ID   IGF1_MOUSE              Reviewed;         153 AA.
AC   P05017; P05018; Q6LDP4; Q8C4U6;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 2.
DT   27-MAR-2024, entry version 217.
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   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 [LARGE SCALE MRNA] (ISOFORM IGF-IA).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 18-153 (ISOFORM IGF-IB).
RC   STRAIN=FVB/N; TISSUE=Liver;
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   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 27-153 (ISOFORMS IGF-IA AND IGF-IB).
RC   TISSUE=Liver;
RX   PubMed=3774549; DOI=10.1093/nar/14.20.7873;
RA   Bell G.I., Stempien M.M., Fong N.M., Rall L.B.;
RT   "Sequences of liver cDNAs encoding two different mouse insulin-like growth
RT   factor I precursors.";
RL   Nucleic Acids Res. 14:7873-7882(1986).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 75-134.
RX   PubMed=2474537; DOI=10.1016/s0021-9258(18)80073-4;
RA   Tollefsen S.E., Lajara R., McCusker R.H., Clemmons D.R., Rotwein P.;
RT   "Insulin-like growth factors (IGF) in muscle development. Expression of
RT   IGF-I, the IGF-I receptor, and an IGF binding protein during myoblast
RT   differentiation.";
RL   J. Biol. Chem. 264:13810-13817(1989).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 75-134.
RX   PubMed=3467309; DOI=10.1073/pnas.83.24.9343;
RA   Mathews L.S., Norstedt G., Palmiter R.D.;
RT   "Regulation of insulin-like growth factor I gene expression by growth
RT   hormone.";
RL   Proc. Natl. Acad. Sci. U.S.A. 83:9343-9347(1986).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
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).
RN   [7]
RP   INDUCTION.
RX   PubMed=20685873; DOI=10.1210/en.2010-0407;
RA   Kawai M., Delany A.M., Green C.B., Adamo M.L., Rosen C.J.;
RT   "Nocturnin suppresses igf1 expression in bone by targeting the 3'
RT   untranslated region of igf1 mRNA.";
RL   Endocrinology 151:4861-4870(2010).
RN   [8]
RP   INTERACTION WITH SH2D3C.
RX   PubMed=20881139; DOI=10.1523/jneurosci.3289-10.2010;
RA   Wang L., Vervoort V., Wallez Y., Core N., Cremer H., Pasquale E.B.;
RT   "The SRC homology 2 domain protein Shep1 plays an important role in the
RT   penetration of olfactory sensory axons into the forebrain.";
RL   J. Neurosci. 30:13201-13210(2010).
RN   [9]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=21496647; DOI=10.1016/j.cell.2011.03.034;
RA   Cao P., Maximov A., Suedhof T.C.;
RT   "Activity-dependent IGF-1 exocytosis is controlled by the Ca(2+)-sensor
RT   synaptotagmin-10.";
RL   Cell 145:300-311(2011).
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 (By similarity). Ca(2+)-dependent exocytosis of IGF1 is
CC       required for sensory perception of smell in the olfactory bulb
CC       (PubMed:21496647). Acts as a ligand for IGF1R. Binds to the alpha
CC       subunit of IGF1R, leading to the activation of the intrinsic tyrosine
CC       kinase activity which autophosphorylates tyrosine residues in the beta
CC       subunit thus initiating a cascade of down-stream signaling events
CC       leading to activation of the PI3K-AKT/PKB and the Ras-MAPK pathways.
CC       Binds to integrins ITGAV:ITGB3 and ITGA6:ITGB4. Its binding to
CC       integrins and subsequent ternary complex formation with integrins and
CC       IGFR1 are essential for IGF1 signaling. Induces the phosphorylation and
CC       activation of IGFR1, MAPK3/ERK1, MAPK1/ERK2 and AKT1 (By similarity).
CC       As part of the MAPK/ERK signaling pathway, acts as a negative regulator
CC       of apoptosis in cardiomyocytes via promotion of STUB1/CHIP-mediated
CC       ubiquitination and degradation of ICER-type isoforms of CREM (By
CC       similarity). {ECO:0000250|UniProtKB:P05019,
CC       ECO:0000250|UniProtKB:P08025, ECO:0000269|PubMed:21496647}.
