O35568 · FBLN3_RAT

  • Protein
    EGF-containing fibulin-like extracellular matrix protein 1
  • Gene
    Efemp1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

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.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentbasement membrane
Cellular Componentextracellular space
Molecular Functioncalcium ion binding
Molecular Functionepidermal growth factor receptor activity
Molecular Functionepidermal growth factor receptor binding
Molecular Functiongrowth factor activity
Biological Processcamera-type eye development
Biological Processembryonic eye morphogenesis
Biological Processepidermal growth factor receptor signaling pathway
Biological Processnegative regulation of chondrocyte differentiation
Biological Processnegative regulation of neuron projection development
Biological Processpeptidyl-tyrosine phosphorylation
Biological Processpositive regulation of cell population proliferation
Biological Processpositive regulation of cell projection organization
Biological Processpost-embryonic eye morphogenesis
Biological Processregulation of DNA-templated transcription
Biological Processregulation of glial cell migration

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    EGF-containing fibulin-like extracellular matrix protein 1
  • Alternative names
    • Fibulin-3 (FIBL-3)
    • T16 protein

Gene names

    • Name
      Efemp1
    • Synonyms
      Fbln3

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus

Accessions

  • Primary accession
    O35568

Proteomes

Organism-specific databases

Subcellular Location

Note: Localizes to the lamina propria underneath the olfactory epithelium.

Keywords

PTM/Processing

Features

Showing features for signal, chain, disulfide bond, glycosylation.

TypeIDPosition(s)Description
Signal1-17
ChainPRO_000000757318-493EGF-containing fibulin-like extracellular matrix protein 1
Disulfide bond177↔190
Disulfide bond184↔199
Disulfide bond201↔212
Disulfide bond218↔228
Disulfide bond224↔237
Disulfide bond239↔252
Glycosylation249N-linked (GlcNAc...) asparagine
Disulfide bond258↔268
Disulfide bond264↔277
Disulfide bond279↔292
Disulfide bond298↔309
Disulfide bond305↔318
Disulfide bond320↔332
Disulfide bond338↔350
Disulfide bond344↔359
Disulfide bond365↔377

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Expressed by olfactory ensheathing cells (at protein level). Detected in lung, intestine and kidney.

Interaction

Subunit

Interacts with ECM1. Interacts with TIMP3.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain26-71EGF-like 1; atypical
Domain173-213EGF-like 2; calcium-binding
Domain214-253EGF-like 3; calcium-binding
Domain254-293EGF-like 4; calcium-binding
Region259-493Mediates interaction with TIMP3
Domain294-333EGF-like 5; calcium-binding
Domain334-378EGF-like 6; calcium-binding

Sequence similarities

Belongs to the fibulin family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    493
  • Mass (Da)
    54,596
  • Last updated
    1998-01-01 v1
  • Checksum
    22DAFD70BACF1CA5
MLQTVFLTMLTLALVKSQVTEETITYTQCTDGYEWDPVRQQCKDIDECDIVPDACKGGMKCVNHYGGYLCLPKTAQIIVNNEQPQQETPAAEASSGAATGTIAARSMATSGVIPGGGFIASATAVAGPEVQTGRNNFVIRRNPADPQRIPSNPSHRIQCAAGYEQSEHNVCQDIDECTSGTHNCRLDQVCINLRGSFTCHCLPGYQKRGEQCVDIDECSVPPYCHQGCVNTPGSFYCQCNPGFQLAANNYTCVDINECDASNQCAQQCYNILGSFICQCNQGYELSSDRLNCEDIDECRTSSYLCQYQCVNEPGKFSCMCPQGYQVVRSRTCQDINECETTNECREDEMCWNYHGGFRCYPQNPCQDPYVLTSENRCVCPVSNTMCRDVPQSIVYKYMNIRSDRSVPSDIFQIQATTIYANTINTFRIKSGNENGEFYLRQTSPVSAMLVLVKSLTGPREHIVGLEMLTVSSIGTFRTSSVLRLTIIVGPFSF

Computationally mapped potential isoform sequences

There are 3 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A8I6A7G5A0A8I6A7G5_RATEfemp1500
A0A8I6A1M7A0A8I6A1M7_RATEfemp1507
Q6AXN2Q6AXN2_RATEfemp1493

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
D89730
EMBL· GenBank· DDBJ
BAA22265.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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