[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=2937782 [NCBI, ExPASy, EBI, Israel, Japan] Rotwein P., Pollock K.M., Didier D.K., Krivi G.G.; "Organization and sequence of the human insulin-like growth factor I gene. Alternative RNA processing produces two insulin-like growth factor I precursor peptides."; J. Biol. Chem. 261:4828-4832(1986).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1038/306609a0; PubMed=6358902 [NCBI, ExPASy, EBI, Israel, Japan] Jansen M., van Schaik F.M.A., Ricker A.T., Bullock B., Woods D.E., Gabbay K.H., Nussbaum A.L., Sussenbach J.S., van den Brande J.L.; "Sequence of cDNA encoding human insulin-like growth factor I precursor."; Nature 306:609-611(1983).
[3]	NUCLEOTIDE SEQUENCE. DOI=10.1016/0014-5793(86)80223-X; PubMed=2935423 [NCBI, ExPASy, EBI, Israel, Japan] le Bouc Y., Dreyer D., Jaeger F., Binoux M., Sondermeyer P.; "Complete characterization of the human IGF-I nucleotide sequence isolated from a newly constructed adult liver cDNA library."; FEBS Lett. 196:108-112(1986).
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1016/0014-5793(86)80156-9; PubMed=3002851 [NCBI, ExPASy, EBI, Israel, Japan] de Pagter-Holthuizen P., van Schaik F.M.A., Verduijn G.M., van Ommen G.J.B., Bouma B.N., Jansen M., Sussenbach J.S.; "Organization of the human genes for insulin-like growth factors I and II."; FEBS Lett. 195:179-184(1986).
[5]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Liver; DOI=10.1016/0006-291X(91)91593-2; PubMed=2018498 [NCBI, ExPASy, EBI, Israel, Japan] Steenbergh P.H., Koonen-Reemst A.M.C.B., Cleutjens C.B.J.M., Sussenbach J.S.; "Complete nucleotide sequence of the high molecular weight human IGF-I mRNA."; Biochem. Biophys. Res. Commun. 175:507-514(1991).
[6]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Brain; DOI=10.1016/0169-328X(92)90094-R; PubMed=1372070 [NCBI, ExPASy, EBI, Israel, Japan] Sandberg-Nordqvist A.-C., Staehlbom P.-A., Lake M., Sara V.R.; "Characterization of two cDNAs encoding insulin-like growth factor 1 (IGF-1) in the human fetal brain."; Brain Res. Mol. Brain Res. 12:275-277(1992).
[7]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Rieder M.J., Livingston R.J., Daniels M.R., Chung M.-W., Miyamoto K.E., Nguyen C.P., Nguyen D.A., Poel C.L., Robertson P.D., Schackwitz W.S., Sherwood J.K., Witrak L.A., Nickerson D.A.; "NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu)."; Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
[8]	NUCLEOTIDE SEQUENCE OF 24-50 AND 119-153. DOI=10.1038/310777a0; PubMed=6382022 [NCBI, ExPASy, EBI, Israel, Japan] Dull T.J., Gray A., Hayflick J.S., Ullrich A.; "Insulin-like growth factor II precursor gene organization in relation to insulin gene family."; Nature 310:777-781(1984).
[9]	PROTEIN SEQUENCE OF 49-118. PubMed=632300 [NCBI, ExPASy, EBI, Israel, Japan] Rinderknecht E., Humbel R.E.; "The amino acid sequence of human insulin-like growth factor I and its structural homology with proinsulin."; J. Biol. Chem. 253:2769-2776(1978).
[10]	3D-STRUCTURE MODELING. PubMed=6189745 [NCBI, ExPASy, EBI, Israel, Japan] Blundell T.L., Bedarkar S., Humbel R.E.; "Tertiary structures, receptor binding, and antigenicity of insulinlike growth factors."; Fed. Proc. 42:2592-2597(1983).
[11]	STRUCTURE BY NMR. DOI=10.1021/bi00236a022; PubMed=2036417 [NCBI, ExPASy, EBI, Israel, Japan] Cooke R.M., Harvey T.S., Campbell I.D.; "Solution structure of human insulin-like growth factor 1: a nuclear magnetic resonance and restrained molecular dynamics study."; Biochemistry 30:5484-5491(1991).
[12]	STRUCTURE BY NMR. PubMed=1319992 [NCBI, ExPASy, EBI, Israel, Japan] Sato A., Nishimura S., Ohkubo T., Kyogoku Y., Koyama S., Kobayashi M., Yasuda T., Kobayashi Y.; "1H-NMR assignment and secondary structure of human insulin-like growth factor-I (IGF-I) in solution."; J. Biochem. 111:529-536(1992).
[13]	DISULFIDE BONDS. PubMed=3242681 [NCBI, ExPASy, EBI, Israel, Japan] Raschdorf F., Dahinden R., Maerki W., Richter W.J., Merryweather J.P.; "Location of disulphide bonds in human insulin-like growth factors (IGFs) synthesized by recombinant DNA technology."; Biomed. Environ. Mass Spectrom. 16:3-8(1988).
[14]	INVOLVEMENT IN IGF1 DEFICIENCY. DOI=10.1056/NEJM199610313351805; PubMed=8857020 [NCBI, ExPASy, EBI, Israel, Japan] Woods K.A., Camacho-Hubner C., Savage M.O., Clark A.J.; "Intrauterine growth retardation and postnatal growth failure associated with deletion of the insulin-like growth factor I gene."; N. Engl. J. Med. 335:1363-1367(1996).

