IGF1_RAT
ID IGF1_RAT Reviewed; 153 AA.
AC P08025; P08024;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 3.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Insulin-like growth factor I;
DE Short=IGF-I;
DE AltName: Full=Somatomedin;
DE Flags: Precursor;
GN Name=Igf1; Synonyms=Igf-1;
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] (ISOFORMS IGF-IA AND IGF-IB).
RC TISSUE=Liver;
RX PubMed=3034909; DOI=10.1016/s0021-9258(18)47652-1;
RA Shimatsu A., Rotwein P.;
RT "Mosaic evolution of the insulin-like growth factors. Organization,
RT sequence, and expression of the rat insulin-like growth factor I gene.";
RL J. Biol. Chem. 262:7894-7900(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM IGF-IA).
RC TISSUE=Testis;
RX PubMed=3652906; DOI=10.1089/dna.1987.6.325;
RA Casella S.J., Smith E.P., van Wyk J.J., Joseph D.R., Hynes M.A., Hoyt E.C.,
RA Lund P.K.;
RT "Isolation of rat testis cDNAs encoding an insulin-like growth factor I
RT precursor.";
RL DNA 6:325-330(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM IGF-IA).
RX PubMed=3453891; DOI=10.1210/mend-1-3-243;
RA Roberts C.T. Jr., Lasky S.R., Lowe W.L. Jr., Seaman W.T., LeRoith D.;
RT "Molecular cloning of rat insulin-like growth factor I complementary
RT deoxyribonucleic acids: differential messenger ribonucleic acid processing
RT and regulation by growth hormone in extrahepatic tissues.";
RL Mol. Endocrinol. 1:243-248(1987).
RN [4]
RP NUCLEOTIDE SEQUENCE (ISOFORM IGF-IB).
RX PubMed=3658684; DOI=10.1093/nar/15.17.7196;
RA Shimatsu A., Rotwein P.;
RT "Sequence of two rat insulin-like growth factor I mRNAs differing within
RT the 5' untranslated region.";
RL Nucleic Acids Res. 15:7196-7196(1987).
RN [5]
RP NUCLEOTIDE SEQUENCE (ISOFORM IGF-IA).
RX PubMed=1368571; DOI=10.1271/bbb1961.54.1599;
RA Kato H., Okoshi A., Miura Y., Noguchi T.;
RT "A new cDNA clone relating to larger molecular species of rat insulin-like
RT growth factor-I mRNA.";
RL Agric. Biol. Chem. 54:1599-1601(1990).
RN [6]
RP NUCLEOTIDE SEQUENCE OF 46-153 (ISOFORM IGF-IA).
RX PubMed=3595538; DOI=10.1210/endo-121-2-684;
RA Murphy L.J., Bell G.I., Duckworth M.L., Friesen H.G.;
RT "Identification, characterization, and regulation of a rat complementary
RT deoxyribonucleic acid which encodes insulin-like growth factor-I.";
RL Endocrinology 121:684-691(1987).
RN [7]
RP PROTEIN SEQUENCE OF 49-118.
RX PubMed=2538424; DOI=10.1016/s0021-9258(18)83592-x;
RA Tamura K., Kobayashi M., Ishii Y., Tamura T., Hashimoto K., Nakamura S.,
RA Niwa M., Zapf J.;
RT "Primary structure of rat insulin-like growth factor-I and its biological
RT activities.";
RL J. Biol. Chem. 264:5616-5621(1989).
CC -!- FUNCTION: The insulin-like growth factors, isolated from plasma, are
CC structurally and functionally related to insulin but have a much higher
CC growth-promoting activity. May be a physiological regulator of [1-14C]-
CC 2-deoxy-D-glucose (2DG) transport and glycogen synthesis in
CC osteoblasts. Stimulates glucose transport in bone-derived osteoblastic
CC (PyMS) cells and is effective at much lower concentrations than
CC insulin, not only regarding glycogen and DNA synthesis but also with
CC regard to enhancing glucose uptake. May play a role in synapse
CC maturation. Ca(2+)-dependent exocytosis of IGF1 is required for sensory
CC perception of smell in the olfactory bulb. Acts as a ligand for IGF1R.
CC Binds to the alpha subunit of IGF1R, leading to the activation of the
CC intrinsic tyrosine kinase activity which autophosphorylates tyrosine
CC residues in the beta subunit thus initiatiating a cascade of down-
CC stream signaling events leading to activation of the PI3K-AKT/PKB and
CC the Ras-MAPK pathways. Binds to integrins ITGAV:ITGB3 and ITGA6:ITGB4.
