RELH_RABIT
ID RELH_RABIT Reviewed; 178 AA.
AC P51456;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Relaxin-like protein SQ10;
DE Contains:
DE RecName: Full=Relaxin-like protein SQ10 B chain;
DE Contains:
DE RecName: Full=Relaxin-like protein SQ10 A chain;
DE Flags: Precursor;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 21-32; 54-77 AND
RP 120-128.
RC TISSUE=Tracheobronchial epithelium;
RX PubMed=1339318;
RA Jetten A.M., Bernacki S.H., Floyd E.E., Saunders N.A., Pieniazek J.,
RA Lotan R.;
RT "Expression of a preprorelaxin-like gene during squamous differentiation of
RT rabbit tracheobronchial epithelial cells and its suppression by retinoic
RT acid.";
RL Cell Growth Differ. 3:549-556(1992).
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 -!- INDUCTION: During squamous cell differentiation. Repressed by retinoic
CC acid.
CC -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR EMBL; S45940; AAB23648.1; -; mRNA.
DR PIR; A49014; A49014.
DR RefSeq; NP_001075789.1; NM_001082320.1.
DR AlphaFoldDB; P51456; -.
DR STRING; 9986.ENSOCUP00000024474; -.
DR GeneID; 100009160; -.
DR KEGG; ocu:100009160; -.
DR CTD; 6013; -.
DR eggNOG; ENOG502TH8D; Eukaryota.
DR OrthoDB; 1331287at2759; -.
DR Proteomes; UP000001811; 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; 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; Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:1339318"
FT PEPTIDE 21..52
FT /note="Relaxin-like protein SQ10 B chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000016127"
FT PROPEP 54..150
FT /note="Connecting peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000016128"
FT PEPTIDE 155..178
FT /note="Relaxin-like protein SQ10 A chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000016129"
FT DISULFID 34..165
FT /note="Interchain (between B and A chains)"
FT /evidence="ECO:0000250"
FT DISULFID 46..178
FT /note="Interchain (between B and A chains)"
FT /evidence="ECO:0000250"
FT DISULFID 164..169
FT /evidence="ECO:0000250"
SQ SEQUENCE 178 AA; 20294 MW; F6A54D98A6B53211 CRC64;
MPALLFYLLG FCLLQGQVTG RVTYEWMMEN VKICRNDFVR TAIEVCGHVH LERESPSPEN
PFLSSGPAAE TVPSSIKKDA ENANTMLESI PNLPQELTAT LFEKQPSKLY LQYLPTLKKS
NVSFEEFKKI IQNIQRGVQG SSASESNTFS RKKRQFSESL PEECCKYGCP RYYLLMYC