Comments

FUNCTION: The insulin-like growth factors, isolated from plasma, are structurally and functionally related to insulin but have a much higher growth-promoting activity.
SUBCELLULAR LOCATION: Secreted.
ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.

Name IGF-IA

Isoform ID P01343-1

This is the isoform sequence displayed in this entry.

Name IGF-IB

Isoform ID P05019-1

This isoform is stored in UniProtKB/Swiss-Prot entry P05019.
DISEASE: Defects in IGF1 are the cause of insulin-like growth factor I deficiency (IGF1 deficiency) [MIM:608747]. IGF1 deficiency is an autosomal recessive disorder characterized by growth retardation, sensorineural deafness and mental retardation.
SIMILARITY: Belongs to the insulin family.
WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and polymorphism database; URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=HLA-DQB1";.
WEB RESOURCE: Name=Wikipedia; Note=Insulin-like growth factor 1 entry; URL="http://en.wikipedia.org/wiki/Insulin-like_growth_factor_1";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M14156; AAA52538.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M12659; AAA52538.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M14153; AAA52538.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M14154; AAA52538.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X00173; CAA24998.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M27544; AAA52787.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X03420; CAA27152.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X03421; CAA27153.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X03422; CAA27154.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X57025; CAA40342.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X56773; CAA40092.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY260957; AAO74829.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X03563; CAA27250.1; ALT_SEQ; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A92581; IGHU1.

NP_000609.1; -.

3D structure databases

PDB

1B9G; NMR; -; A=49-118.	[ExPASy / RCSB / EBI]
1GZR; X-ray; 2.00 A; B=49-118.	[ExPASy / RCSB / EBI]
1GZY; X-ray; 2.54 A; B=49-118.	[ExPASy / RCSB / EBI]
1GZZ; X-ray; 2.30 A; B=49-118.	[ExPASy / RCSB / EBI]
1H02; X-ray; 2.00 A; B=49-118.	[ExPASy / RCSB / EBI]
1H59; X-ray; 2.10 A; A=49-118.	[ExPASy / RCSB / EBI]
1IMX; X-ray; 1.82 A; A=49-118.	[ExPASy / RCSB / EBI]
1TGR; X-ray; 1.42 A; A/B=49-110.	[ExPASy / RCSB / EBI]
2GF1; NMR; -; A=49-118.	[ExPASy / RCSB / EBI]
3GF1; NMR; -; A=49-118.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1B9G; -.
1GZR; -.
1GZY; -.
1GZZ; -.
1H02; -.
1H59; -.
1IMX; -.
1TGR; -.
2GF1; -.
3GF1; -.

ModBase

P01343.

PTM databases

PhosphoSite

P01343; -.

Enzyme and pathway databases

Reactome

REACT_604; Hemostasis.