CC   -!- SUBUNIT: Forms a ternary complex with IGFR1 and ITGAV:ITGB3. Forms a
CC       ternary complex with IGFR1 and ITGA6:ITGB4. Interacts with SH2D3C
CC       isoform 2 (PubMed:20881139). {ECO:0000250|UniProtKB:P05019,
CC       ECO:0000269|PubMed:20881139}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21496647}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=IGF-IA;
CC         IsoId=P05017-1; Sequence=Displayed;
CC       Name=IGF-IB;
CC         IsoId=P05017-2; Sequence=VSP_012165;
CC   -!- INDUCTION: Expression in the bone oscillates in a circadian manner and
CC       its expression is negatively regulated by CCRN4L/NOC.
CC       {ECO:0000269|PubMed:20685873}.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH12409.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AK081019; BAC38117.1; -; mRNA.
DR   EMBL; BC012409; AAH12409.1; ALT_INIT; mRNA.
DR   EMBL; X04480; CAA28168.1; -; mRNA.
DR   EMBL; X04482; CAA28170.1; -; mRNA.
DR   EMBL; M28139; AAA74553.1; -; Genomic_DNA.
DR   EMBL; M14983; AAA37925.1; -; Genomic_DNA.
DR   CCDS; CCDS48661.1; -. [P05017-1]
DR   PIR; A25540; A25540.
DR   RefSeq; NP_001104745.1; NM_001111275.2. [P05017-1]
DR   RefSeq; NP_001300939.1; NM_001314010.1. [P05017-1]
DR   RefSeq; NP_034642.2; NM_010512.5.
DR   AlphaFoldDB; P05017; -.
DR   SMR; P05017; -.
DR   MINT; P05017; -.
DR   STRING; 10090.ENSMUSP00000100937; -.
DR   iPTMnet; P05017; -.
DR   PhosphoSitePlus; P05017; -.
DR   CPTAC; non-CPTAC-3716; -.
DR   MaxQB; P05017; -.
DR   PaxDb; 10090-ENSMUSP00000056668; -.
DR   PeptideAtlas; P05017; -.
DR   ProteomicsDB; 267220; -. [P05017-1]
DR   ProteomicsDB; 267221; -. [P05017-2]
DR   ABCD; P05017; 1 sequenced antibody.
DR   Antibodypedia; 18040; 1619 antibodies from 42 providers.
DR   DNASU; 16000; -.
DR   Ensembl; ENSMUST00000095360.11; ENSMUSP00000093005.5; ENSMUSG00000020053.19. [P05017-1]
DR   Ensembl; ENSMUST00000122386.8; ENSMUSP00000113905.2; ENSMUSG00000020053.19. [P05017-1]
DR   GeneID; 16000; -.
DR   KEGG; mmu:16000; -.
DR   UCSC; uc007gqw.2; mouse. [P05017-1]
DR   AGR; MGI:96432; -.
DR   CTD; 3479; -.
DR   MGI; MGI:96432; Igf1.
DR   VEuPathDB; HostDB:ENSMUSG00000020053; -.
DR   eggNOG; ENOG502RCAB; Eukaryota.
DR   GeneTree; ENSGT00940000159081; -.
DR   HOGENOM; CLU_123939_0_0_1; -.
DR   InParanoid; P05017; -.
DR   OMA; NECCFQS; -.
DR   OrthoDB; 5402912at2759; -.
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   Reactome; R-MMU-422085; Synthesis, secretion, and deacylation of Ghrelin.
DR   BioGRID-ORCS; 16000; 2 hits in 77 CRISPR screens.
DR   ChiTaRS; Igf1; mouse.
DR   PRO; PR:P05017; -.
DR   Proteomes; UP000000589; Chromosome 10.
DR   RNAct; P05017; Protein.
DR   Bgee; ENSMUSG00000020053; Expressed in stria vascularis of cochlear duct and 272 other cell types or tissues.
DR   ExpressionAtlas; P05017; baseline and differential.
DR   GO; GO:0035867; C:alphav-beta3 integrin-IGF-1-IGF1R complex; ISS:UniProtKB.
