ID   IGF1_COTJA              Reviewed;         124 AA.
AC   P51462;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Insulin-like growth factor I;
DE            Short=IGF-I;
DE   AltName: Full=Somatomedin;
DE   Flags: Precursor; Fragment;
GN   Name=IGF1;
OS   Coturnix japonica (Japanese quail) (Coturnix coturnix japonica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Perdicinae; Coturnix.
OX   NCBI_TaxID=93934;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7881819;
RA   Kida S., Iwaki M., Nakamura A., Miura Y., Takenaka A., Takahashi S.,
RA   Noguchi T.;
RT   "Insulin-like growth factor-I messenger RNA content in the oviduct of
RT   Japanese quail (Coturnix coturnix japonica): changes during growth and
RT   development or after estrogen administration.";
RL   Comp. Biochem. Physiol. 109C:191-204(1994).
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}.
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DR   EMBL; S75247; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; P51462; -.
DR   SMR; P51462; -.
DR   Proteomes; UP000694412; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0005179; F:hormone activity; IEA:InterPro.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR   GO; GO:0090201; P:negative regulation of release of cytochrome c from mitochondria; ISS:UniProtKB.
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   2: Evidence at transcript level;
KW   Disulfide bond; Growth factor; Reference proteome; Secreted.
FT   PROPEP          <1..19
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000015693"
FT   CHAIN           20..89
FT                   /note="Insulin-like growth factor I"
FT                   /id="PRO_0000015694"
FT   PROPEP          90..124
FT                   /note="E peptide"
FT                   /id="PRO_0000015695"
FT   REGION          20..48
FT                   /note="B"
FT   REGION          49..60
FT                   /note="C"
FT   REGION          61..81
FT                   /note="A"
FT   REGION          82..89
FT                   /note="D"
FT   REGION          86..124
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        92..109
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        110..124
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        25..67
FT                   /evidence="ECO:0000250"
FT   DISULFID        37..80
FT                   /evidence="ECO:0000250"
FT   DISULFID        66..71
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   124 AA;  13888 MW;  52254EB1BA52C3B6 CRC64;
     IHFFYLGLCL LTLTSSAAAG PETLCGAELV DALQFVCGDR GFYFSKPTGY GSSSRRLHHK
     GIVDECCFQS CDLRRLEMYC APIKPPKSAR SVRAQRHTDM PKAQKEVHLK NTSRGNTGNR
     NYRM