Q9JJZ5 · EGFL6_MOUSE
- ProteinEpidermal growth factor-like protein 6
- GeneEgfl6
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids550 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
May bind integrin alpha-8/beta-1 and play a role in hair follicle morphogenesis. Promotes matrix assembly.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | basement membrane | |
Cellular Component | extracellular matrix | |
Cellular Component | extracellular region | |
Cellular Component | membrane | |
Molecular Function | calcium ion binding | |
Biological Process | cell adhesion | |
Biological Process | cell differentiation | |
Biological Process | extracellular matrix organization | |
Biological Process | positive regulation of cell-substrate adhesion |
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameEpidermal growth factor-like protein 6
- Short namesEGF-like protein 6
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ9JJZ5
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 362 | Loss of adhesive activity. | ||||
Sequence: D → E |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 47 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-18 | |||||
Sequence: MQPPWGLALPLLLPWVTG | ||||||
Chain | PRO_0000295812 | 19-550 | Epidermal growth factor-like protein 6 | |||
Sequence: GVGTSPWDYGLSALAHQPGVCQYGTKMACCYGWKRNNKGVCEAMCEPRCKFGECVGPNKCRCFPGYTGKTCTQDVNECGVKPRPCQHRCVNTHGSYKCFCLSGHMLLPDATCSNSRTCARLNCQYGCEDTEEGPRCVCPSSGLRLGPNGRVCLDIDECASSKAVCPSNRRCVNTFGSYYCKCHIGFELKYIGRRYDCVDINECALNTHPCSPHANCLNTRGSFKCKCKQGYRGNGLQCSVIPEHSVKEILTAPGTIKDRIKKLLAHKRTMKKKVKLKMVTPRPASTRVPKVNLPYSSEEGVSRGRNYDGEQKKKEEGKRERLEEEKGEKTLRNEVEQERTLRGDVFSPKVNEAEDLDLVYVQRKELNSKLKHKDLNISVDCSFDLGVCDWKQDREDDFDWHPADRDNDVGYYMAVPALAGHKKNIGRLKLLLPNLTPQSNFCLLFDYRLAGDKVGKLRVFVKNSNNALAWEETKNEDGRWRTGKIQLYQGIDTTKSVIFEAERGKGKTGEIAVDGVLLVSGLCPDDFLSVEG | ||||||
Disulfide bond | 59↔72 | |||||
Sequence: CEAMCEPRCKFGEC | ||||||
Disulfide bond | 63↔78 | |||||
Sequence: CEPRCKFGECVGPNKC | ||||||
Disulfide bond | 80↔89 | |||||
Sequence: CFPGYTGKTC | ||||||
Disulfide bond | 96↔107 | |||||
Sequence: CGVKPRPCQHRC | ||||||
Disulfide bond | 103↔116 | |||||
Sequence: CQHRCVNTHGSYKC | ||||||
Disulfide bond | 118↔130 | |||||
Sequence: CLSGHMLLPDATC | ||||||
Disulfide bond | 176↔189 | |||||
Sequence: CASSKAVCPSNRRC | ||||||
Disulfide bond | 183↔198 | |||||
Sequence: CPSNRRCVNTFGSYYC | ||||||
Disulfide bond | 221↔234 | |||||
Sequence: CALNTHPCSPHANC | ||||||
Disulfide bond | 228↔243 | |||||
Sequence: CSPHANCLNTRGSFKC | ||||||
Disulfide bond | 245↔256 | |||||
Sequence: CKQGYRGNGLQC | ||||||
Glycosylation | 394 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed at basement membrane of pelage follicles (at protein level).
Developmental stage
Detected in early lateral dermatome and in all dermatome derivatives. Expressed at the basement membrane of embryonic skin and developing hair follicles. At 16.5 dpc, present in lung epithelium, and developing oral and tooth germ epithelia (at protein level).
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 55-90 | EGF-like 1 | ||||
Sequence: NKGVCEAMCEPRCKFGECVGPNKCRCFPGYTGKTCT | ||||||
Domain | 92-131 | EGF-like 2; calcium-binding | ||||
Sequence: DVNECGVKPRPCQHRCVNTHGSYKCFCLSGHMLLPDATCS | ||||||
Domain | 135-171 | EGF-like 3 | ||||
Sequence: TCARLNCQYGCEDTEEGPRCVCPSSGLRLGPNGRVCL | ||||||
Domain | 172-210 | EGF-like 4; calcium-binding | ||||
Sequence: DIDECASSKAVCPSNRRCVNTFGSYYCKCHIGFELKYIG | ||||||
Domain | 217-257 | EGF-like 5; calcium-binding | ||||
Sequence: DINECALNTHPCSPHANCLNTRGSFKCKCKQGYRGNGLQCS | ||||||
Region | 295-354 | Disordered | ||||
Sequence: KMVTPRPASTRVPKVNLPYSSEEGVSRGRNYDGEQKKKEEGKRERLEEEKGEKTLRNEVE | ||||||
Compositional bias | 321-354 | Basic and acidic residues | ||||
Sequence: RGRNYDGEQKKKEEGKRERLEEEKGEKTLRNEVE | ||||||
Coiled coil | 327-357 | |||||
Sequence: GEQKKKEEGKRERLEEEKGEKTLRNEVEQER | ||||||
Domain | 397-543 | MAM | ||||
Sequence: VDCSFDLGVCDWKQDREDDFDWHPADRDNDVGYYMAVPALAGHKKNIGRLKLLLPNLTPQSNFCLLFDYRLAGDKVGKLRVFVKNSNNALAWEETKNEDGRWRTGKIQLYQGIDTTKSVIFEAERGKGKTGEIAVDGVLLVSGLCPD |
Sequence similarities
Belongs to the nephronectin family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length550
- Mass (Da)61,520
- Last updated2000-10-01 v1
- ChecksumDEF936325C9F31B3
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 321-354 | Basic and acidic residues | ||||
Sequence: RGRNYDGEQKKKEEGKRERLEEEKGEKTLRNEVE |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ245672 EMBL· GenBank· DDBJ | CAB92138.1 EMBL· GenBank· DDBJ | mRNA | ||
AL672174 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC117702 EMBL· GenBank· DDBJ | AAI17703.1 EMBL· GenBank· DDBJ | mRNA | ||
AK053738 EMBL· GenBank· DDBJ | BAC35499.1 EMBL· GenBank· DDBJ | mRNA |