IGF2_MOUSE
ID IGF2_MOUSE Reviewed; 180 AA.
AC P09535; E9QLW5;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Insulin-like growth factor II;
DE AltName: Full=IGF-II;
DE AltName: Full=Multiplication-stimulating polypeptide;
DE Contains:
DE RecName: Full=Insulin-like growth factor II;
DE Contains:
DE RecName: Full=Preptin;
DE Flags: Precursor;
GN Name=Igf2; Synonyms=Igf-2;
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 [MRNA].
RX PubMed=3780370; DOI=10.1089/dna.1986.5.357;
RA Stempien M.M., Fong N.M., Rall L.B., Bell G.I.;
RT "Sequence of a placental cDNA encoding the mouse insulin-like growth factor
RT II precursor.";
RL DNA 5:357-361(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1702294; DOI=10.1089/dna.1990.9.725;
RA Rotwein P., Hall L.J.;
RT "Evolution of insulin-like growth factor II: characterization of the mouse
RT IGF-II gene and identification of two pseudo-exons.";
RL DNA Cell Biol. 9:725-735(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9039503; DOI=10.1093/dnares/3.5.331;
RA Sasaki H., Shimozaki K., Zubair M., Aoki N., Hatano N., Moore T., Feil R.,
RA Constancia M., Reik W., Rotwein P.;
RT "Nucleotide sequence of a 28-kb mouse genomic region comprising the
RT imprinted Igf2 gene.";
RL DNA Res. 3:331-335(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 2).
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-52.
RX PubMed=2537977; DOI=10.1073/pnas.86.5.1543;
RA Tollefsen S.E., Sadow J.L., Rotwein P.;
RT "Coordinate expression of insulin-like growth factor II and its receptor
RT during muscle differentiation.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:1543-1547(1989).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-52 AND 103-180.
RC STRAIN=BALB/cJ; TISSUE=Spleen;
RX PubMed=8265819; DOI=10.1016/0167-0115(93)90337-8;
RA Holthuizen P.E., Cleutjens C.B., Veenstra G.J., van der Lee F.M.,
RA Koonen-Reemst A.M., Sussenbach J.S.;
RT "Differential expression of the human, mouse and rat IGF-II genes.";
RL Regul. Pept. 48:77-89(1993).
RN [8]
RP PROTEIN SEQUENCE OF 93-126, AND INSULIN-ENHANCING FUNCTION OF PREPTIN.
RX PubMed=11716772; DOI=10.1042/0264-6021:3600431;
RA Buchanan C.M., Phillips A.R., Cooper G.J.;
RT "Preptin derived from proinsulin-like growth factor II (proIGF-II) is
RT secreted from pancreatic islet beta-cells and enhances insulin secretion.";
RL Biochem. J. 360:431-439(2001).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=2330056; DOI=10.1038/345078a0;
RA DeChiara T.M., Efstratiadis A., Robertson E.J.;
RT "A growth-deficiency phenotype in heterozygous mice carrying an insulin-
RT like growth factor II gene disrupted by targeting.";
RL Nature 345:78-80(1990).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, AND MISCELLANEOUS.
RX PubMed=1997210; DOI=10.1016/0092-8674(91)90513-x;
RA DeChiara T.M., Robertson E.J., Efstratiadis A.;
RT "Parental imprinting of the mouse insulin-like growth factor II gene.";
RL Cell 64:849-859(1991).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12087403; DOI=10.1038/nature00819;
RA Constancia M., Hemberger M., Hughes J., Dean W., Ferguson-Smith A.,
RA Fundele R., Stewart F., Kelsey G., Fowden A., Sibley C., Reik W.;
RT "Placental-specific IGF-II is a major modulator of placental and fetal
RT growth.";
RL Nature 417:945-948(2002).
RN [12]
RP FUNCTION.
RX PubMed=16901893; DOI=10.1074/jbc.m605445200;
RA Wilson E.M., Rotwein P.;
RT "Control of MyoD function during initiation of muscle differentiation by an
RT autocrine signaling pathway activated by insulin-like growth factor-II.";
RL J. Biol. Chem. 281:29962-29971(2006).
RN [13]
RP OSTEOGENIC FUNCTION OF PREPTIN.