CC Its binding to integrins and subsequent ternary complex formation with
CC integrins and IGFR1 are essential for IGF1 signaling. Induces the
CC phosphorylation and activation of IGFR1, MAPK3/ERK1, MAPK1/ERK2 and
CC AKT1 (By similarity). {ECO:0000250|UniProtKB:P05017,
CC ECO:0000250|UniProtKB:P05019}.
CC -!- SUBUNIT: Forms a ternary complex with IGFR1 and ITGAV:ITGB3. Forms a
CC ternary complex with IGFR1 and ITGA6:ITGB4.
CC {ECO:0000250|UniProtKB:P05019}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P05017}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=IGF-IA;
CC IsoId=P08025-1; Sequence=Displayed;
CC Name=IGF-IB;
CC IsoId=P08025-2; Sequence=VSP_012166;
CC -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA41385.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAA41386.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAA41387.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M15651; AAA41215.1; -; Genomic_DNA.
DR EMBL; M15647; AAA41215.1; JOINED; Genomic_DNA.
DR EMBL; M15648; AAA41215.1; JOINED; Genomic_DNA.
DR EMBL; M15649; AAA41215.1; JOINED; Genomic_DNA.
DR EMBL; M15650; AAA41214.1; -; Genomic_DNA.
DR EMBL; M15647; AAA41214.1; JOINED; Genomic_DNA.
DR EMBL; M15648; AAA41214.1; JOINED; Genomic_DNA.
DR EMBL; M15649; AAA41214.1; JOINED; Genomic_DNA.
DR EMBL; M17335; AAA41386.1; ALT_INIT; mRNA.
DR EMBL; M15480; AAA41385.1; ALT_INIT; mRNA.
DR EMBL; M15481; AAA41387.1; ALT_INIT; mRNA.
DR EMBL; X06107; CAA29480.1; -; mRNA.
DR EMBL; X06043; CAA29436.1; -; mRNA.
DR PIR; A27804; A27804.
DR PIR; A40912; A40912.
DR PIR; B27804; B27804.
DR RefSeq; NP_001075946.2; NM_001082477.2.
DR RefSeq; NP_001075947.1; NM_001082478.1.
DR RefSeq; NP_001075948.1; NM_001082479.1. [P08025-1]
DR RefSeq; XP_006241253.1; XM_006241191.2.
DR RefSeq; XP_006241254.1; XM_006241192.1.
DR RefSeq; XP_006241255.1; XM_006241193.3. [P08025-1]
DR AlphaFoldDB; P08025; -.
DR SMR; P08025; -.
DR STRING; 10116.ENSRNOP00000005995; -.
DR iPTMnet; P08025; -.
DR PaxDb; P08025; -.
DR ABCD; P08025; 1 sequenced antibody.
DR Ensembl; ENSRNOT00000118307; ENSRNOP00000097781; ENSRNOG00000004517. [P08025-1]
DR GeneID; 24482; -.
DR KEGG; rno:24482; -.
DR CTD; 3479; -.
DR RGD; 2868; Igf1.
DR eggNOG; ENOG502RCAB; Eukaryota.
DR GeneTree; ENSGT00940000159081; -.
DR HOGENOM; CLU_123939_0_0_1; -.
DR InParanoid; P08025; -.
DR OMA; FFYLALC; -.
DR OrthoDB; 1644517at2759; -.
DR PhylomeDB; P08025; -.
DR TreeFam; TF332820; -.
DR Reactome; R-RNO-114608; Platelet degranulation.
DR Reactome; R-RNO-2404192; Signaling by Type 1 Insulin-like Growth Factor 1 Receptor (IGF1R).
DR Reactome; R-RNO-2428928; IRS-related events triggered by IGF1R.
DR Reactome; R-RNO-2428933; SHC-related events triggered by IGF1R.
DR Reactome; R-RNO-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-RNO-422085; Synthesis, secretion, and deacylation of Ghrelin.
DR PRO; PR:P08025; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000004517; Expressed in liver and 19 other tissues.
DR ExpressionAtlas; P08025; baseline and differential.
DR Genevisible; P08025; RN.
DR GO; GO:0035867; C:alphav-beta3 integrin-IGF-1-IGF1R complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0070382; C:exocytic vesicle; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0042567; C:insulin-like growth factor ternary complex; ISO:RGD.
