Variant position: 345 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 493 The length of the canonical sequence.
Location on the sequence:
The residue change on the sequence. Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown.
Residue conservation: The multiple alignment of the region surrounding the variant against various orthologous sequences.
Human QVVRSRTCQDINECETTNEC REDEMCWNYHGGFRCYPRNPC
Mouse EVVRSRTCQDINECETTNEC REDEMCWNYHGGFRCYPRNPC
Rat QVVRSRTCQDINECETTNEC REDEMCWNYHGGFRCYPQNPC
Sequence annotation in neighborhood: The regions or sites of interest surrounding the variant. In general the features listed are posttranslational modifications, binding sites, enzyme active sites, local secondary structure or other characteristics reported in the cited references. The "Sequence annotation in neighborhood" lines have a fixed format:
Type: the type of sequence feature. Positions: endpoints of the sequence feature. Description: contains additional information about the feature.
Type Positions Description
18 – 493 EGF-containing fibulin-like extracellular matrix protein 1
334 – 378 EGF-like 6; calcium-binding
259 – 493 Mediates interaction with TIMP3
338 – 350
344 – 359
Aberrant accumulation of EFEMP1 underlies drusen formation in Malattia Leventinese and age-related macular degeneration.
Marmorstein L.Y.; Munier F.L.; Arsenijevic Y.; Schorderet D.F.; McLaughlin P.J.; Chung D.; Traboulsi E.; Marmorstein A.D.;
Proc. Natl. Acad. Sci. U.S.A. 99:13067-13072(2002)
Cited for: TISSUE SPECIFICITY; CHARACTERIZATION OF VARIANT DHRD TRP-345;
A single EFEMP1 mutation associated with both malattia Leventinese and Doyne honeycomb retinal dystrophy.
Stone E.M.; Lotery A.J.; Munier F.L.; Heon E.; Piguet B.; Guymer R.H.; Vandenburgh K.; Cousin P.; Nishimura D.; Swiderski R.E.; Silvestri G.; Mackey D.A.; Hagerman G.S.; Bird A.C.; Sheffield V.C.; Schorderet D.F.;
Nat. Genet. 22:199-202(1999)
Cited for: VARIANT DHRD TRP-345; VARIANT PHE-220;
Dominant radial drusen and Arg345Trp EFEMP1 mutation.
Matsumoto M.; Traboulsi E.I.;
Am. J. Ophthalmol. 131:810-812(2001)
Cited for: VARIANT DHRD TRP-345;
The R345W mutation in EFEMP1 is pathogenic and causes AMD-like deposits in mice.
Fu L.; Garland D.; Yang Z.; Shukla D.; Rajendran A.; Pearson E.; Stone E.M.; Zhang K.; Pierce E.A.;
Hum. Mol. Genet. 16:2411-2422(2007)
Cited for: CHARACTERIZATION OF VARIANT DHRD TRP-345;
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