DR   GO; GO:0070382; C:exocytic vesicle; IDA:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IDA:MGI.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0042567; C:insulin-like growth factor ternary complex; ISS:BHF-UCL.
DR   GO; GO:0005614; C:interstitial matrix; ISO:MGI.
DR   GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR   GO; GO:0099013; C:neuronal dense core vesicle lumen; IDA:SynGO.
DR   GO; GO:0031091; C:platelet alpha granule; ISO:MGI.
DR   GO; GO:0098794; C:postsynapse; IEA:GOC.
DR   GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0005179; F:hormone activity; ISO:MGI.
DR   GO; GO:0005158; F:insulin receptor binding; IDA:MGI.
DR   GO; GO:0005159; F:insulin-like growth factor receptor binding; IPI:MGI.
DR   GO; GO:0005178; F:integrin binding; ISO:MGI.
DR   GO; GO:0043539; F:protein serine/threonine kinase activator activity; ISO:MGI.
DR   GO; GO:0048018; F:receptor ligand activity; IDA:MGI.
DR   GO; GO:0005496; F:steroid binding; ISO:MGI.
DR   GO; GO:0030297; F:transmembrane receptor protein tyrosine kinase activator activity; IDA:MGI.
DR   GO; GO:0030521; P:androgen receptor signaling pathway; IMP:MGI.
DR   GO; GO:0001974; P:blood vessel remodeling; IMP:MGI.
DR   GO; GO:0035630; P:bone mineralization involved in bone maturation; ISO:MGI.
DR   GO; GO:0048754; P:branching morphogenesis of an epithelial tube; IMP:MGI.
DR   GO; GO:0001775; P:cell activation; ISO:MGI.
DR   GO; GO:0048468; P:cell development; IMP:MGI.
DR   GO; GO:0008283; P:cell population proliferation; IMP:MGI.
DR   GO; GO:1904646; P:cellular response to amyloid-beta; ISO:MGI.
DR   GO; GO:0071333; P:cellular response to glucose stimulus; IDA:MGI.
DR   GO; GO:1990314; P:cellular response to insulin-like growth factor stimulus; IMP:MGI.
DR   GO; GO:0021930; P:cerebellar granule cell precursor proliferation; IDA:MGI.
DR   GO; GO:0050650; P:chondroitin sulfate proteoglycan biosynthetic process; IDA:MGI.
DR   GO; GO:0007623; P:circadian rhythm; IEP:UniProtKB.
DR   GO; GO:0050974; P:detection of mechanical stimulus involved in sensory perception; ISO:MGI.
DR   GO; GO:0031017; P:exocrine pancreas development; IMP:MGI.
DR   GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IDA:MGI.
DR   GO; GO:0010001; P:glial cell differentiation; IMP:MGI.
DR   GO; GO:0048839; P:inner ear development; IDA:MGI.
DR   GO; GO:0048009; P:insulin-like growth factor receptor signaling pathway; IDA:MGI.
DR   GO; GO:0048286; P:lung alveolus development; IMP:MGI.
DR   GO; GO:0030324; P:lung development; IGI:MGI.
DR   GO; GO:0060463; P:lung lobe morphogenesis; IMP:MGI.
DR   GO; GO:0060426; P:lung vasculature development; IMP:MGI.
DR   GO; GO:0030879; P:mammary gland development; IMP:MGI.
DR   GO; GO:0007613; P:memory; ISO:MGI.
DR   GO; GO:0035264; P:multicellular organism growth; IDA:MGI.
DR   GO; GO:0014896; P:muscle hypertrophy; ISO:MGI.
DR   GO; GO:0045445; P:myoblast differentiation; ISO:MGI.
DR   GO; GO:0051450; P:myoblast proliferation; ISO:MGI.
DR   GO; GO:0014904; P:myotube cell development; ISO:MGI.
DR   GO; GO:0014902; P:myotube differentiation; IDA:MGI.
DR   GO; GO:1902430; P:negative regulation of amyloid-beta formation; ISO:MGI.
DR   GO; GO:0060766; P:negative regulation of androgen receptor signaling pathway; IMP:MGI.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:MGI.