RX PubMed=16912056; DOI=10.1152/ajpendo.00642.2005;
RA Cornish J., Callon K.E., Bava U., Watson M., Xu X., Lin J.M., Chan V.A.,
RA Grey A.B., Naot D., Buchanan C.M., Cooper G.J., Reid I.R.;
RT "Preptin, another peptide product of the pancreatic beta-cell, is
RT osteogenic in vitro and in vivo.";
RL Am. J. Physiol. 292:E117-E122(2007).
RN [14]
RP INTERACTION WITH MYORG.
RX PubMed=19706595; DOI=10.1074/jbc.m109.034041;
RA Datta K., Guan T., Gerace L.;
RT "NET37, a nuclear envelope transmembrane protein with glycosidase homology,
RT is involved in myoblast differentiation.";
RL J. Biol. Chem. 284:29666-29676(2009).
RN [15]
RP REVIEW OF FUNCTION.
RX PubMed=24593700; DOI=10.1111/cen.12446;
RA Livingstone C., Borai A.;
RT "Insulin-like growth factor-II: its role in metabolic and endocrine
RT disease.";
RL Clin. Endocrinol. (Oxf.) 80:773-781(2014).
RN [16]
RP ALTERNATIVE SPLICING, MISCELLANEOUS, SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=28522536; DOI=10.1126/science.aah6895;
RA Yang P., Wang Y., Hoang D., Tinkham M., Patel A., Sun M.A., Wolf G.,
RA Baker M., Chien H.C., Lai K.N., Cheng X., Shen C.J., Macfarlan T.S.;
RT "A placental growth factor is silenced in mouse embryos by the zinc finger
RT protein ZFP568.";
RL Science 356:757-759(2017).
RN [17]
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=29440408; DOI=10.1073/pnas.1719278115;
RA Younis S., Schoenke M., Massart J., Hjortebjerg R., Sundstroem E.,
RA Gustafson U., Bjoernholm M., Krook A., Frystyk J., Zierath J.R.,
RA Andersson L.;
RT "The ZBED6-IGF2 axis has a major effect on growth of skeletal muscle and
RT internal organs in placental mammals.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:E2048-E2057(2018).
RN [18]
RP FUNCTION.
RX PubMed=32557799; DOI=10.1096/fj.201901321r;
RA Younis S., Naboulsi R., Wang X., Cao X., Larsson M., Sargsyan E.,
RA Bergsten P., Welsh N., Andersson L.;
RT "The importance of the ZBED6-IGF2 axis for metabolic regulation in mouse
RT myoblast cells.";
RL FASEB J. 34:10250-10266(2020).
CC -!- FUNCTION: The insulin-like growth factors possess growth-promoting
CC activity (PubMed:29440408). Major fetal growth hormone in mammals.
CC Plays a key role in regulating fetoplacental development (Probable)
CC (PubMed:2330056, PubMed:12087403). IGF2 is influenced by placental
CC lactogen (Probable). Also involved in tissue differentiation
CC (Probable). In adults, involved in glucose metabolism in adipose
CC tissue, skeletal muscle and liver (Probable). Acts as a ligand for
CC integrin which is required for IGF2 signaling (By similarity).
CC Positively regulates myogenic transcription factor MYOD1 function by
CC facilitating the recruitment of transcriptional coactivators, thereby
CC controlling muscle terminal differentiation (PubMed:16901893). Inhibits
CC myoblast differentiation and modulates metabolism via increasing the
CC mitochondrial respiration rate (PubMed:32557799).
CC {ECO:0000250|UniProtKB:P01344, ECO:0000269|PubMed:12087403,
CC ECO:0000269|PubMed:16901893, ECO:0000269|PubMed:2330056,
CC ECO:0000269|PubMed:29440408, ECO:0000269|PubMed:32557799,
CC ECO:0000305|PubMed:24593700, ECO:0000305|PubMed:28522536}.
CC -!- FUNCTION: Preptin undergoes glucose-mediated co-secretion with insulin,
CC and acts as 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:0000269|PubMed:16912056}.
