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PR01981

Identifier
IGFBPFAMILY5  [View Relations]  [View Alignment]  
Accession
PR01981
No. of Motifs
3
Creation Date
11-JUN-2009
Title
Insulin-like growth factor-binding protein 5 signature
Database References
PRINTS; PR01976 IGFBPFAMILY
INTERPRO; IPR012213
PDB; 1H59; 1BOE
SCOP; 1H59; 1BOE
CATH; 1H59; 1BOE
MIM; 146734
Literature References
1. STEWART, C. AND ROTWEIN, P.
Growth, differentiation and survival: multiple physiological functions for
insulin-like growth factors.
PHYSIOL.REV. 76 1005-1026 (1996).
 
2. HWA, V., OH, Y. AND ROSENFELD, R.
The Insulin-Like Growth Factor-Binding Protein (IGFBP) Superfamily.
ENDOCR.REV. 20 761-787 (1999).
 
3. OH, Y., MULLER. H., PHAM, H. AND ROSENFELD, R.
Demonstration of receptors for insulin-like growth factor binding
protein-3 on Hs578T human breast cancer cells.
J.BIOL.CHEM. 268 26045-26048 (1993).
 
4. ANDRESS, D.
Heparin modulates the binding of insulin-like growth factor (IGF) binding
protein-5 to a membrane protein in osteoblastic cells.
J.BIOL.CHEM. 270 28289-28296 (1995).
 
5. MOHAN, S., NAKAO, Y., HONDA, Y., LANDALE, E., LESSER, U., DONY, C.,
LANG, K. AND BAYLINK, D.
Studies on the mechanisms by which insulin-like growth factor (IGF) binding
protein-4 (IGFBP-4) and IGFBP-5 modulate IGF actions in bone cells.
J.BIOL.CHEM.270 20424-20431 (1995).
 
6. RAJAH, R., VALENTINIS, B. AND COHEN, P.
Insulin-like growth factor (IGF)-binding protein-3 induces apoptosis and
mediates the effects of transforming growth factor-beta1 on programmed cell
death through a p53- and IGF-independent mechanism.
J.BIOL.CHEM. 272 12181-12188 (1997).
 
7. SCHNEIDER, M., WOLF, E., HOEFLICH, A. AND LAHM, H. 
IGF-binding protein-5: flexible player in the IGF system and effector on 
its own. 
J.ENDOCRINOL. 172 423-440 (2002).
 
8. SCHEDLICH, L., YOUNG, T., FIRTH, S. AND BAXTER, R. 
Insulin-like growth factor-binding protein (IGFBP)-3 and IGFBP-5 share a 
common nuclear transport pathway in T47D human breast carcinoma cells. 
J.BIOL.CHEM. 273 18347-18352 (1998).

Documentation
Insulin-like growth factors (IGFs)-I and -II are small secreted peptides
that stimulate the survival, and promote the proliferation and
differentiation, of many cell types [1]. In biological fluids, these growth
factors are usually bound to IGF binding proteins (IGFBPs), which regulate
their availability and activity by prolonging their half-life and
modulating their receptor interactions.
 
To date, six IGFBP family members have been identified (termed IGFBP1-6)
[2]. They share a conserved gene (intron-exon) organisation and high IGF
binding affinity. Structurally, the proteins also share a common domain
architecture, possessing a conserved N-terminal IGFBP domain, a highly
variable mid-section, and a thyroglobulin type-1 (Tg1) domain in their
C-terminal regions.
 
In addition to their role in the regulation of IGF activity, there is
evidence for the direct association of IGFBPs with a variety of
extracellular and cell surface molecules [3,4], with consequent effects
upon important biological processes. These include modulation of bone cell
proliferation [5], and growth arrest of breast and prostate cancer cells
[3,6].
 
IGFBP5 is an essential regulator of physiological processes in bone, kidney
and mammary gland [7]. In common with IGFBP3, IGFBP5 contains a putative 
nuclear localisation signal in its C-terminal region, consistent with its
translocation to the nucleus of human breast cancer cells [8].
 
IGFBPFAMILY5 is a 3-element fingerprint that provides a signature for
insulin-like growth factor-binding protein 5. The fingerprint was derived 
from an initial alignment of 6 sequences: the motifs were drawn from
conserved regions in the N- and C-terminal thirds of the alignment, 
focusing on those sections that characterise IGFBP5 but distinguish it from
other family members - motif 1 lies within the IGFBP domain, and motifs 2 
and 3 reside within the Tg1 domain. Two iterations on SPTR57_40f were 
required to reach convergence, at which point a true set comprising 13 
sequences was identified.
Summary Information
13 codes involving  3 elements
0 codes involving 2 elements
Composite Feature Index
3131313
2000
123
True Positives
A5PLA3_DANRE  B0S525_DANRE  B3GS77_SHEEP  IBP5_BOVIN    
IBP5_HUMAN IBP5_MOUSE IBP5_PIG IBP5_RAT
IBP5_XENLA Q0IJ34_XENTR Q3HNB1_ONCMY Q3UQV0_MOUSE
Q800E1_DANRE
Sequence Titles
A5PLA3_DANRE Zgc:165472 protein - Danio rerio (Zebrafish) (Brachydanio rerio). 
B0S525_DANRE Insulin-like growth factor binding protein 5 - Danio rerio (Zebrafish) (Brachydanio rerio).
B3GS77_SHEEP Insulin-like growth factor-binding protein-5 - Ovis aries (Sheep).
IBP5_BOVIN Insulin-like growth factor-binding protein 5 - Bos taurus (Bovine).
IBP5_HUMAN Insulin-like growth factor-binding protein 5 - Homo sapiens (Human).
IBP5_MOUSE Insulin-like growth factor-binding protein 5 - Mus musculus (Mouse).
IBP5_PIG Insulin-like growth factor-binding protein 5 - Sus scrofa (Pig).
IBP5_RAT Insulin-like growth factor-binding protein 5 - Rattus norvegicus (Rat).
IBP5_XENLA Insulin-like growth factor-binding protein 5 - Xenopus laevis (African clawed frog).
Q0IJ34_XENTR Putative uncharacterized protein - Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
Q3HNB1_ONCMY Insulin-like growth factor binding protein 5 - Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
Q3UQV0_MOUSE Putative uncharacterized protein - Mus musculus (Mouse).
Q800E1_DANRE Insulin-like growth factor binding protein 5 - Danio rerio (Zebrafish) (Brachydanio rerio).
Scan History
SPTR57_40f 2  300  NSINGLE    
Initial Motifs
Motif 1  width=13
Element Seqn Id St Int Rpt
LSMCPPSPLGCEL IBP5_PIG 34 34 -
LSMCPPSPLGCEL IBP5_BOVIN 34 34 -
MSMCPPTPVGCEL IBP5_XENLA 36 36 -
MSMCPPTPVGCEL Q0IJ34_XENTR 35 35 -
LSMCPPVPVGCQL Q3HNB1_ONCMY 33 33 -
MSMCPPVRNGCQV A5PLA3_DANRE 33 33 -