DR GO; GO:0005614; C:interstitial matrix; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0031091; C:platelet alpha granule; IDA:RGD.
DR GO; GO:0008083; F:growth factor activity; TAS:RGD.
DR GO; GO:0005179; F:hormone activity; IDA:RGD.
DR GO; GO:0005158; F:insulin receptor binding; ISO:RGD.
DR GO; GO:0005159; F:insulin-like growth factor receptor binding; IDA:RGD.
DR GO; GO:0005178; F:integrin binding; ISO:RGD.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; IDA:BHF-UCL.
DR GO; GO:0005496; F:steroid binding; IDA:RGD.
DR GO; GO:0032148; P:activation of protein kinase B activity; ISO:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0001974; P:blood vessel remodeling; ISO:RGD.
DR GO; GO:0060348; P:bone development; IEP:RGD.
DR GO; GO:0035630; P:bone mineralization involved in bone maturation; ISO:RGD.
DR GO; GO:0048754; P:branching morphogenesis of an epithelial tube; ISO:RGD.
DR GO; GO:0003230; P:cardiac atrium development; IEP:RGD.
DR GO; GO:0001775; P:cell activation; ISO:RGD.
DR GO; GO:0048468; P:cell development; ISO:RGD.
DR GO; GO:0008283; P:cell population proliferation; ISO:RGD.
DR GO; GO:1904646; P:cellular response to amyloid-beta; ISO:RGD.
DR GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEP:RGD.
DR GO; GO:0071257; P:cellular response to electrical stimulus; IEP:RGD.
DR GO; GO:0071392; P:cellular response to estradiol stimulus; IEP:RGD.
DR GO; GO:0071333; P:cellular response to glucose stimulus; ISO:RGD.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IEP:RGD.
DR GO; GO:1990314; P:cellular response to insulin-like growth factor stimulus; ISO:RGD.
DR GO; GO:0071316; P:cellular response to nicotine; IEP:RGD.
DR GO; GO:0071393; P:cellular response to progesterone stimulus; IEP:RGD.
DR GO; GO:1904017; P:cellular response to Thyroglobulin triiodothyronine; IEP:RGD.
DR GO; GO:0050650; P:chondroitin sulfate proteoglycan biosynthetic process; ISO:RGD.
DR GO; GO:0007623; P:circadian rhythm; ISO:RGD.
DR GO; GO:0060363; P:cranial suture morphogenesis; IEP:RGD.
DR GO; GO:0050974; P:detection of mechanical stimulus involved in sensory perception; IMP:RGD.
DR GO; GO:0070371; P:ERK1 and ERK2 cascade; ISO:RGD.
DR GO; GO:0031017; P:exocrine pancreas development; ISO:RGD.
DR GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; ISO:RGD.
DR GO; GO:0007565; P:female pregnancy; IEP:RGD.
DR GO; GO:0010001; P:glial cell differentiation; ISO:RGD.
DR GO; GO:0048839; P:inner ear development; ISO:RGD.
DR GO; GO:0048009; P:insulin-like growth factor receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0048286; P:lung alveolus development; ISO:RGD.
DR GO; GO:0030324; P:lung development; ISO:RGD.
DR GO; GO:0060463; P:lung lobe morphogenesis; ISO:RGD.
DR GO; GO:0060426; P:lung vasculature development; ISO:RGD.
DR GO; GO:0030879; P:mammary gland development; ISO:RGD.
DR GO; GO:0007613; P:memory; IMP:RGD.
DR GO; GO:0035264; P:multicellular organism growth; ISO:RGD.
DR GO; GO:0014896; P:muscle hypertrophy; ISO:RGD.
DR GO; GO:0045445; P:myoblast differentiation; ISO:RGD.
DR GO; GO:0051450; P:myoblast proliferation; ISO:RGD.
DR GO; GO:0014904; P:myotube cell development; ISO:RGD.
DR GO; GO:1902430; P:negative regulation of amyloid-beta formation; ISO:RGD.
DR GO; GO:0060766; P:negative regulation of androgen receptor signaling pathway; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:RGD.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:RGD.
DR GO; GO:1904193; P:negative regulation of cholangiocyte apoptotic process; IMP:RGD.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:BHF-UCL.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISO:RGD.
DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IDA:BHF-UCL.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR GO; GO:0002683; P:negative regulation of immune system process; IMP:RGD.
DR GO; GO:0032691; P:negative regulation of interleukin-1 beta production; ISO:RGD.
DR GO; GO:0010656; P:negative regulation of muscle cell apoptotic process; IMP:RGD.
DR GO; GO:0150079; P:negative regulation of neuroinflammatory response; ISO:RGD.
DR GO; GO:1901215; P:negative regulation of neuron death; IDA:RGD.
DR GO; GO:1900142; P:negative regulation of oligodendrocyte apoptotic process; IDA:RGD.
DR GO; GO:0060283; P:negative regulation of oocyte development; ISO:RGD.
DR GO; GO:0050732; P:negative regulation of peptidyl-tyrosine phosphorylation; ISO:RGD.
DR GO; GO:0090201; P:negative regulation of release of cytochrome c from mitochondria; ISS:UniProtKB.
DR GO; GO:0034392; P:negative regulation of smooth muscle cell apoptotic process; ISO:RGD.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; ISO:RGD.
DR GO; GO:1905460; P:negative regulation of vascular associated smooth muscle cell apoptotic process; ISO:RGD.
DR GO; GO:0007399; P:nervous system development; ISO:RGD.
DR GO; GO:0001649; P:osteoblast differentiation; ISO:RGD.
DR GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; ISO:RGD.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; ISO:RGD.
DR GO; GO:0042104; P:positive regulation of activated T cell proliferation; ISO:RGD.
DR GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; IGI:BHF-UCL.
DR GO; GO:0070886; P:positive regulation of calcineurin-NFAT signaling cascade; ISO:RGD.
DR GO; GO:0010613; P:positive regulation of cardiac muscle hypertrophy; ISO:RGD.
DR GO; GO:0030307; P:positive regulation of cell growth; IDA:RGD.
DR GO; GO:0061051; P:positive regulation of cell growth involved in cardiac muscle cell development; ISO:RGD.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0021940; P:positive regulation of cerebellar granule cell precursor proliferation; ISO:RGD.
DR GO; GO:0043388; P:positive regulation of DNA binding; ISO:RGD.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; ISO:RGD.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:RGD.
DR GO; GO:0045600; P:positive regulation of fat cell differentiation; IDA:RGD.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0060252; P:positive regulation of glial cell proliferation; IDA:RGD.
DR GO; GO:0046326; P:positive regulation of glucose import; ISS:UniProtKB.
DR GO; GO:0045725; P:positive regulation of glycogen biosynthetic process; ISS:UniProtKB.
DR GO; GO:0045821; P:positive regulation of glycolytic process; ISO:RGD.
DR GO; GO:0010560; P:positive regulation of glycoprotein biosynthetic process; ISO:RGD.
DR GO; GO:0043568; P:positive regulation of insulin-like growth factor receptor signaling pathway; ISO:RGD.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:RGD.
DR GO; GO:0045840; P:positive regulation of mitotic nuclear division; ISO:RGD.
DR GO; GO:0031643; P:positive regulation of myelination; ISO:RGD.
DR GO; GO:2000288; P:positive regulation of myoblast proliferation; ISO:RGD.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IDA:RGD.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:BHF-UCL.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IDA:BHF-UCL.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:RGD.
DR GO; GO:0050714; P:positive regulation of protein secretion; ISO:RGD.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IDA:BHF-UCL.
DR GO; GO:0046579; P:positive regulation of Ras protein signal transduction; ISO:RGD.
DR GO; GO:0014911; P:positive regulation of smooth muscle cell migration; ISO:RGD.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISO:RGD.
DR GO; GO:0090031; P:positive regulation of steroid hormone biosynthetic process; IDA:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:2000679; P:positive regulation of transcription regulatory region DNA binding; ISO:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:1904075; P:positive regulation of trophectodermal cell proliferation; ISO:RGD.
DR GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; ISO:RGD.
DR GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; ISO:RGD.
DR GO; GO:1905564; P:positive regulation of vascular endothelial cell proliferation; IGI:BHF-UCL.
DR GO; GO:0060527; P:prostate epithelial cord arborization involved in prostate glandular acinus morphogenesis; ISO:RGD.
DR GO; GO:0060740; P:prostate gland epithelium morphogenesis; ISO:RGD.
DR GO; GO:0060736; P:prostate gland growth; ISO:RGD.
DR GO; GO:0060741; P:prostate gland stromal morphogenesis; ISO:RGD.
DR GO; GO:0043491; P:protein kinase B signaling; ISO:RGD.