CC -!- SUBUNIT: Interacts with MYORG; this interaction is required for IGF2
CC secretion (PubMed:19706595). Interacts with integrins ITGAV:ITGB3 and
CC ITGA6:ITGB4; integrin-binding is required for IGF2 signaling (By
CC similarity). {ECO:0000250|UniProtKB:P01344,
CC ECO:0000269|PubMed:19706595}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28522536}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage; Named isoforms=2;
CC Name=1;
CC IsoId=P09535-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P09535-2; Sequence=VSP_059113;
CC -!- TISSUE SPECIFICITY: Expressed in the heart, blood serum, kidney and
CC skeletal muscle including the tibialis anterior muscle.
CC {ECO:0000269|PubMed:29440408}.
CC -!- DEVELOPMENTAL STAGE: At 8 dpc, 9.5 dpc and 16.5 dpc, transcripts from
CC parental allele are detected in embryonic and extraembryonic tissues
CC (PubMed:28522536, PubMed:1997210). At 16.5 dpc, transcripts from
CC parental and maternal alleles are detected only in the choroid plexus
CC and the leptomeninges (PubMed:1997210). Expressed in fetal muscle and
CC brain tissue at 12.5 dpc (PubMed:29440408). Low levels of expression
CC during myoblast proliferation. Levels rise rapidly during myoblast
CC differentiation and then decrease. {ECO:0000269|PubMed:1997210,
CC ECO:0000269|PubMed:28522536, ECO:0000269|PubMed:29440408}.
CC -!- DEVELOPMENTAL STAGE: [Isoform 2]: Predominant isoform expressed in
CC fetal muscle tissues at 12.5 dpc. {ECO:0000269|PubMed:29440408}.
CC -!- PTM: Proteolytically processed by PCSK4, proIGF2 is cleaved at Arg-128
CC and Arg-92 to generate big-IGF2 and mature IGF2.
CC {ECO:0000250|UniProtKB:P01344}.
CC -!- DISRUPTION PHENOTYPE: Heterozygous animals are smaller than their wild
CC type littermates but appear normal, reach sexual maturity and are
CC fertile (PubMed:2330056). Transmission of this mutation through the
CC male germline results in heterozygous progeny that are growth
CC deficient. In contrast, when the disrupted gene is transmitted
CC maternally, the heterozygous offspring are phenotypically normal.
CC Homozygous mutants are indistinguishable in appearance from growth-
CC deficient heterozygous siblings (PubMed:1997210). Mutant animals for
CC transcript P0 specifically show a reduced growth of the placenta
CC followed by fetal growth restriction, passive permeability for
CC nutrients of the placenta is decreased (PubMed:12087403).
CC {ECO:0000269|PubMed:12087403, ECO:0000269|PubMed:1997210,
CC ECO:0000269|PubMed:2330056}.
CC -!- MISCELLANEOUS: The IGF2 locus is imprinted. Paternal inherited gene is
CC expressed, while the maternal inherited gene is imprinted, hence
CC silenced (PubMed:1997210). It is differentially regulated in the
CC placenta and fetus, transcribed from 3 promoters P1, P2 and P3 in both
CC fetus and placenta and additionally from a fourth placental-specific
CC promoter, P0 (Probable). {ECO:0000269|PubMed:1997210,
CC ECO:0000305|PubMed:28522536}.
CC -!- MISCELLANEOUS: [Isoform 1]: Product of 4 different transcripts
CC regulated by 4 different promoters, denominated P0, P1, P2 and P3.
CC {ECO:0000305|PubMed:28522536}.
CC -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR EMBL; M14951; AAA37683.1; -; mRNA.
DR EMBL; M36332; AAA37926.1; -; Genomic_DNA.
DR EMBL; M36331; AAA37926.1; JOINED; Genomic_DNA.
DR EMBL; U71085; AAC53516.1; -; Genomic_DNA.
DR EMBL; M24633; AAA37923.1; -; Genomic_DNA.
DR EMBL; X71921; CAA50737.1; -; Genomic_DNA.
DR EMBL; X71922; CAA50738.1; -; Genomic_DNA.
DR EMBL; AC013548; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC053489; AAH53489.1; -; mRNA.
DR CCDS; CCDS22033.2; -. [P09535-2]
DR CCDS; CCDS52458.1; -. [P09535-1]
DR PIR; A24913; A24913.