Polymorphism databases

NIEHS-SNPs

IGF1.

Organism-specific databases

HIX0036838; -.

HGNC:5464; IGF1.

147440; gene. [NCBI / EBI]
608747; phenotype. [NCBI / EBI]

PharmGKB

PA29697; -.

GeneCards

P01343.

Gene expression databases

ArrayExpress

P01343; -.

CleanEx

HS_IGF1; -.

GermOnline

ENSG00000017427; Homo sapiens.

Ontologies

GO:0031093;	Cellular component: platelet alpha granule lumen (inferred from experiment from Reactome).
GO:0008083;	Molecular function: growth factor activity (inferred from electronic annotation from UniProtKB-KW).
GO:0005179;	Molecular function: hormone activity (traceable author statement from ProtInc).
GO:0005159;	Molecular function: insulin-like growth factor receptor binding (traceable author statement from ProtInc).
GO:0006928;	Biological process: cell motion (traceable author statement from ProtInc).
GO:0006260;	Biological process: DNA replication (traceable author statement from ProtInc).
GO:0009441;	Biological process: glycolate metabolic process (traceable author statement from ProtInc).
GO:0007517;	Biological process: muscle development (traceable author statement from ProtInc).
GO:0007265;	Biological process: Ras protein signal transduction (traceable author statement from ProtInc).
GO:0033143;	Biological process: regulation of steroid hormone receptor signaling pathway (inferred from direct assay from MGI).
GO:0007605;	Biological process: sensory perception of sound (inferred from electronic annotation from UniProtKB-KW).
GO:0001501;	Biological process: skeletal system development (traceable author statement from ProtInc).
QuickGo view.

Family and domain databases

InterPro

IPR004825; Ins/IGF/relaxin.
Graphical view of domain structure.

Gene3D

G3DSA:1.10.100.10; Ins/IGF/relaxin; 1.

Pfam

PF00049; Insulin; 1.
Pfam graphical view of domain structure.

PRINTS

PR00276; INSULINA.
PR00277; INSULINB.

ProDom

PD001048; Bombyxin; 1.
PD015667; Mollusc_ins; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00078; IlGF; 1.
SMART graphical view of domain structure.

PS00262; INSULIN; 1.

Other

Genome annotation databases

Ensembl

ENSG00000017427; Homo sapiens. [Contig view]

GeneID

3479; -.

KEGG

hsa:3479; -.

Phylogenomic databases

HOVERGEN

P01343; -.

Other

P01343; -.

13678; -.

IGF1; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Alternative splicing; Deafness; Direct protein sequencing; Growth factor; Secreted; Signal.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 21`	`21`	`Potential.`
`PROPEP`	`22 48`	`27`		`PRO_0000015660`
`CHAIN`	`49 118`	`70`	`Insulin-like growth factor IA.`	`PRO_0000015661`
`PROPEP`	`119 153`	`35`	`E peptide.`	`PRO_0000015662`
`REGION`	`49 77`	`29`	`B.`
`REGION`	`78 89`	`12`	`C.`
`REGION`	`90 110`	`21`	`A.`
`REGION`	`111 118`	`8`	`D.`
`DISULFID`	`54 96`
`DISULFID`	`66 109`
`DISULFID`	`95 100`
`HELIX`	`52 66`	`15`
`HELIX`	`67 69`	`3`
`HELIX`	`75 95`	`21`
`STRAND`	`96 98`	`3`
`HELIX`	`102 108`	`7`

Sequence information

Length: 153 AA [This is the length of the unprocessed precursor]

Molecular weight: 17026 Da [This is the MW of the unprocessed precursor]

CRC64: C6ECD92DCA9B37BC [This is a checksum on the sequence]

        10         20         30         40         50         60 
MGKISSLPTQ LFKCCFCDFL KVKMHTMSSS HLFYLALCLL TFTSSATAGP ETLCGAELVD 

        70         80         90        100        110        120 
ALQFVCGDRG FYFNKPTGYG SSSRRAPQTG IVDECCFRSC DLRRLEMYCA PLKPAKSARS 

       130        140        150 
VRAQRHTDMP KTQKEVHLKN ASRGSAGNKN YRM

P01343 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools