ID   IGF1_RHIRO              Reviewed;         153 AA.
AC   Q68LC0;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Insulin-like growth factor I;
DE            Short=IGF-I;
DE   AltName: Full=Somatomedin;
DE   Flags: Precursor;
GN   Name=IGF1;
OS   Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Colobinae; Rhinopithecus.
OX   NCBI_TaxID=61622;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RA   Song L., Hu X., Yue B., Zhang Z., Zhu M., Shen F., Zhang W.;
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
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; AY677085; AAT97354.1; -; mRNA.
DR   AlphaFoldDB; Q68LC0; -.
DR   SMR; Q68LC0; -.
DR   STRING; 61622.XP_010355571.1; -.
DR   Proteomes; UP000233200; Whole Genome Shotgun Assembly.
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; 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:0005159; F:insulin-like growth factor receptor binding; ISS:UniProtKB.
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: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   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   Cleavage on pair of basic residues; Disulfide bond; Growth factor;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..?
FT   PROPEP          ?..48
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000015676"
FT   CHAIN           49..118
FT                   /note="Insulin-like growth factor I"
FT                   /id="PRO_0000015677"
FT   PROPEP          119..153
FT                   /note="E peptide"
FT                   /id="PRO_0000015678"
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   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;  16974 MW;  5B1D232DCA91CC00 CRC64;
     MGKISSLPTQ LFKCCFCDFL KVKMHIMSSS HLLYLALCLL TFTSSATAGP ETLCGAELVD
     ALQFVCGDRG FYFNKPTGYG SSSRRAPQTG IVDECCFRSC DLRRLEMYCA PLKPAKSARS
     VRAQRHTDMP KAQKEVHLKN ASRGSAGNKN YRM