DR RefSeq; NP_001116208.1; NM_001122736.2. [P09535-1]
DR RefSeq; NP_001116209.1; NM_001122737.2. [P09535-1]
DR RefSeq; NP_001302417.1; NM_001315488.1. [P09535-1]
DR RefSeq; NP_001302418.1; NM_001315489.1. [P09535-1]
DR RefSeq; NP_034644.2; NM_010514.3. [P09535-2]
DR RefSeq; XP_006508550.1; XM_006508487.1. [P09535-1]
DR AlphaFoldDB; P09535; -.
DR SMR; P09535; -.
DR BioGRID; 200549; 3.
DR STRING; 10090.ENSMUSP00000101556; -.
DR iPTMnet; P09535; -.
DR PhosphoSitePlus; P09535; -.
DR CPTAC; non-CPTAC-3521; -.
DR MaxQB; P09535; -.
DR PaxDb; P09535; -.
DR PeptideAtlas; P09535; -.
DR PRIDE; P09535; -.
DR ProteomicsDB; 269532; -. [P09535-1]
DR ProteomicsDB; 269533; -. [P09535-2]
DR ABCD; P09535; 1 sequenced antibody.
DR Antibodypedia; 1027; 606 antibodies from 40 providers.
DR DNASU; 16002; -.
DR Ensembl; ENSMUST00000000033; ENSMUSP00000000033; ENSMUSG00000048583. [P09535-1]
DR Ensembl; ENSMUST00000097936; ENSMUSP00000095549; ENSMUSG00000048583. [P09535-1]
DR Ensembl; ENSMUST00000105935; ENSMUSP00000101555; ENSMUSG00000048583. [P09535-1]
DR Ensembl; ENSMUST00000105936; ENSMUSP00000101556; ENSMUSG00000048583. [P09535-1]
DR Ensembl; ENSMUST00000121128; ENSMUSP00000114076; ENSMUSG00000048583. [P09535-2]
DR GeneID; 16002; -.
DR KEGG; mmu:16002; -.
DR UCSC; uc009kod.2; mouse. [P09535-1]
DR CTD; 3481; -.
DR MGI; MGI:96434; Igf2.
DR VEuPathDB; HostDB:ENSMUSG00000048583; -.
DR eggNOG; ENOG502S0I0; Eukaryota.
DR GeneTree; ENSGT00940000160745; -.
DR HOGENOM; CLU_092464_1_0_1; -.
DR InParanoid; P09535; -.
DR OMA; PSHAKYS; -.
DR OrthoDB; 1644517at2759; -.
DR PhylomeDB; P09535; -.
DR TreeFam; TF332820; -.
DR Reactome; R-MMU-114608; Platelet degranulation.
DR Reactome; R-MMU-2404192; Signaling by Type 1 Insulin-like Growth Factor 1 Receptor (IGF1R).
DR Reactome; R-MMU-2428928; IRS-related events triggered by IGF1R.
DR Reactome; R-MMU-2428933; SHC-related events triggered by IGF1R.
DR Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR BioGRID-ORCS; 16002; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Igf2; mouse.
DR PRO; PR:P09535; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P09535; protein.
DR Bgee; ENSMUSG00000048583; Expressed in extraembryonic membrane and 176 other tissues.
DR ExpressionAtlas; P09535; baseline and differential.
DR Genevisible; P09535; MM.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0008083; F:growth factor activity; ISO:MGI.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR GO; GO:0005158; F:insulin receptor binding; ISO:MGI.
DR GO; GO:0005159; F:insulin-like growth factor receptor binding; IPI:MGI.
DR GO; GO:0005178; F:integrin binding; ISS:UniProtKB.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; IMP:BHF-UCL.
DR GO; GO:0048018; F:receptor ligand activity; IMP:BHF-UCL.
DR GO; GO:0009887; P:animal organ morphogenesis; IMP:MGI.
DR GO; GO:0001892; P:embryonic placenta development; IMP:UniProtKB.
DR GO; GO:0060669; P:embryonic placenta morphogenesis; IMP:UniProtKB.
DR GO; GO:0031017; P:exocrine pancreas development; IMP:MGI.
DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0001701; P:in utero embryonic development; IMP:UniProtKB.
DR GO; GO:0038028; P:insulin receptor signaling pathway via phosphatidylinositol 3-kinase; IMP:BHF-UCL.
DR GO; GO:0007613; P:memory; ISO:MGI.
DR GO; GO:0051148; P:negative regulation of muscle cell differentiation; IMP:UniProtKB.