Motif 2 width=14
Element Seqn Id St Int Rpt
KASPRMVPRAVYLP IBP5_PIG 203 156 -
KASPRMVPRAVYLP IBP5_BOVIN 203 156 -
KLSHRVYPRAFYLP IBP5_XENLA 197 148 -
KLSHRVYPRAFYLP Q0IJ34_XENTR 193 145 -
KDTSRVMALSLYLP Q3HNB1_ONCMY 201 155 -
KDTSRVMALSLYLP A5PLA3_DANRE 198 152 -

Motif 3 width=14
Element Seqn Id St Int Rpt
EYVDGDFQCHSFDS IBP5_PIG 254 37 -
EYVDGDFQCHTFDS IBP5_BOVIN 254 37 -
DYVNGDLQCHSFDS IBP5_XENLA 248 37 -
DYVNGDLQCHSFDS Q0IJ34_XENTR 244 37 -
DYSGGDIQCKDLES Q3HNB1_ONCMY 252 37 -
DFNGGNIQCKEVES A5PLA3_DANRE 249 37 -
Final Motifs
Motif 1  width=13
Element Seqn Id St Int Rpt
LSMCPPSPLGCEL B3GS77_SHEEP 34 34 -
LSMCPPSPLGCEL Q3UQV0_MOUSE 34 34 -
LSMCPPSPLGCEL IBP5_RAT 34 34 -
LSMCPPSPLGCEL IBP5_PIG 34 34 -
LSMCPPSPLGCEL IBP5_MOUSE 34 34 -
LSMCPPSPLGCEL IBP5_HUMAN 35 35 -
LSMCPPSPLGCEL IBP5_BOVIN 34 34 -
MSMCPPTPVGCEL IBP5_XENLA 36 36 -
MSMCPPTPVGCEL Q0IJ34_XENTR 35 35 -
LSMCPPVPVGCQL Q3HNB1_ONCMY 33 33 -
LSMCPPVPVGCQL B0S525_DANRE 31 31 -
LSMCPPVPVGCQL Q800E1_DANRE 31 31 -
MSMCPPVRNGCQV A5PLA3_DANRE 33 33 -

Motif 2 width=14
Element Seqn Id St Int Rpt
KASPRMVPRAVYLP B3GS77_SHEEP 203 156 -
KASPRMVPRAVYLP Q3UQV0_MOUSE 203 156 -
KASPRMVPRAVYLP IBP5_RAT 203 156 -
KASPRMVPRAVYLP IBP5_PIG 203 156 -
KASPRMVPRAVYLP IBP5_MOUSE 203 156 -
KASPRMVPRAVYLP IBP5_HUMAN 204 156 -
KASPRMVPRAVYLP IBP5_BOVIN 203 156 -
KLSHRVYPRAFYLP IBP5_XENLA 197 148 -
KLSHRVYPRAFYLP Q0IJ34_XENTR 193 145 -
KDTSRVMALSLYLP Q3HNB1_ONCMY 201 155 -
KDTSRVMALSLYLP B0S525_DANRE 195 151 -
KDTSRVMALSLYLP Q800E1_DANRE 195 151 -
KDTSRVMALSLYLP A5PLA3_DANRE 198 152 -

Motif 3 width=14
Element Seqn Id St Int Rpt
EYVDGDFQCHTFDS B3GS77_SHEEP 254 37 -
EYVDGDFQCHAFDS Q3UQV0_MOUSE 254 37 -
EYVDGDFQCHAFDS IBP5_RAT 254 37 -
EYVDGDFQCHSFDS IBP5_PIG 254 37 -
EYVDGDFQCHAFDS IBP5_MOUSE 254 37 -
EYVDGDFQCHTFDS IBP5_HUMAN 255 37 -
EYVDGDFQCHTFDS IBP5_BOVIN 254 37 -
DYVNGDLQCHSFDS IBP5_XENLA 248 37 -
DYVNGDLQCHSFDS Q0IJ34_XENTR 244 37 -
DYSGGDIQCKDLES Q3HNB1_ONCMY 252 37 -
DYSGGNIQCKDLEN B0S525_DANRE 246 37 -
DYSGGNIQCKDLEN Q800E1_DANRE 246 37 -
DFNGGNIQCKEVES A5PLA3_DANRE 249 37 -