DR   GO; GO:1904193; P:negative regulation of cholangiocyte apoptotic process; ISO:MGI.
DR   GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IGI:MGI.
DR   GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; ISO:MGI.
DR   GO; GO:0010629; P:negative regulation of gene expression; IDA:BHF-UCL.
DR   GO; GO:0002683; P:negative regulation of immune system process; ISO:MGI.
DR   GO; GO:0032691; P:negative regulation of interleukin-1 beta production; ISO:MGI.
DR   GO; GO:0010656; P:negative regulation of muscle cell apoptotic process; ISO:MGI.
DR   GO; GO:0150079; P:negative regulation of neuroinflammatory response; ISO:MGI.
DR   GO; GO:1900142; P:negative regulation of oligodendrocyte apoptotic process; ISO:MGI.
DR   GO; GO:0060283; P:negative regulation of oocyte development; ISO:MGI.
DR   GO; GO:0050732; P:negative regulation of peptidyl-tyrosine phosphorylation; IMP:MGI.
DR   GO; GO:0090201; P:negative regulation of release of cytochrome c from mitochondria; IDA:UniProtKB.
DR   GO; GO:0034392; P:negative regulation of smooth muscle cell apoptotic process; ISS:UniProtKB.
DR   GO; GO:0032720; P:negative regulation of tumor necrosis factor production; ISO:MGI.
DR   GO; GO:1905460; P:negative regulation of vascular associated smooth muscle cell apoptotic process; ISO:MGI.
DR   GO; GO:0007399; P:nervous system development; IMP:MGI.
DR   GO; GO:0001649; P:osteoblast differentiation; IEP:BHF-UCL.
DR   GO; GO:0043491; P:phosphatidylinositol 3-kinase/protein kinase B signal transduction; IDA:MGI.
DR   GO; GO:0042104; P:positive regulation of activated T cell proliferation; ISO:MGI.
DR   GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; ISO:MGI.
DR   GO; GO:0070886; P:positive regulation of calcineurin-NFAT signaling cascade; ISO:MGI.
DR   GO; GO:0010613; P:positive regulation of cardiac muscle hypertrophy; ISO:MGI.
DR   GO; GO:0030307; P:positive regulation of cell growth; ISO:MGI.
DR   GO; GO:0061051; P:positive regulation of cell growth involved in cardiac muscle cell development; ISO:MGI.
DR   GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR   GO; GO:0021940; P:positive regulation of cerebellar granule cell precursor proliferation; IDA:MGI.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISO:MGI.
DR   GO; GO:0050679; P:positive regulation of epithelial cell proliferation; ISO:MGI.
DR   GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR   GO; GO:0045600; P:positive regulation of fat cell differentiation; ISO:MGI.
DR   GO; GO:0048146; P:positive regulation of fibroblast proliferation; ISO:MGI.
DR   GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR   GO; GO:0060252; P:positive regulation of glial cell proliferation; ISO:MGI.
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:MGI.
DR   GO; GO:0010560; P:positive regulation of glycoprotein biosynthetic process; ISO:MGI.
DR   GO; GO:0043568; P:positive regulation of insulin-like growth factor receptor signaling pathway; ISO:MGI.
DR   GO; GO:0043410; P:positive regulation of MAPK cascade; ISS:UniProtKB.
DR   GO; GO:0045840; P:positive regulation of mitotic nuclear division; ISO:MGI.
DR   GO; GO:0031643; P:positive regulation of myelination; IDA:ARUK-UCL.
DR   GO; GO:2000288; P:positive regulation of myoblast proliferation; IMP:MGI.
DR   GO; GO:0045669; P:positive regulation of osteoblast differentiation; ISO:MGI.
DR   GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:MGI.
DR   GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IDA:MGI.
DR   GO; GO:0050714; P:positive regulation of protein secretion; ISO:MGI.
DR   GO; GO:0046579; P:positive regulation of Ras protein signal transduction; ISO:MGI.
DR   GO; GO:0014911; P:positive regulation of smooth muscle cell migration; ISO:MGI.
DR   GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISO:MGI.
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; IDA:MGI.
