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P01346 (IGF2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Insulin-like growth factor II

Short name=IGF-II
Alternative name(s):
Multiplication-stimulating activity
Short name=MSA
Multiplication-stimulating polypeptide

Cleaved into the following 2 chains:

  1. Insulin-like growth factor II
  2. Preptin
Gene names
Name:Igf2
Synonyms:Igf-2
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length180 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The insulin-like growth factors possess growth-promoting activity. In vitro, they are potent mitogens for cultured cells. IGF-II is influenced by placental lactogen and may play a role in fetal development. Ref.9

Preptin undergoes glucose-mediated co-secretion with insulin, and acts as physiological amplifier of glucose-mediated insulin secretion. Exhibits osteogenic properties by increasing osteoblast mitogenic activity through phosphoactivation of MAPK1 and MAPK3. Ref.9

Subcellular location

Secreted.

Sequence similarities

Belongs to the insulin family.

Sequence caution

The sequence AAB95624.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAA25427.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAA25429.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Glucose metabolism
Osteogenesis
   Cellular componentSecreted
   DomainSignal
   Molecular functionGrowth factor
Hormone
Mitogen
   PTMCleavage on pair of basic residues
Disulfide bond
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcell proliferation

Traceable author statement Ref.4. Source: RGD

cellular response to mechanical stimulus

Inferred from expression pattern PubMed 20695079. Source: RGD

exocrine pancreas development

Inferred from electronic annotation. Source: Ensembl

female pregnancy

Inferred from expression pattern PubMed 19776249. Source: RGD

glucose metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

insulin receptor signaling pathway via phosphatidylinositol 3-kinase

Inferred from electronic annotation. Source: Ensembl

memory

Inferred from mutant phenotype PubMed 21270887. Source: RGD

organ morphogenesis

Inferred from electronic annotation. Source: Ensembl

osteoblast differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of MAPK cascade

Inferred from electronic annotation. Source: Ensembl

positive regulation of activated T cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell division

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of glycogen (starch) synthase activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of glycogen biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of insulin receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of mitosis

Inferred from electronic annotation. Source: Ensembl

positive regulation of peptidyl-tyrosine phosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein kinase B signaling

Inferred from electronic annotation. Source: Ensembl

positive regulation of steroid hormone biosynthetic process

Inferred from direct assay PubMed 17023532. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from direct assay PubMed 18778817. Source: RGD

response to estradiol

Inferred from expression pattern PubMed 18946176. Source: RGD

response to ethanol

Inferred from expression pattern PubMed 18505416. Source: RGD

response to nicotine

Inferred from direct assay PubMed 19494366. Source: RGD

response to nutrient levels

Inferred from expression pattern PubMed 17626604. Source: RGD

response to organic cyclic compound

Inferred from direct assay PubMed 17407073. Source: RGD

response to radiation

Inferred from expression pattern PubMed 17630476. Source: RGD

striated muscle cell differentiation

Inferred from electronic annotation. Source: Ensembl

wound healing

Inferred from expression pattern PubMed 7770004. Source: RGD

   Cellular_componentextracellular space

Inferred from direct assay Ref.6. Source: RGD

   Molecular_functiongrowth factor activity

Traceable author statement Ref.4. Source: RGD

protein binding

Inferred from physical interaction PubMed 2538475PubMed 2974285. Source: UniProtKB

protein serine/threonine kinase activator activity

Inferred from electronic annotation. Source: Ensembl

receptor activator activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Ref.8
Chain25 – 9167Insulin-like growth factor II
PRO_0000015729
Propeptide92 – 18089E peptide
PRO_0000015730
Peptide93 – 12634Preptin
PRO_0000370380

Regions

Region25 – 5228B
Region53 – 6412C
Region65 – 8521A
Region86 – 916D

Amino acid modifications

Disulfide bond33 ↔ 71 By similarity
Disulfide bond45 ↔ 84 By similarity
Disulfide bond70 ↔ 75 By similarity

Experimental info

Sequence conflict1 – 88Missing Ref.2
Sequence conflict571S → G Ref.3

Sequences

Sequence LengthMass (Da)Tools
P01346 [UniParc].

Last modified March 20, 1987. Version 1.
Checksum: AF12B4EEC0DBCC34

FASTA18020,086
        10         20         30         40         50         60 
MGIPVGKSML VLLISLAFAL CCIAAYRPSE TLCGGELVDT LQFVCSDRGF YFSRPSSRAN 

        70         80         90        100        110        120 
RRSRGIVEEC CFRSCDLALL ETYCATPAKS ERDVSTSQAV LPDDFPRYPV GKFFKFDTWR 

       130        140        150        160        170        180 
QSAGRLRRGL PALLRARRGR MLAKELEAFR EAKRHRPLIV LPPKDPAHGG ASSEMSSNHQ 

