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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
 
 
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