DR   GO; GO:1904075; P:positive regulation of trophectodermal cell proliferation; ISO:MGI.
DR   GO; GO:1904692; P:positive regulation of type B pancreatic cell proliferation; IGI:MGI.
DR   GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; ISO:MGI.
DR   GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; ISO:MGI.
DR   GO; GO:1905564; P:positive regulation of vascular endothelial cell proliferation; ISO:MGI.
DR   GO; GO:0099170; P:postsynaptic modulation of chemical synaptic transmission; IDA:SynGO.
DR   GO; GO:0060527; P:prostate epithelial cord arborization involved in prostate glandular acinus morphogenesis; IMP:MGI.
DR   GO; GO:0060740; P:prostate gland epithelium morphogenesis; IMP:MGI.
DR   GO; GO:0060736; P:prostate gland growth; IDA:MGI.
DR   GO; GO:0060741; P:prostate gland stromal morphogenesis; IMP:MGI.
DR   GO; GO:0050821; P:protein stabilization; ISO:MGI.
DR   GO; GO:0030166; P:proteoglycan biosynthetic process; ISO:MGI.
DR   GO; GO:0051924; P:regulation of calcium ion transport; ISO:MGI.
DR   GO; GO:0042127; P:regulation of cell population proliferation; ISO:MGI.
DR   GO; GO:0032878; P:regulation of establishment or maintenance of cell polarity; IDA:MGI.
DR   GO; GO:0010468; P:regulation of gene expression; ISO:MGI.
DR   GO; GO:0045428; P:regulation of nitric oxide biosynthetic process; IMP:MGI.
DR   GO; GO:0051246; P:regulation of protein metabolic process; IGI:MGI.
DR   GO; GO:0001932; P:regulation of protein phosphorylation; IDA:MGI.
DR   GO; GO:0006417; P:regulation of translation; ISO:MGI.
DR   GO; GO:0045471; P:response to ethanol; ISO:MGI.
DR   GO; GO:0009408; P:response to heat; ISO:MGI.
DR   GO; GO:1990009; P:retinal cell apoptotic process; ISO:MGI.
DR   GO; GO:0007608; P:sensory perception of smell; TAS:UniProtKB.
DR   GO; GO:0014834; P:skeletal muscle satellite cell maintenance involved in skeletal muscle regeneration; ISO:MGI.
DR   GO; GO:0044342; P:type B pancreatic cell proliferation; IGI:MGI.
DR   GO; GO:0060509; P:type I pneumocyte differentiation; IMP:MGI.
DR   GO; GO:0060510; P:type II pneumocyte differentiation; IMP:MGI.
DR   GO; GO:0042060; P:wound healing; ISO:MGI.
DR   CDD; cd04368; IlGF; 1.
DR   Gene3D; 1.10.100.10; Insulin-like; 1.
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   PANTHER; PTHR46845; INSULIN-LIKE GROWTH FACTOR I; 1.
DR   PANTHER; PTHR46845:SF1; INSULIN-LIKE GROWTH FACTOR I; 1.
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; Insulin-like; 1.
DR   PROSITE; PS00262; INSULIN; 1.
DR   Genevisible; P05017; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; Disulfide bond; Growth factor; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..?
FT                   /evidence="ECO:0000255"
FT   PROPEP          ?..48
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000015666"
FT   CHAIN           49..118
FT                   /note="Insulin-like growth factor I"
FT                   /id="PRO_0000015667"
FT   PROPEP          119..153
FT                   /note="E peptide"
FT                   /id="PRO_0000015668"
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          120..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 -> SPSLSTNKKTKLQRRRKGSTFEE (in
FT                   isoform IGF-IB)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:3774549"
FT                   /id="VSP_012165"
SQ   SEQUENCE   153 AA;  17093 MW;  967596AEAC0CA387 CRC64;
     MGKISSLPTQ LFKICLCDFL KIKIHIMSSS HLFYLALCLL TFTSSTTAGP ETLCGAELVD
     ALQFVCGPRG FYFNKPTGYG SSIRRAPQTG IVDECCFRSC DLRRLEMYCA PLKPTKAARS
     IRAQRHTDMP KTQKEVHLKN TSRGSAGNKT YRM
//