
DR RefSeq; NP_999037.1; NM_213872.1.
DR AlphaFoldDB; P01348; -.
DR SMR; P01348; -.
DR MINT; P01348; -.
DR STRING; 9823.ENSSSCP00000005607; -.
DR PaxDb; P01348; -.
DR PRIDE; P01348; -.
DR GeneID; 396891; -.
DR KEGG; ssc:396891; -.
DR CTD; 6019; -.
DR eggNOG; ENOG502TH8D; Eukaryota.
DR InParanoid; P01348; -.
DR OrthoDB; 1331287at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR GO; GO:0001832; P:blastocyst growth; IDA:CACAO.
DR GO; GO:0030317; P:flagellated sperm motility; IDA:CACAO.
DR GO; GO:0001556; P:oocyte maturation; IDA:CACAO.
DR GO; GO:2000344; P:positive regulation of acrosome reaction; IDA:CACAO.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IDA:CACAO.
DR GO; GO:0046326; P:positive regulation of glucose import; IDA:CACAO.
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; Pyrrolidone carboxylic acid; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:851452"
FT PEPTIDE 25..56
FT /note="Relaxin B chain"
FT /evidence="ECO:0000269|PubMed:6897721"
FT /id="PRO_0000016112"
FT PROPEP 57..154
FT /note="Connecting peptide"
FT /id="PRO_0000016113"
FT PROPEP 159..160
FT /evidence="ECO:0000269|PubMed:938497"
FT /id="PRO_0000016114"
FT PEPTIDE 161..182
FT /note="Relaxin A chain"
FT /evidence="ECO:0000269|PubMed:6897721"
FT /id="PRO_0000016115"
FT MOD_RES 25
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:843375,
FT ECO:0000269|PubMed:876374"
FT DISULFID 34..169
FT /note="Interchain (between B and A chains)"
FT /evidence="ECO:0000269|PubMed:887933"
FT DISULFID 46..182
FT /note="Interchain (between B and A chains)"
FT /evidence="ECO:0000269|PubMed:887933"
FT DISULFID 168..173
FT /evidence="ECO:0000269|PubMed:887933"
FT CONFLICT 47
FT /note="G -> GVWS (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 51..54
FT /note="WGRT -> TWGR (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="S -> L (in Ref. 2; AAA31115)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="Q -> E (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 182 AA; 20818 MW; 20736EB089F13AB4 CRC64;
MPRLFSYLLG VWLLLSQLPR EIPGQSTNDF IKACGRELVR LWVEICGSVS WGRTALSLEE
PQLETGPPAE TMPSSITKDA EILKMMLEFV PNLPQELKAT LSERQPSLRE LQQSASKDSN
LNFEEFKKII LNRQNEAEDK SLLELKNLGL DKHSRKKRLF RMTLSEKCCQ VGCIRKDIAR
LC
