IGF1_BOVIN
ID IGF1_BOVIN Reviewed; 154 AA.
AC P07455;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Insulin-like growth factor I;
DE Short=IGF-I;
DE AltName: Full=Somatomedin;
DE Flags: Precursor;
GN Name=IGF1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-154.
RX PubMed=2308858; DOI=10.1093/nar/18.3.676;
RA Fotsis T., Murphy C., Gannon F.;
RT "Nucleotide sequence of the bovine insulin-like growth factor 1 (IGF-1) and
RT its IGF-1A precursor.";
RL Nucleic Acids Res. 18:676-676(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 50-119.
RX PubMed=7867698; DOI=10.1055/s-0029-1211305;
RA Schmidt A., Einspanier R., Amselgruber W., Sinowatz F., Schams D.;
RT "Expression of insulin-like growth factor 1 (IGF-1) in the bovine oviduct
RT during the oestrous cycle.";
RL Exp. Clin. Endocrinol. 102:364-369(1994).
RN [3]
RP PROTEIN SEQUENCE OF 50-119.
RX PubMed=3941093; DOI=10.1016/s0021-9258(17)36130-6;
RA Honegger A., Humbel R.E.;
RT "Insulin-like growth factors I and II in fetal and adult bovine serum.
RT Purification, primary structures, and immunological cross-reactivities.";
RL J. Biol. Chem. 261:569-575(1986).
RN [4]
RP PROTEIN SEQUENCE OF 50-119.
RX PubMed=3390164; DOI=10.1042/bj2510095;
RA Francis G.L., Upton F.M., Ballard F.J., McNeil K.A., Wallace J.C.;
RT "Insulin-like growth factors 1 and 2 in bovine colostrum. Sequences and
RT biological activities compared with those of a potent truncated form.";
RL Biochem. J. 251:95-103(1988).
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 -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR EMBL; X15726; CAA33746.1; -; mRNA.
DR EMBL; S76122; AAD14209.1; -; mRNA.
DR PIR; S12672; IGBO1.
DR RefSeq; NP_001071296.1; NM_001077828.1.
DR AlphaFoldDB; P07455; -.
DR BMRB; P07455; -.
DR SMR; P07455; -.
DR STRING; 9913.ENSBTAP00000055243; -.
DR PaxDb; P07455; -.
DR PRIDE; P07455; -.
DR Ensembl; ENSBTAT00000014713; ENSBTAP00000014713; ENSBTAG00000011082.
DR GeneID; 281239; -.
DR KEGG; bta:281239; -.
DR CTD; 3479; -.
DR VEuPathDB; HostDB:ENSBTAG00000011082; -.
DR VGNC; VGNC:30076; IGF1.
DR eggNOG; ENOG502RCAB; Eukaryota.
DR GeneTree; ENSGT00940000159081; -.
DR HOGENOM; CLU_123939_0_0_1; -.
DR InParanoid; P07455; -.
DR OMA; FFYLALC; -.
DR Reactome; R-BTA-114608; Platelet degranulation.
DR Reactome; R-BTA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-BTA-422085; Synthesis, secretion, and deacylation of Ghrelin.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000011082; Expressed in myometrium and 100 other tissues.
DR ExpressionAtlas; P07455; baseline and differential.
DR GO; GO:0035867; C:alphav-beta3 integrin-IGF-1-IGF1R complex; ISS:UniProtKB.
DR GO; GO:0070382; C:exocytic vesicle; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:AgBase.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0005179; F:hormone activity; IBA:GO_Central.
DR GO; GO:0005159; F:insulin-like growth factor receptor binding; ISS:UniProtKB.
DR GO; GO:0008283; P:cell population proliferation; IDA:AgBase.
DR GO; GO:0042538; P:hyperosmotic salinity response; IMP:AgBase.
DR GO; GO:0048009; P:insulin-like growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:1903407; P:negative regulation of P-type sodium:potassium-exchanging transporter activity; IMP:AgBase.
DR GO; GO:0090201; P:negative regulation of release of cytochrome c from mitochondria; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
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:1903408; P:positive regulation of P-type sodium:potassium-exchanging transporter activity; IMP:AgBase.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IBA:GO_Central.
DR GO; GO:0001932; P:regulation of protein phosphorylation; IBA:GO_Central.
DR GO; GO:0051602; P:response to electrical stimulus; IDA:AgBase.
DR GO; GO:0032094; P:response to food; IDA:AgBase.
DR GO; GO:0060416; P:response to growth hormone; IDA:AgBase.
DR GO; GO:0032868; P:response to insulin; IDA:AgBase.
DR GO; GO:0071000; P:response to magnetism; IDA:AgBase.
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; 1.
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 Direct protein sequencing; Disulfide bond; Growth factor;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..?
FT /evidence="ECO:0000255"
FT PROPEP ?..49
FT /id="PRO_0000015647"
FT CHAIN 50..119
FT /note="Insulin-like growth factor I"
FT /id="PRO_0000015648"
FT PROPEP 120..154
FT /note="E peptide"
FT /id="PRO_0000015649"
FT REGION 50..78
FT /note="B"
FT REGION 79..90
FT /note="C"
FT REGION 91..111
FT /note="A"
FT REGION 112..119
FT /note="D"
FT REGION 121..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 55..97
FT /evidence="ECO:0000250"
FT DISULFID 67..110
FT /evidence="ECO:0000250"
FT DISULFID 96..101
FT /evidence="ECO:0000250"
SQ SEQUENCE 154 AA; 17066 MW; 64201B6AF3140999 CRC64;
MGKISSLPTQ LFKCCFCDFL KQVKMPITSS SHLFYLALCL LAFTSSATAG PETLCGAELV
DALQFVCGDR GFYFNKPTGY GSSSRRAPQT GIVDECCFRS CDLRRLEMYC APLKPAKSAR
SVRAQRHTDM PKAQKEVHLK NTSRGSAGNK NYRM
