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P24594 (IBP5_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 123. 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 5

Short name=IBP-5
Short name=IGF-binding protein 5
Short name=IGFBP-5
Gene names
Name:Igfbp5
Synonyms:Igfbp-5
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length271 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subcellular location

Secreted.

Tissue specificity

Mostly in kidney.

Sequence similarities

Contains 1 IGFBP N-terminal domain.

Contains 1 thyroglobulin type-1 domain.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   LigandGrowth factor binding
   PTMDisulfide bond
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to cAMP

Inferred from electronic annotation. Source: Ensembl

glucose homeostasis

Inferred from electronic annotation. Source: Ensembl

glucose metabolic process

Inferred from electronic annotation. Source: Ensembl

hair follicle morphogenesis

Inferred from electronic annotation. Source: Ensembl

intracellular signal transduction

Inferred from expression pattern PubMed 12193414. Source: RGD

mammary gland involution

Inferred from electronic annotation. Source: Ensembl

negative regulation of insulin-like growth factor receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of osteoblast differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of smooth muscle cell migration

Inferred from electronic annotation. Source: Ensembl

negative regulation of smooth muscle cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of translation

Inferred from electronic annotation. Source: Ensembl

osteoblast differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of insulin-like growth factor receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein kinase B signaling

Inferred from electronic annotation. Source: Ensembl

regulation of cell growth

Inferred from electronic annotation. Source: Ensembl

regulation of glucose metabolic process

Inferred from electronic annotation. Source: Ensembl

skeletal muscle tissue growth

Inferred from expression pattern PubMed 12397024. Source: RGD

striated muscle cell differentiation

Inferred from electronic annotation. Source: Ensembl

type B pancreatic cell proliferation

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioninsulin-like growth factor binding

Inferred from direct assay Ref.1. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 271252Insulin-like growth factor-binding protein 5
PRO_0000014388

Regions

Domain22 – 10281IGFBP N-terminal
Domain188 – 26275Thyroglobulin type-1

Amino acid modifications

Disulfide bond44 ↔ 58 By similarity
Disulfide bond66 ↔ 79 By similarity
Disulfide bond191 ↔ 218 By similarity
Disulfide bond229 ↔ 240 By similarity
Disulfide bond242 ↔ 262 By similarity

Sequences

Sequence LengthMass (Da)Tools
P24594 [UniParc].

Last modified March 1, 1992. Version 1.
Checksum: 545B4C48F9BB5493

FASTA27130,298
        10         20         30         40         50         60 
MVISVVLLLL AACAVPAQGL GSFVHCEPCD EKALSMCPPS PLGCELVKEP GCGCCMTCAL 

        70         80         90        100        110        120 
AEGQSCGVYT ERCAQGLRCL PRQDEEKPLH ALLHGRGVCL NEKSYGEQTK IERDSREHEE 

       130        140        150        160        170        180 
PTTSEMAEET YSPKVFRPKH TRISELKAEA VKKDRRKKLT QSKFVGGAEN TAHPRVIPAP 

       190        200        210        220        230        240 
EMRQESDQGP CRRHMEASLQ EFKASPRMVP RAVYLPNCDR KGFYKRKQCK PSRGRKRGIC 

       250        260        270 
WCVDKYGMKL PGMEYVDGDF QCHAFDSSNV E 

« Hide

References

[1]"Identification of five different insulin-like growth factor binding proteins (IGFBPs) from adult rat serum and molecular cloning of a novel IGFBP-5 in rat and human."
Shimasaki S., Shimonaka M., Zhang H.-P., Ling N.
J. Biol. Chem. 266:10646-10653(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-53.
Tissue: Ovary.
[2]"Cloning of the rat insulin-like growth factor binding protein-5 gene and DNA sequence analysis of its promoter region."
Zhu X., Ling N., Shimasaki S.
Biochem. Biophys. Res. Commun. 190:1045-1052(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Sprague-Dawley.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M62781 mRNA. Translation: AAA53533.1.
L08275 Genomic DNA. No translation available.
PIRJC1463.
RefSeqNP_036949.1. NM_012817.1.
UniGeneRn.1593.

3D structure databases

ProteinModelPortalP24594.
SMRP24594. Positions 24-104.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-204226.
STRING10116.ENSRNOP00000023530.

Protein family/group databases

MEROPSI31.952.

Proteomic databases

PRIDEP24594.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000023530; ENSRNOP00000023530; ENSRNOG00000017206.
GeneID25285.
KEGGrno:25285.
UCSCRGD:2876. rat.

Organism-specific databases

CTD3488.
RGD2876. Igfbp5.

Phylogenomic databases

eggNOGNOG42882.
GeneTreeENSGT00550000074457.
HOGENOMHOG000253012.
HOVERGENHBG002631.
InParanoidP24594.
OMAYREQAKI.
OrthoDBEOG74N5HG.
PhylomeDBP24594.
TreeFamTF331211.

Gene expression databases

GenevestigatorP24594.

Family and domain databases

Gene3D4.10.40.20. 1 hit.
4.10.800.10. 1 hit.
InterProIPR009030. Growth_fac_rcpt_N_dom.
IPR012213. IGFBP-5.
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:SF4. PTHR11551:SF4. 1 hit.
PfamPF00219. IGFBP. 1 hit.
PF00086. Thyroglobulin_1. 1 hit.
[Graphical view]
PRINTSPR01976. IGFBPFAMILY.
PR01981. IGFBPFAMILY5.
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

NextBio606017.
PROP24594.

Entry information

Entry nameIBP5_RAT
AccessionPrimary (citable) accession number: P24594
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: March 1, 1992
Last modified: April 16, 2014
This is version 123 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