« Hide

References

[1]"Insulin-like growth factor II precursor gene organization in relation to insulin gene family."
Dull T.J., Gray A., Hayflick J.S., Ullrich A.
Nature 310:777-781(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: BRL-3A.
[2]"Developmental and tissue-specific expression of a family of transcripts related to rat insulin-like growth factor II mRNA."
Soares M.B., Ishii D.N., Efstratiadis A.
Nucleic Acids Res. 13:1119-1134(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Buffalo.
[3]"Rat insulin-like growth factor II gene. A single gene with two promoters expressing a multitranscript family."
Soares M.B., Turken A., Ishii D.N., Mills L., Episkopou V., Cotter S., Zeitlin S., Efstratiadis A.
J. Mol. Biol. 192:737-752(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
[4]"Structure and expression of the rat insulin-like growth factor II (rIGF-II) gene. rIGF-II RNAs are transcribed from two promoters."
Frunzio R., Chiariotti L., Brown A.L., Graham D.E., Rechler M.M., Bruni C.B.
J. Biol. Chem. 261:17138-17149(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"Transcriptional deviation of the rat insulin-like growth factor II gene initiated at three alternative leader-exons between neonatal tissues and ascites hepatomas."
Ueno T., Takahashi K., Matsuguchi T., Endo H., Yamamoto M.
Biochim. Biophys. Acta 950:411-419(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
[6]"Isolation of a cDNA clone encoding rat insulin-like growth factor-II precursor."
Whitfield H.J., Bruni C.B., Frunzio R., Terrell J.E., Nissley S.P., Rechler M.M.
Nature 312:277-280(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 62-180.
[7]"Structure of the rat insulin-like growth factor II transcriptional unit: heterogeneous transcripts are generated from two promoters by use of multiple polyadenylation sites and differential ribonucleic acid splicing."
Chiariotti L., Brown A.L., Frunzio R., Clemmons D.R., Rechler M.M., Bruni C.B.
Mol. Endocrinol. 2:1115-1126(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 103-180.
[8]"Purification and primary structure of a polypeptide with multiplication-stimulating activity from rat liver cell cultures. Homology with human insulin-like growth factor II."
Marquardt H., Todaro G.J., Henderson L.E., Oroszlan S.
J. Biol. Chem. 256:6859-6865(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 25-91.
[9]"Preptin, another peptide product of the pancreatic beta-cell, is osteogenic in vitro and in vivo."
Cornish J., Callon K.E., Bava U., Watson M., Xu X., Lin J.M., Chan V.A., Grey A.B., Naot D., Buchanan C.M., Cooper G.J., Reid I.R.
Am. J. Physiol. 292:E117-E122(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: OSTEOGENIC FUNCTION OF PREPTIN.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X00911 mRNA. Translation: CAA25428.1.
X00911 mRNA. Translation: CAA25427.1. Different initiation.
X00911 mRNA. Translation: CAA25429.1. Different initiation.
M13871, M13869, M13870 Genomic DNA. Translation: AAB95624.1. Different initiation.
M29880, M29879 Genomic DNA. Translation: AAA41391.1.
X02213 mRNA. Translation: CAA26136.1.
X13101 mRNA. Translation: CAA31493.1.
X14833 mRNA. Translation: CAA32942.1.
X14834 mRNA. Translation: CAA32943.1.
M30273 mRNA. Translation: AAA41432.1.
M31221 Genomic DNA. Translation: AAA42046.1.
PIRIGRT2. A25350.
RefSeqNP_001177091.1. NM_001190162.1.
NP_001177092.1. NM_001190163.1.
NP_113699.2. NM_031511.2.
XP_006230727.1. XM_006230665.1.
UniGeneRn.118681.
Rn.224460.

3D structure databases

ProteinModelPortalP01346.
SMRP01346. Positions 25-91.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP01346. 1 interaction.
STRING10116.ENSRNOP00000047037.

Proteomic databases

PaxDbP01346.
PRIDEP01346.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000050760; ENSRNOP00000047037; ENSRNOG00000020369.
ENSRNOT00000073850; ENSRNOP00000066983; ENSRNOG00000020369.
GeneID24483.
KEGGrno:24483.
UCSCRGD:2870. rat.

Organism-specific databases

CTD3481.
RGD2870. Igf2.

Phylogenomic databases

eggNOGNOG44017.
GeneTreeENSGT00530000063856.
HOGENOMHOG000233362.
HOVERGENHBG006137.
InParanoidP01346.
KOK13769.
OrthoDBEOG7TF7CG.
PhylomeDBP01346.
TreeFamTF332820.

Gene expression databases

ArrayExpressP01346.
GenevestigatorP01346.

Family and domain databases

Gene3D1.10.100.10. 1 hit.
InterProIPR022334. IGF2.
IPR013576. IGF2_C.
IPR016179. Insulin-like.
IPR022350. Insulin-like_growth_factor.
IPR022353. Insulin_CS.
IPR022352. Insulin_family.
[Graphical view]
PfamPF08365. IGF2_C. 1 hit.
PF00049. Insulin. 1 hit.
[Graphical view]
PRINTSPR02002. INSLNLIKEGF.
PR02006. INSLNLIKEGF2.
PR00276. INSULINFAMLY.
ProDomPD005188. IGF2_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00078. IlGF. 1 hit.
[Graphical view]
SUPFAMSSF56994. SSF56994. 1 hit.
PROSITEPS00262. INSULIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio603459.
PROP01346.

Entry information

Entry nameIGF2_RAT
AccessionPrimary (citable) accession number: P01346
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: March 20, 1987
Last modified: July 9, 2014
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families