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P12843 (IBP2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 120. 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-binding protein 2

Short name=IBP-2
Short name=IGF-binding protein 2
Short name=IGFBP-2
Alternative name(s):
BRL-BP
Gene names
Name:Igfbp2
Synonyms:Igfbp-2
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length304 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Inhibits IGF-mediated growth and developmental rates By similarity. IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors.

Subunit structure

Binds IGF2 more than IGF1.

Subcellular location

Secreted Ref.1 Ref.4 Ref.5.

Tissue specificity

In adults, expressed in brain, testes, ovaries, and kidney. Expression in the adult liver is barely detectable. Ref.2

Developmental stage

Predominantly expressed at fetal stages with highest expression in fetal liver. Also expressed in fetal kidney, intestine and lung, as well as muscle, heart and stomach. Ref.1 Ref.2

Domain

The C-terminus is required for IGF-binding and growth inhibition. Ref.6

Post-translational modification

O-glycosylated By similarity.

Sequence similarities

Contains 1 IGFBP N-terminal domain.

Contains 1 thyroglobulin type-1 domain.

Ontologies

Keywords
   Biological processGrowth regulation
   Cellular componentSecreted
   DomainSignal
   LigandGrowth factor binding
   Molecular functionDevelopmental protein
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processaging

Inferred from expression pattern PubMed 10191834. Source: RGD

cellular response to hormone stimulus

Inferred from expression pattern PubMed 16720626. Source: RGD

female pregnancy

Inferred from expression pattern PubMed 17123939. Source: RGD

multicellular organismal development

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of activated T cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of cell growth

Inferred from electronic annotation. Source: InterPro

regulation of insulin-like growth factor receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

response to drug

Inferred from expression pattern PubMed 15613074. Source: RGD

response to estradiol

Inferred from expression pattern PubMed 10842239. Source: RGD

response to estrogen

Inferred from expression pattern PubMed 12801995. Source: RGD

response to glucocorticoid

Inferred from expression pattern PubMed 15705658. Source: RGD

response to lithium ion

Inferred from expression pattern PubMed 16738484. Source: RGD

response to mechanical stimulus

Inferred from expression pattern PubMed 17308996. Source: RGD

response to nutrient

Inferred from expression pattern PubMed 15576465. Source: RGD

response to retinoic acid

Inferred from expression pattern PubMed 11880314. Source: RGD

response to steroid hormone

Inferred from expression pattern PubMed 10842239. Source: RGD

signal transduction

Inferred from expression pattern PubMed 11914028. Source: RGD

   Cellular_componentapical plasma membrane

Inferred from direct assay PubMed 10842239. Source: RGD

cytoplasmic vesicle

Inferred from direct assay PubMed 15705658. Source: RGD

extracellular region

Inferred from direct assay Ref.5Ref.4. Source: UniProtKB

extracellular space

Inferred from direct assay Ref.1PubMed 9396554. Source: RGD

   Molecular_functioninsulin-like growth factor I binding

Inferred from direct assay Ref.1. Source: UniProtKB

insulin-like growth factor II binding

Inferred from physical interaction Ref.1Ref.6. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3434 Ref.4
Chain35 – 304270Insulin-like growth factor-binding protein 2
PRO_0000014373

Regions

Domain36 – 11883IGFBP N-terminal
Domain203 – 28583Thyroglobulin type-1
Motif280 – 2823Cell attachment site

Amino acid modifications

Disulfide bond206 ↔ 240 By similarity
Disulfide bond251 ↔ 262 By similarity
Disulfide bond264 ↔ 285 By similarity

Experimental info

Sequence conflict2981A → V in AAA40829. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P12843 [UniParc].

Last modified May 1, 2007. Version 3.
Checksum: 8558B7E2C9152B9F

FASTA30432,855
        10         20         30         40         50         60 
MLPRLGGPAL PLLLPSLLLL LLLGAGGCGP GVRAEVLFRC PPCTPERLAA CGPPPDAPCA 

        70         80         90        100        110        120 
ELVREPGCGC CSVCARQEGE ACGVYIPRCA QTLRCYPNPG SELPLKALVT GAGTCEKRRV 

       130        140        150        160        170        180 
GATPQQVADS EDDHSEGGLV ENHVDGTMNM LGGSSAGRKP PKSGMKELAV FREKVNEQHR 

       190        200        210        220        230        240 
QMGKGAKHLS LEEPKKLRPP PARTPCQQEL DQVLERISTM RLPDDRGPLE HLYSLHIPNC 

