ID G1DGC9_CAPHI Unreviewed; 179 AA.
AC G1DGC9;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Insulin-like growth factor II {ECO:0000256|ARBA:ARBA00018566};
GN Name=IGF2 {ECO:0000313|EMBL:AEJ84333.1};
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925 {ECO:0000313|EMBL:AEJ84333.1};
RN [1] {ECO:0000313|EMBL:AEJ84333.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Kidney {ECO:0000313|EMBL:AEJ84333.1};
RA Sharma U., Joshi J., Banerjee P., Vijh R.K.;
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Preptin undergoes glucose-mediated co-secretion with insulin,
CC and acts as a physiological amplifier of glucose-mediated insulin
CC secretion. Exhibits osteogenic properties by increasing osteoblast
CC mitogenic activity through phosphoactivation of MAPK1 and MAPK3.
CC {ECO:0000256|ARBA:ARBA00043916}.
CC -!- FUNCTION: The insulin-like growth factors possess growth-promoting
CC activity (By similarity). Major fetal growth hormone in mammals. Plays
CC a key role in regulating fetoplacental development. IGF2 is influenced
CC by placental lactogen. Also involved in tissue differentiation. In
CC adults, involved in glucose metabolism in adipose tissue, skeletal
CC muscle and liver. Acts as a ligand for integrin which is required for
CC IGF2 signaling. Positively regulates myogenic transcription factor
CC MYOD1 function by facilitating the recruitment of transcriptional
CC coactivators, thereby controlling muscle terminal differentiation (By
CC similarity). Inhibits myoblast differentiation and modulates metabolism
CC via increasing the mitochondrial respiration rate.
CC {ECO:0000256|ARBA:ARBA00025573}.
CC -!- SUBUNIT: Interacts with MYORG; this interaction is required for IGF2
CC secretion. Interacts with integrins ITGAV:ITGB3 and ITGA6:ITGB4;
CC integrin-binding is required for IGF2 signaling.
CC {ECO:0000256|ARBA:ARBA00011472}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613,
CC ECO:0000256|RuleBase:RU000406}.
CC -!- SIMILARITY: Belongs to the insulin family.
CC {ECO:0000256|ARBA:ARBA00009034, ECO:0000256|RuleBase:RU000406}.
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DR EMBL; JI861845; AEJ84333.1; -; mRNA.
DR AlphaFoldDB; G1DGC9; -.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0005179; F:hormone activity; IEA:InterPro.
DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0001503; P:ossification; IEA:UniProtKB-KW.
DR GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR CDD; cd04368; IlGF; 1.
DR Gene3D; 1.10.100.10; Insulin-like; 1.
DR InterPro; IPR022334; IGF2.
DR InterPro; IPR013576; IGF2_C.
DR InterPro; IPR016179; Insulin-like.
DR InterPro; IPR022350; Insulin-like_growth_factor.
DR InterPro; IPR036438; Insulin-like_sf.
DR InterPro; IPR022353; Insulin_CS.
DR InterPro; IPR022352; Insulin_family.
DR PANTHER; PTHR46886; INSULIN-LIKE GROWTH FACTOR II; 1.
DR PANTHER; PTHR46886:SF1; INSULIN-LIKE GROWTH FACTOR II; 1.
DR Pfam; PF08365; IGF2_C; 1.
DR Pfam; PF00049; Insulin; 2.
DR PRINTS; PR02002; INSLNLIKEGF.
DR PRINTS; PR02006; INSLNLIKEGF2.
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 Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR622350-50};
KW Glucose metabolism {ECO:0000256|ARBA:ARBA00022526};
KW Growth factor {ECO:0000256|ARBA:ARBA00023030};
KW Mitogen {ECO:0000256|ARBA:ARBA00023246};
KW Osteogenesis {ECO:0000256|ARBA:ARBA00022855};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU000406};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..179
FT /note="Insulin-like growth factor II"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003412052"
FT DOMAIN 30..84
FT /note="Insulin-like"
FT /evidence="ECO:0000259|SMART:SM00078"
FT REGION 157..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 33..71
FT /evidence="ECO:0000256|PIRSR:PIRSR622350-50"
FT DISULFID 45..84
FT /evidence="ECO:0000256|PIRSR:PIRSR622350-50"
FT DISULFID 70..75
FT /evidence="ECO:0000256|PIRSR:PIRSR622350-50"
SQ SEQUENCE 179 AA; 19495 MW; 02A736671BCFB6B0 CRC64;
MGITAGKSML VLLAFLPFAT CCYAPSRPSE TLCGGELVDT LQFVCGDRGF YFSRPSSRIN
RRSRGIGEEC CFRSCDLALL ETYCPPPAKS ERDVSASTTV LPDDFTASPV GKFFQSDPWK
QSPQRLRRGL PAFLRAPRGR TLAKELEALR EAKSHRPLIA LPTRAPATHG GASPEASSD
//
