ID:FBLN3_HUMAN DESCRIPTION: RecName: Full=EGF-containing fibulin-like extracellular matrix protein 1; AltName: Full=Extracellular protein S1-5; AltName: Full=Fibrillin-like protein; AltName: Full=Fibulin-3; Short=FIBL-3; Flags: Precursor; FUNCTION: Binds EGFR, the EGF receptor, inducing EGFR autophosphorylation and the activation of downstream signaling pathways. May play a role in cell adhesion and migration. May function as a negative regulator of chondrocyte differentiation. In the olfactory epithelium, it may regulate glial cell migration, differentiation and the ability of glial cells to support neuronal neurite outgrowth. SUBUNIT: Interacts with ECM1. Interacts with TIMP3. INTERACTION: P10398:ARAF; NbExp=3; IntAct=EBI-536772, EBI-365961; P54259:ATN1; NbExp=3; IntAct=EBI-536772, EBI-945980; SUBCELLULAR LOCATION: Secreted, extracellular space (By similarity). Secreted, extracellular space, extracellular matrix (By similarity). Note=Localizes to the lamina propria underneath the olfactory epithelium (By similarity). TISSUE SPECIFICITY: In the eye, associated with photoreceptor outer and inner segment regions, the nerve fiber layer, outer nuclear layer and inner and outer plexiform layers of the retina. DISEASE: Defects in EFEMP1 are a cause of Doyne honeycomb retinal dystrophy (DHRD) [MIM:126600]; also known as malattia leventinese (MLVT) (ML). DHRD is an autosomal dominant disease characterized by yellow-white deposits known as drusen that accumulate beneath the retinal pigment epithelium. MISCELLANEOUS: Up-regulated in malignant gliomas. May increase glioma cell adhesiveness and invasive properties. SIMILARITY: Belongs to the fibulin family. SIMILARITY: Contains 6 EGF-like domains. WEB RESOURCE: Name=Mutations of the EFEMP1 gene; Note=Retina International's Scientific Newsletter; URL="http://www.retina-international.org/files/sci-news/efempmut.htm"; WEB RESOURCE: Name=GeneReviews; URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/EFEMP1";
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on Q12805
Front
Top
Side
The pictures above may be empty if there is no ModBase structure for the protein. The ModBase structure frequently covers just a fragment of the protein. You may be asked to log onto ModBase the first time you click on the pictures. It is simplest after logging in to just click on the picture again to get to the specific info on that model.
Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
US Server
Sequence and Links to Tools and Databases 
Common Gene Haplotype Alleles 
