ID   IGF1_ONCMY              Reviewed;         176 AA.
AC   Q02815;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Insulin-like growth factor I;
DE            Short=IGF-I;
DE   AltName: Full=Somatomedin;
DE   Flags: Precursor;
GN   Name=igf1;
OS   Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Oncorhynchus.
OX   NCBI_TaxID=8022;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=1409585; DOI=10.1073/pnas.89.19.8913;
RA   Shamblott M.J., Chen T.T.;
RT   "Identification of a second insulin-like growth factor in a fish species.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:8913-8917(1992).
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; M95183; AAA49412.1; -; mRNA.
DR   PIR; A46244; A46244.
DR   RefSeq; NP_001118168.1; NM_001124696.1.
DR   AlphaFoldDB; Q02815; -.
DR   SMR; Q02815; -.
DR   Ensembl; ENSOMYT00000091213; ENSOMYP00000083744; ENSOMYG00000038605.
DR   GeneID; 100136741; -.
DR   KEGG; omy:100136741; -.
DR   GeneTree; ENSGT00940000159081; -.
DR   OrthoDB; 1644517at2759; -.
DR   SABIO-RK; Q02815; -.
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; IEA:InterPro.
DR   GO; GO:0005159; F:insulin-like growth factor receptor binding; IDA:AgBase.
DR   GO; GO:0042538; P:hyperosmotic salinity response; IDA:AgBase.
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:0061036; P:positive regulation of cartilage development; IDA:AgBase.
DR   GO; GO:0060416; P:response to growth hormone; 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   2: Evidence at transcript level;
KW   Disulfide bond; Growth factor; Secreted; Signal.
FT   SIGNAL          1..?
FT   PROPEP          ?..44
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000015705"
FT   CHAIN           45..114
FT                   /note="Insulin-like growth factor I"
FT                   /id="PRO_0000015706"
FT   PROPEP          115..176
FT                   /note="E peptide"
FT                   /id="PRO_0000015707"
FT   REGION          45..73
FT                   /note="B"
FT   REGION          74..85
FT                   /note="C"
FT   REGION          86..106
FT                   /note="A"
FT   REGION          107..114
FT                   /note="D"
FT   REGION          115..176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        126..141
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        142..163
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        50..92
FT                   /evidence="ECO:0000250"
FT   DISULFID        62..105
FT                   /evidence="ECO:0000250"
FT   DISULFID        91..96
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   176 AA;  19510 MW;  DE86283D80DDAD06 CRC64;
     MSSGHFFQWH LCDVFKSAMC CVSCTHTLSL LLCVLTLTSA ATGAGPETLC GAELVDTLQF
     VCGERGFYFS KPTGYGPSSR RSHNRGIVDE CCFQSCELRR LEMYCAPVKS GKAARSVRAQ
     RHTDMPRTPK VSTAVQSVDR GTERRTAQHP DKTKPKKEVH QKNSSRGNTG GRNYRM