IGF1_ONCKI
ID IGF1_ONCKI Reviewed; 188 AA.
AC P17085; P81268; Q6LDG9; Q91161; Q91162; Q91475;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Insulin-like growth factor I;
DE Short=IGF-I;
DE AltName: Full=Somatomedin;
DE Flags: Precursor;
GN Name=igf1;
OS Oncorhynchus kisutch (Coho salmon) (Salmo kisutch).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Oncorhynchus.
OX NCBI_TaxID=8019;
RN [1]
RP NUCLEOTIDE SEQUENCE (ISOFORM 2).
RC TISSUE=Liver;
RX PubMed=2628735; DOI=10.1210/mend-3-12-2005;
RA Cao Q.-P., Duguay S.J., Plisetskaya E.M., Steiner D.F., Chan S.J.;
RT "Nucleotide sequence and growth hormone-regulated expression of salmon
RT insulin-like growth factor I mRNA.";
RL Mol. Endocrinol. 3:2005-2010(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE (ISOFORM 3).
RX PubMed=8024699; DOI=10.1089/dna.1994.13.555;
RA Kavsan V.M., Grebenjuk V.A., Koval A.P., Skorokhod A.S., Roberts C.T. Jr.,
RA Leroith D.;
RT "Isolation of a second nonallelic insulin-like growth factor I gene from
RT the salmon genome.";
RL DNA Cell Biol. 13:555-559(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE (ISOFORM 3).
RA Grebenjuk V.A., Skorokhod A.S., Anoprienko O.V., Koval A.P.;
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE OF 27-169 (ISOFORMS 1; 2 AND 3).
RC TISSUE=Liver;
RX PubMed=1406698; DOI=10.1210/mend.6.8.1406698;
RA Duguay S.J., Park L.K., Samadpour M., Dickhoff W.W.;
RT "Nucleotide sequence and tissue distribution of three insulin-like growth
RT factor I prohormones in salmon.";
RL Mol. Endocrinol. 6:1202-1210(1992).
RN [5]
RP PROTEIN SEQUENCE OF 45-114.
RX PubMed=8243465; DOI=10.1111/j.1432-1033.1993.tb18366.x;
RA Moriyama S., Duguay S.J., Conlon J.M., Duan C., Dickhoff W.W.,
RA Plisetskaya E.M.;
RT "Recombinant coho salmon insulin-like growth factor I. Expression in
RT Escherichia coli, purification and characterization.";
RL Eur. J. Biochem. 218:205-211(1993).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=3; Synonyms=Ea-3;
CC IsoId=P17085-1; Sequence=Displayed;
CC Name=1; Synonyms=Ea-1;
CC IsoId=P17085-2; Sequence=VSP_010979;
CC Name=2; Synonyms=Ea-2;
CC IsoId=P17085-3; Sequence=VSP_010980;
CC -!- TISSUE SPECIFICITY: All the isoforms are expressed in embryos, juvenile
CC and adult liver, muscle and brain. At least one isoform is expressed in
CC heart, kidney, testes, ovary, adipose tissue and spleen of juvenile
CC salmon.
CC -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
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DR EMBL; M32792; AAA49410.1; -; mRNA.
DR EMBL; AF063216; AAC18833.1; -; Genomic_DNA.
DR EMBL; M81911; AAB59947.1; -; mRNA.
DR EMBL; M81912; AAB59948.1; -; mRNA.
DR EMBL; M81913; AAA49413.1; -; mRNA.
DR EMBL; M81904; AAA18211.1; -; mRNA.
DR PIR; A41396; A41396.
DR PIR; C44012; C44012.
DR AlphaFoldDB; P17085; -.
DR SMR; P17085; -.
DR Proteomes; UP000694557; 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 1: Evidence at protein level;
KW Alternative splicing; Direct protein sequencing; Disulfide bond;
KW Growth factor; Reference proteome; Secreted; Signal.
FT SIGNAL 1..?
FT PROPEP ?..44
FT /evidence="ECO:0000269|PubMed:8243465"
FT /id="PRO_0000015702"
FT CHAIN 45..114
FT /note="Insulin-like growth factor I"
FT /id="PRO_0000015703"
FT PROPEP 115..188
FT /note="E peptide"
FT /id="PRO_0000015704"
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..188
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..158
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..188
FT /note="Polar 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"
FT VAR_SEQ 131..169
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000305"
FT /id="VSP_010979"
FT VAR_SEQ 158..169
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_010980"
FT CONFLICT 6
FT /note="L -> F (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 22
FT /note="I -> V (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 131
FT /note="V -> I (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 155
FT /note="P -> T (in Ref. 4; AAA18211)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="N -> H (in Ref. 4; AAA18211)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 188 AA; 20758 MW; 76253FA958328B00 CRC64;
MSSGHLFQWH LCDVFKSAMC CISCTHTLSL LLCVLTLTSA ATGAGPETLC GAELVDTLQF
VCGERGFYFS KPTGYGPSSR RSHNRGIVDE CCFQSCELRR LEMYCAPVKS GKAARSVRAQ
RHTDMPRTPK VSTAVQNVDR GTERRTAQHP DKTKPKKKPL SGNSHTSCKE VHQKNSSRGN
TGGRNYRM