       250        260        270        280        290        300 
DKHGLYNLKQ CKMSLNGQRG ECWCVNPNTG KPIQGAPTIR GDPECHLFYN EQQENDGAHA 


QRVQ 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence and expression of a cDNA clone encoding a fetal rat binding protein for insulin-like growth factors."
Brown A.L., Chiariotti L., Orlowski C.C., Mehlman T., Burgers W.H., Ackerman E.J., Bruni C.B., Rechler M.M.
J. Biol. Chem. 264:5148-5154(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, INTERACTION WITH IGF1 AND IGF2, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
[2]"A low molecular weight insulin-like growth factor binding protein from rat: cDNA cloning and tissue distribution of its messenger RNA."
Margot J.B., Binkert C., Mary J.-L., Landwehr J., Heinrich G., Schwander J.
Mol. Endocrinol. 3:1053-1060(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Tissue: Liver.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Ovary.
[4]"Identification of a novel binding protein for insulin-like growth factors in adult rat serum."
Shimonaka M., Schroeder R., Shimasaki S., Ling N.
Biochem. Biophys. Res. Commun. 165:189-195(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 35-64, SUBCELLULAR LOCATION.
Tissue: Serum.
[5]"Purification and amino-terminal sequence of an insulin-like growth factor-binding protein secreted by rat liver BRL-3A cells."
Mottola C., Macdonald R.G., Brackett J.L., Mole J.E., Anderson J.K., Czech M.P.
J. Biol. Chem. 261:11180-11188(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 38-68, SUBCELLULAR LOCATION.
[6]"Isolation of a biologically active fragment from the carboxy terminus of the fetal rat binding protein for insulin-like growth factors."
Wang J.F., Hampton B., Mehlman T., Burgess W.H., Rechler M.M.
Biochem. Biophys. Res. Commun. 157:718-726(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 178-204, INTERACTION WITH IGF2, DOMAIN.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J04486 mRNA. Translation: AAA40829.1.
M31672 mRNA. Translation: AAA41381.1.
BC092570 mRNA. Translation: AAH92570.1.
PIRA33274.
RefSeqNP_037254.2. NM_013122.2.
UniGeneRn.6813.

3D structure databases

ProteinModelPortalP12843.
SMRP12843. Positions 199-304.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSI31.953.

PTM databases

PhosphoSiteP12843.

Proteomic databases

PRIDEP12843.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000023068; ENSRNOP00000023068; ENSRNOG00000016957.
GeneID25662.
KEGGrno:25662.

Organism-specific databases

CTD3485.
RGD2873. Igfbp2.

Phylogenomic databases

eggNOGNOG47500.
GeneTreeENSGT00550000074457.
HOGENOMHOG000253012.
HOVERGENHBG002631.
InParanoidP12843.
OMAGAGTCEK.
OrthoDBEOG74N5HG.
PhylomeDBP12843.
TreeFamTF331211.

Gene expression databases

ArrayExpressP12843.
GenevestigatorP12843.

Family and domain databases

Gene3D4.10.40.20. 1 hit.
4.10.800.10. 1 hit.
InterProIPR009030. Growth_fac_rcpt_N_dom.
IPR012210. IGFBP-2.
IPR000867. IGFBP-like.
IPR009168. IGFBP1-6.
IPR022321. IGFBP_1-6_chordata.
IPR017891. Insulin_GF-bd_Cys-rich_CS.
IPR000716. Thyroglobulin_1.
[Graphical view]
PANTHERPTHR11551. PTHR11551. 1 hit.
PTHR11551:SF5. PTHR11551:SF5. 1 hit.
PfamPF00219. IGFBP. 1 hit.
PF00086. Thyroglobulin_1. 1 hit.
[Graphical view]
PRINTSPR01976. IGFBPFAMILY.
PR01978. IGFBPFAMILY2.
SMARTSM00121. IB. 1 hit.
SM00211. TY. 1 hit.
[Graphical view]
SUPFAMSSF57184. SSF57184. 1 hit.
SSF57610. SSF57610. 1 hit.
PROSITEPS00222. IGFBP_N_1. 1 hit.
PS51323. IGFBP_N_2. 1 hit.
PS00484. THYROGLOBULIN_1_1. 1 hit.
PS51162. THYROGLOBULIN_1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio607569.
PROP12843.

Entry information

Entry nameIBP2_RAT
AccessionPrimary (citable) accession number: P12843
Secondary accession number(s): Q569C7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: May 1, 2007
Last modified: April 16, 2014
This is version 120 of the entry and version 3 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