DR GO; GO:0050821; P:protein stabilization; ISO:RGD.
DR GO; GO:0030166; P:proteoglycan biosynthetic process; ISO:RGD.
DR GO; GO:0051924; P:regulation of calcium ion transport; IDA:RGD.
DR GO; GO:0042127; P:regulation of cell population proliferation; IDA:RGD.
DR GO; GO:0032878; P:regulation of establishment or maintenance of cell polarity; ISO:RGD.
DR GO; GO:0010468; P:regulation of gene expression; ISO:RGD.
DR GO; GO:0040014; P:regulation of multicellular organism growth; ISO:RGD.
DR GO; GO:0045428; P:regulation of nitric oxide biosynthetic process; ISO:RGD.
DR GO; GO:0051246; P:regulation of protein metabolic process; ISO:RGD.
DR GO; GO:0001932; P:regulation of protein phosphorylation; ISO:RGD.
DR GO; GO:0006417; P:regulation of translation; IMP:RGD.
DR GO; GO:0014823; P:response to activity; IEP:RGD.
DR GO; GO:0031000; P:response to caffeine; IEP:RGD.
DR GO; GO:0070849; P:response to epidermal growth factor; IEP:RGD.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:0045471; P:response to ethanol; IDA:RGD.
DR GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
DR GO; GO:0060416; P:response to growth hormone; IEP:RGD.
DR GO; GO:0009408; P:response to heat; ISO:RGD.
DR GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0009612; P:response to mechanical stimulus; IEP:RGD.
DR GO; GO:0035094; P:response to nicotine; IEP:RGD.
DR GO; GO:0007584; P:response to nutrient; IEP:RGD.
DR GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0010033; P:response to organic substance; IEP:RGD.
DR GO; GO:0042594; P:response to starvation; IEP:RGD.
DR GO; GO:0048545; P:response to steroid hormone; IEP:RGD.
DR GO; GO:0097066; P:response to thyroid hormone; IEP:RGD.
DR GO; GO:0014834; P:skeletal muscle satellite cell maintenance involved in skeletal muscle regeneration; ISO:RGD.
DR GO; GO:0060509; P:type I pneumocyte differentiation; ISO:RGD.
DR GO; GO:0060510; P:type II pneumocyte differentiation; ISO:RGD.
DR GO; GO:0030104; P:water homeostasis; ISO:RGD.
DR GO; GO:0042060; P:wound healing; ISO:RGD.
DR InterPro; IPR022341; IGF-I.
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; PF00049; Insulin; 2.
DR PRINTS; PR02002; INSLNLIKEGF.
DR PRINTS; PR02005; INSLNLIKEGF1.
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 splicing; Direct protein sequencing; Disulfide bond;
KW Growth factor; Reference proteome; Secreted; Signal.
FT SIGNAL 1..?
FT /evidence="ECO:0000255"
FT PROPEP ?..48
FT /evidence="ECO:0000269|PubMed:2538424"
FT /id="PRO_0000015681"
FT CHAIN 49..118
FT /note="Insulin-like growth factor I"
FT /id="PRO_0000015682"
FT PROPEP 119..153
FT /note="E peptide"
FT /id="PRO_0000015683"
FT REGION 49..77
FT /note="B"
FT REGION 78..89
FT /note="C"
FT REGION 90..110
FT /note="A"
FT REGION 111..118
FT /note="D"
FT REGION 119..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 54..96
FT /evidence="ECO:0000250"
FT DISULFID 66..109
FT /evidence="ECO:0000250"
FT DISULFID 95..100
FT /evidence="ECO:0000250"
FT VAR_SEQ 135..153
FT /note="EVHLKNTSRGSAGNKTYRM -> SQPLSTHKKRKLQRRRKGSTLEEH (in
FT isoform IGF-IB)"
FT /evidence="ECO:0000305"
FT /id="VSP_012166"
FT CONFLICT 110..112
FT /note="APL -> VRC (in Ref. 3; AAA41385/AAA41387)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 153 AA; 17079 MW; 966F3C0FA4EB3DE7 CRC64;
MGKISSLPTQ LFKICLCDFL KIKIHIMSSS HLFYLALCLL TFTSSATAGP ETLCGAELVD
ALQFVCGPRG FYFNKPTGYG SSIRRAPQTG IVDECCFRSC DLRRLEMYCA PLKPTKSARS
IRAQRHTDMP KTQKEVHLKN TSRGSAGNKT YRM
