IGF1_CHICK
ID IGF1_CHICK Reviewed; 153 AA.
AC P18254;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Insulin-like growth factor I;
DE Short=IGF-I;
DE AltName: Full=Somatomedin;
DE Flags: Precursor;
GN Name=IGF1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2628728; DOI=10.1210/mend-3-12-1907;
RA Kajimoto Y., Rotwein P.;
RT "Structure and expression of a chicken insulin-like growth factor I
RT precursor.";
RL Mol. Endocrinol. 3:1907-1913(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
RX PubMed=2033062; DOI=10.1016/s0021-9258(18)92881-4;
RA Rotwein P., Kajimoto Y.;
RT "Structure of the chicken insulin-like growth factor I gene reveals
RT conserved promoter elements.";
RL J. Biol. Chem. 266:9724-9731(1991).
RN [3]
RP PROTEIN SEQUENCE OF 49-118.
RX PubMed=2272467; DOI=10.1016/0016-6480(90)90076-x;
RA Ballard F.J., Johnson R.J., Owens P.C., Francis G.L., Upton F.M.,
RA McMurtry J.P., Wallace J.C.;
RT "Chicken insulin-like growth factor-I: amino acid sequence,
RT radioimmunoassay, and plasma levels between strains and during growth.";
RL Gen. Comp. Endocrinol. 79:459-468(1990).
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. Acts as a ligand for IGF1R. Binds to the
CC alpha subunit of IGF1R, leading to the activation of the intrinsic
CC tyrosine kinase activity which autophosphorylates tyrosine residues in
CC the beta subunit thus initiatiating a cascade of down-stream signaling
CC events leading to activation of the PI3K-AKT/PKB and the Ras-MAPK
CC pathways. Binds to integrins. Its binding to integrins and subsequent
CC ternary complex formation with integrins and IGFR1 are essential for
CC IGF1 signaling. {ECO:0000250|UniProtKB:P05019}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M32791; AAA48828.1; -; mRNA.
DR EMBL; M74176; AAA48829.1; -; Genomic_DNA.
DR PIR; A41399; A41399.
DR RefSeq; NP_001004384.1; NM_001004384.2.
DR AlphaFoldDB; P18254; -.
DR SMR; P18254; -.
DR STRING; 9031.ENSGALP00000020787; -.
DR PaxDb; P18254; -.
DR Ensembl; ENSGALT00000020816; ENSGALP00000020787; ENSGALG00000012755.
DR GeneID; 418090; -.
DR KEGG; gga:418090; -.
DR CTD; 3479; -.
DR VEuPathDB; HostDB:geneid_418090; -.
DR eggNOG; ENOG502RCAB; Eukaryota.
DR GeneTree; ENSGT00940000159081; -.
DR HOGENOM; CLU_123939_0_0_1; -.
DR InParanoid; P18254; -.
DR OMA; FFYLALC; -.
DR OrthoDB; 1644517at2759; -.
DR PhylomeDB; P18254; -.
DR TreeFam; TF332820; -.
DR Reactome; R-GGA-114608; Platelet degranulation.
DR Reactome; R-GGA-2404192; Signaling by Type 1 Insulin-like Growth Factor 1 Receptor (IGF1R).
DR Reactome; R-GGA-2428928; IRS-related events triggered by IGF1R.
DR Reactome; R-GGA-2428933; SHC-related events triggered by IGF1R.
DR Reactome; R-GGA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-GGA-422085; Synthesis, secretion, and deacylation of Ghrelin.
DR PRO; PR:P18254; -.
DR Proteomes; UP000000539; Chromosome 1.
DR Bgee; ENSGALG00000012755; Expressed in liver and 3 other tissues.
DR ExpressionAtlas; P18254; baseline and differential.
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:AgBase.
DR GO; GO:0008283; P:cell population proliferation; IDA:AgBase.
DR GO; GO:0090103; P:cochlea morphogenesis; IMP:AgBase.
DR GO; GO:0061560; P:cranial ganglion formation; IMP:AgBase.
DR GO; GO:0010467; P:gene expression; IDA:AgBase.
DR GO; GO:0048009; P:insulin-like growth factor receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0046676; P:negative regulation of insulin secretion; IDA:AgBase.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:AgBase.
DR GO; GO:0090201; P:negative regulation of release of cytochrome c from mitochondria; ISS:UniProtKB.
DR GO; GO:0007405; P:neuroblast proliferation; IMP:AgBase.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IBA:GO_Central.
DR GO; GO:0090277; P:positive regulation of peptide hormone secretion; IDA:AgBase.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IBA:GO_Central.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IDA:AgBase.
DR GO; GO:0001932; P:regulation of protein phosphorylation; IBA:GO_Central.
DR GO; GO:0009408; P:response to heat; IDA:AgBase.
DR GO; GO:1990418; P:response to insulin-like growth factor stimulus; IDA:AgBase.
DR GO; GO:0021650; P:vestibulocochlear nerve formation; IMP: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 PROPEP ?..48
FT /evidence="ECO:0000269|PubMed:2272467"
FT /id="PRO_0000015690"
FT CHAIN 49..118
FT /note="Insulin-like growth factor I"
FT /id="PRO_0000015691"
FT PROPEP 119..153
FT /note="E peptide"
FT /id="PRO_0000015692"
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"
SQ SEQUENCE 153 AA; 17267 MW; AAE13FDED13EE2F8 CRC64;
MEKINSLSTQ LVKCCFCDFL KVKMHTVSYI HFFYLGLCLL TLTSSAAAGP ETLCGAELVD
ALQFVCGDRG FYFSKPTGYG SSSRRLHHKG IVDECCFQSC DLRRLEMYCA PIKPPKSARS
VRAQRHTDMP KAQKEVHLKN TSRGNTGNRN YRM