DR GO; GO:0045953; P:negative regulation of natural killer cell mediated cytotoxicity; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0001649; P:osteoblast differentiation; IEP:BHF-UCL.
DR GO; GO:0042104; P:positive regulation of activated T cell proliferation; ISO:MGI.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISO:MGI.
DR GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; ISO:MGI.
DR GO; GO:0043085; P:positive regulation of catalytic activity; IMP:BHF-UCL.
DR GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:2000467; P:positive regulation of glycogen (starch) synthase activity; IMP:BHF-UCL.
DR GO; GO:0045725; P:positive regulation of glycogen biosynthetic process; IMP:BHF-UCL.
DR GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; IMP:BHF-UCL.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:MGI.
DR GO; GO:0045840; P:positive regulation of mitotic nuclear division; ISO:MGI.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IMP:MGI.
DR GO; GO:0046622; P:positive regulation of organ growth; IMP:UniProtKB.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IMP:BHF-UCL.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:BHF-UCL.
DR GO; GO:0048633; P:positive regulation of skeletal muscle tissue growth; IMP:UniProtKB.
DR GO; GO:0090031; P:positive regulation of steroid hormone biosynthetic process; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:1905564; P:positive regulation of vascular endothelial cell proliferation; ISO:MGI.
DR GO; GO:0031056; P:regulation of histone modification; IMP:UniProtKB.
DR GO; GO:0051147; P:regulation of muscle cell differentiation; IMP:UniProtKB.
DR GO; GO:0035094; P:response to nicotine; ISO:MGI.
DR GO; GO:0014070; P:response to organic cyclic compound; ISO:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; ISO:MGI.
DR GO; GO:0060720; P:spongiotrophoblast cell proliferation; IMP:CACAO.
DR GO; GO:0051146; P:striated muscle cell differentiation; IGI:MGI.
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 Pfam; PF08365; IGF2_C; 1.
DR Pfam; PF00049; Insulin; 1.
DR PRINTS; PR02002; INSLNLIKEGF.
DR PRINTS; PR02006; INSLNLIKEGF2.
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 Alternative promoter usage; Carbohydrate metabolism;
KW Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; Glucose metabolism; Growth factor; Hormone; Mitogen;
KW Osteogenesis; Reference proteome; Secreted; Signal.
FT SIGNAL 1..24
FT CHAIN 25..91
FT /note="Insulin-like growth factor II"
FT /id="PRO_0000015720"
FT PROPEP 92..180
FT /note="E peptide"
FT /id="PRO_0000015721"
FT PEPTIDE 93..126
FT /note="Preptin"
FT /id="PRO_0000370377"
FT REGION 25..52
FT /note="B"
FT REGION 53..64
FT /note="C"
FT REGION 65..85
FT /note="A"
FT REGION 86..91
FT /note="D"
FT REGION 157..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 48
FT /note="Important for interaction with integrin"
FT /evidence="ECO:0000250|UniProtKB:P01344"
FT SITE 58
FT /note="Important for interaction with integrin"
FT /evidence="ECO:0000250|UniProtKB:P01344"
FT SITE 61
FT /note="Important for interaction with integrin"
FT /evidence="ECO:0000250|UniProtKB:P01344"
FT SITE 62
FT /note="Important for interaction with integrin"
FT /evidence="ECO:0000250|UniProtKB:P01344"
FT DISULFID 33..71
FT /evidence="ECO:0000250"
FT DISULFID 45..84
FT /evidence="ECO:0000250"
FT DISULFID 70..75
FT /evidence="ECO:0000250"
FT VAR_SEQ 1
FT /note="M -> MGGSVAGFQVPM (in isoform 2)"
FT /id="VSP_059113"
SQ SEQUENCE 180 AA; 20030 MW; 01730F8856EE6D7B CRC64;
MGIPVGKSML VLLISLAFAL CCIAAYGPGE TLCGGELVDT LQFVCSDRGF YFSRPSSRAN
RRSRGIVEEC CFRSCDLALL ETYCATPAKS ERDVSTSQAV LPDDFPRYPV GKFFQYDTWR
QSAGRLRRGL PALLRARRGR MLAKELKEFR EAKRHRPLIV LPPKDPAHGG ASSEMSSNHQ
