REL3_PANTR
ID REL3_PANTR Reviewed; 142 AA.
AC Q5CZK2;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Relaxin-3;
DE AltName: Full=Prorelaxin H3;
DE Contains:
DE RecName: Full=Relaxin-3 B chain;
DE Contains:
DE RecName: Full=Relaxin-3 A chain;
DE Flags: Precursor;
GN Name=RLN3;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2]
RP IDENTIFICATION.
RX PubMed=15707501; DOI=10.1186/1471-2148-5-14;
RA Wilkinson T.N., Speed T.P., Tregear G.W., Bathgate R.A.D.;
RT "Evolution of the relaxin-like peptide family.";
RL BMC Evol. Biol. 5:14-14(2005).
CC -!- FUNCTION: May play a role in neuropeptide signaling processes. Ligand
CC for LGR7, RXFP3 and RXFP4 (By similarity). {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 -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR RefSeq; XP_001171356.2; XM_001171356.5.
DR AlphaFoldDB; Q5CZK2; -.
DR STRING; 9598.ENSPTRP00000018051; -.
DR PaxDb; Q5CZK2; -.
DR Ensembl; ENSPTRT00000019501; ENSPTRP00000018051; ENSPTRG00000010576.
DR GeneID; 747967; -.
DR KEGG; ptr:747967; -.
DR CTD; 117579; -.
DR VGNC; VGNC:2265; RLN3.
DR eggNOG; ENOG502S2C4; Eukaryota.
DR GeneTree; ENSGT00940000154396; -.
DR HOGENOM; CLU_120043_0_0_1; -.
DR InParanoid; Q5CZK2; -.
DR OMA; CEWGCSK; -.
DR OrthoDB; 1354498at2759; -.
DR TreeFam; TF333404; -.
DR Proteomes; UP000002277; Chromosome 19.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IBA:GO_Central.
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 Pfam; PF00049; Insulin; 1.
DR PRINTS; PR00276; INSULINFAMLY.
DR SMART; SM00078; IlGF; 1.
DR SUPFAM; SSF56994; SSF56994; 1.
DR PROSITE; PS00262; INSULIN; 1.
PE 3: Inferred from homology;
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..52
FT /note="Relaxin-3 B chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000016088"
FT PROPEP 55..118
FT /note="Connecting peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000016089"
FT PEPTIDE 119..142
FT /note="Relaxin-3 A chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000016090"
FT DISULFID 35..129
FT /note="Interchain (between B and A chains)"
FT /evidence="ECO:0000250"
FT DISULFID 47..142
FT /note="Interchain (between B and A chains)"
FT /evidence="ECO:0000250"
FT DISULFID 128..133
FT /evidence="ECO:0000250"
SQ SEQUENCE 142 AA; 15348 MW; B00AA5B29E3E2087 CRC64;
MARYKLLLLL AVWVLTGELW PGAEARAAPY GVRLCGREFI RAVIFTCGGS RWRRSDILAH
EAMGDTFPDA DADGDSLAGE LDEAMGSSEW LALTKSPQAF YRGRPSWQGT PGALRGSRDV
LAGLSSSCCK WGCSKSEISS LC