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Database: UniProt
Entry: INSL3_RAT
LinkDB: INSL3_RAT
Original site: INSL3_RAT 
ID   INSL3_RAT               Reviewed;         128 AA.
AC   Q9WUK0; Q9WUK1;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2003, sequence version 2.
DT   24-JAN-2024, entry version 145.
DE   RecName: Full=Insulin-like 3;
DE   AltName: Full=Leydig insulin-like peptide;
DE            Short=Ley-I-L;
DE   AltName: Full=Relaxin-like factor;
DE   Contains:
DE     RecName: Full=Insulin-like 3 B chain;
DE   Contains:
DE     RecName: Full=Insulin-like 3 A chain;
DE   Flags: Precursor;
GN   Name=Insl3; Synonyms=Rlf;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RC   STRAIN=Sprague-Dawley; TISSUE=Testis;
RX   PubMed=10542371;
RX   DOI=10.1002/(sici)1098-2795(199912)54:4<319::aid-mrd1>3.0.co;2-z;
RA   Spiess A.-N., Balvers M., Tena-Sempere M., Huhtaniemi I., Parry L.,
RA   Ivell R.;
RT   "Structure and expression of the rat relaxin-like factor (RLF) gene.";
RL   Mol. Reprod. Dev. 54:319-325(1999).
CC   -!- FUNCTION: Seems to play a role in testicular function. May be a trophic
CC       hormone with a role in testicular descent in fetal life. Is a ligand
CC       for LGR8 receptor (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.
CC   -!- TISSUE SPECIFICITY: Expressed in Leydig cells of the testis, and weakly
CC       in the theca interna cells of antral follicles and the corpus luteum of
CC       the ovary. {ECO:0000269|PubMed:10542371}.
CC   -!- DEVELOPMENTAL STAGE: Highly expressed in adult testis and low
CC       expression in the ovary. Highly up-regulated in testes of day 19
CC       embryos, but not in later neonatal stages, nor any ovarian tissue from
CC       this period. {ECO:0000269|PubMed:10542371}.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   EMBL; AF139918; AAD33663.2; -; mRNA.
DR   EMBL; AF139920; AAD33851.1; -; Genomic_DNA.
DR   RefSeq; NP_446132.1; NM_053680.1.
DR   AlphaFoldDB; Q9WUK0; -.
DR   SMR; Q9WUK0; -.
DR   STRING; 10116.ENSRNOP00000025349; -.
DR   PaxDb; 10116-ENSRNOP00000025349; -.
DR   Ensembl; ENSRNOT00000080146.2; ENSRNOP00000073659.2; ENSRNOG00000068505.1.
DR   Ensembl; ENSRNOT00055016310; ENSRNOP00055013109; ENSRNOG00055009650.
DR   Ensembl; ENSRNOT00060019730; ENSRNOP00060015527; ENSRNOG00060011653.
DR   Ensembl; ENSRNOT00065035501; ENSRNOP00065028608; ENSRNOG00065020905.
DR   GeneID; 114215; -.
DR   KEGG; rno:114215; -.
DR   UCSC; RGD:620117; rat.
DR   AGR; RGD:620117; -.
DR   CTD; 3640; -.
DR   RGD; 620117; Insl3.
DR   eggNOG; ENOG502TFQI; Eukaryota.
DR   GeneTree; ENSGT00940000163613; -.
DR   HOGENOM; CLU_164865_0_0_1; -.
DR   InParanoid; Q9WUK0; -.
DR   OMA; NPAHHCC; -.
DR   OrthoDB; 5310508at2759; -.
DR   PhylomeDB; Q9WUK0; -.
DR   TreeFam; TF106361; -.
DR   Reactome; R-RNO-444821; Relaxin receptors.
DR   PRO; PR:Q9WUK0; -.
DR   Proteomes; UP000002494; Chromosome 16.
DR   Bgee; ENSRNOG00000018757; Expressed in testis and 11 other cell types or tissues.
DR   Genevisible; Q9WUK0; RN.
DR   GO; GO:0005615; C:extracellular space; IDA:RGD.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR   GO; GO:0001664; F:G protein-coupled receptor binding; IPI:RGD.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR   GO; GO:0002020; F:protease binding; ISO:RGD.
DR   GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IDA:RGD.
DR   GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR   GO; GO:0008584; P:male gonad development; IDA:RGD.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IDA:RGD.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:RGD.
DR   GO; GO:0001556; P:oocyte maturation; IDA:RGD.
DR   GO; GO:0043950; P:positive regulation of cAMP-mediated signaling; IDA:RGD.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:RGD.
DR   GO; GO:0010634; P:positive regulation of epithelial cell migration; ISO:RGD.
DR   GO; GO:0090303; P:positive regulation of wound healing; ISO:RGD.
DR   GO; GO:2000018; P:regulation of male gonad development; ISO:RGD.
DR   CDD; cd04365; IlGF_relaxin_like; 1.
DR   Gene3D; 1.10.100.10; Insulin-like; 1.
DR   InterPro; IPR043387; INSL3/INSL4.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR036438; Insulin-like_sf.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   PANTHER; PTHR10423; INSULIN-LIKE 3; 1.
DR   PANTHER; PTHR10423:SF3; INSULIN-LIKE 3; 1.
DR   Pfam; PF00049; Insulin; 1.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; Insulin-like; 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..15
FT                   /evidence="ECO:0000255"
FT   PEPTIDE         16..?
FT                   /note="Insulin-like 3 B chain"
FT                   /id="PRO_0000016152"
FT   PROPEP          ?..100
FT                   /note="C peptide like"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000016153"
FT   PEPTIDE         103..128
FT                   /note="Insulin-like 3 A chain"
FT                   /id="PRO_0000016154"
FT   REGION          81..101
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        29..113
FT                   /note="Interchain (between B and A chains)"
FT                   /evidence="ECO:0000250"
FT   DISULFID        41..126
FT                   /note="Interchain (between B and A chains)"
FT                   /evidence="ECO:0000250"
FT   DISULFID        112..117
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   128 AA;  14110 MW;  ABF2EE3AE30ADD53 CRC64;
     MHALLLLLLL ALGSALRSPQ PPEARAKLCG HHLVRALVRV CGGPRWSPEA TQPVDTRDRE
     LLQWLEQRHL LHALVADADP ALDPDPALDP QLPHQASQRQ RRSVATNAVH RCCLTGCTQQ
     DLLGLCPH
//
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