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INSL3_MOUSE
ID   INSL3_MOUSE             Reviewed;         122 AA.
AC   O09107; P97744;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2001, sequence version 2.
DT   25-MAY-2022, entry version 139.
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   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/SvJ;
RA   Zimmermann S.H.;
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Testis;
RX   PubMed=8770925; DOI=10.1210/endo.137.7.8770925;
RA   Pusch W., Balvers M., Ivell R.;
RT   "Molecular cloning and expression of the relaxin-like factor from the mouse
RT   testis.";
RL   Endocrinology 137:3009-3013(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/SvJ;
RX   PubMed=9428631; DOI=10.1016/s0014-5793(97)01454-3;
RA   Koskimies P., Spiess A.N., Lahti P., Huhtaniemi I., Ivell R.;
RT   "The mouse relaxin-like factor gene and its promoter are located within the
RT   3' region of the JAK3 genomic sequence.";
RL   FEBS Lett. 419:186-190(1997).
RN   [4]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=10391220; DOI=10.1038/10364;
RA   Nef S., Parada L.F.;
RT   "Cryptorchidism in mice mutant for Insl3.";
RL   Nat. Genet. 22:295-299(1999).
RN   [5]
RP   FUNCTION.
RX   PubMed=11342953; DOI=10.1016/s0022-5347(05)66389-6;
RA   Kubota Y., Nef S., Farmer P.J., Temelcos C., Parada L.F., Hutson J.M.;
RT   "Leydig insulin-like hormone, gubernacular development and testicular
RT   descent.";
RL   J. Urol. 165:1673-1675(2001).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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       ECO:0000269|PubMed:10391220, ECO:0000269|PubMed:11342953}.
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 exclusively in Leydig cells of the
CC       testis.
CC   -!- DISRUPTION PHENOTYPE: Male mice exhibit bilateral abdominal
CC       cryptorchidism due to alteration of gubernaculum development.
CC       {ECO:0000269|PubMed:10391220}.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR   EMBL; X95603; CAA64861.1; -; Genomic_DNA.
DR   EMBL; S82815; AAB39365.1; -; mRNA.
DR   EMBL; AF136524; AAD24585.1; -; Genomic_DNA.
DR   CCDS; CCDS22404.1; -.
DR   AlphaFoldDB; O09107; -.
DR   STRING; 10090.ENSMUSP00000034261; -.
DR   PaxDb; O09107; -.
DR   PRIDE; O09107; -.
DR   ProteomicsDB; 269065; -.
DR   MGI; MGI:108427; Insl3.
DR   eggNOG; ENOG502TFQI; Eukaryota.
DR   InParanoid; O09107; -.
DR   PhylomeDB; O09107; -.
DR   Reactome; R-MMU-418555; G alpha (s) signalling events.
DR   Reactome; R-MMU-444821; Relaxin receptors.
DR   PRO; PR:O09107; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; O09107; protein.
DR   GO; GO:0005615; C:extracellular space; ISO:MGI.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR   GO; GO:0001664; F:G protein-coupled receptor binding; ISO:MGI.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR   GO; GO:0002020; F:protease binding; ISO:MGI.
DR   GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; ISO:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0008584; P:male gonad development; IMP:MGI.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR   GO; GO:0001556; P:oocyte maturation; ISO:MGI.
DR   GO; GO:0043950; P:positive regulation of cAMP-mediated signaling; ISO:MGI.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR   GO; GO:0010634; P:positive regulation of epithelial cell migration; ISO:MGI.
DR   GO; GO:0090303; P:positive regulation of wound healing; ISO:MGI.
DR   GO; GO:2000018; P:regulation of male gonad development; IMP:CACAO.
DR   InterPro; IPR040113; INSL3.
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; PTHR10423; 1.
DR   PANTHER; PTHR10423:SF6; PTHR10423:SF6; 1.
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   1: Evidence at protein 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_0000016143"
FT   PROPEP          ?..94
FT                   /note="C peptide like"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000016144"
FT   PEPTIDE         97..122
FT                   /note="Insulin-like 3 A chain"
FT                   /id="PRO_0000016145"
FT   DISULFID        29..107
FT                   /note="Interchain (between B and A chains)"
FT                   /evidence="ECO:0000250"
FT   DISULFID        41..120
FT                   /note="Interchain (between B and A chains)"
FT                   /evidence="ECO:0000250"
FT   DISULFID        106..111
FT                   /evidence="ECO:0000250"
FT   CONFLICT        21
FT                   /note="P -> T (in Ref. 1; CAA64861)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        54..58
FT                   /note="VETRD -> CGDPG (in Ref. 1; CAA64861)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        73
FT                   /note="A -> S (in Ref. 1; CAA64861)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        92..96
FT                   /note="QRQRR -> HARG (in Ref. 1; CAA64861)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   122 AA;  13586 MW;  10783AB4896CF103 CRC64;
     MRAPLLLMLL ALGSALRSPQ PPEARAKLCG HHLVRTLVRV CGGPRWSPEA TQPVETRDRE
     LLQWLEQRHL LHALVADVDP ALDPQLPRQA SQRQRRSAAT NAVHRCCLTG CTQQDLLGLC
     PH
 
 
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