Sequence information
Variant position: 244 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 504 The length of the canonical sequence.
Location on the sequence:
ASRILKESPSGYLRSGEGDT
G CGELVWVGEPLTLRTAETIT
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 AS---------RILKESPSGYLRSGEG----------------------------------------DTG C--GELVWVGEPLT----------LRTAETIT
AS---------RILKESPSGHPRNEEG--------------
Mouse AS---------QILKENPSGRPRSKEG--------------
Rat AS---------QILK-NQSGHPRSKEG--------------
Bovine AS---------QILKESPSGHPRNEEG--------------
Rabbit AS---------RILKENPPVLPRGEEG--------------
Cat AS---------RILKESPSGHPRSEEG--------------
Slime mold ATLMKSTPHYIRTIKPNDLKKPNILEGGRVLHQVKYLGLLD
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
Chain
33 – 504
Myocilin
Chain
227 – 504
Myocilin, C-terminal fragment
Domain
244 – 503
Olfactomedin-like
Mutagenesis
226 – 226
R -> A. Reduced processing. Impairs endoproteolytic processing; when associated with A-229 or A-230. Completely processed after 6 days of expression, and releases a C-terminal fragment with similar electrophoretic mobility to that obtained by processing wild-type myocilin; when associated with A-229 or A-230.
Mutagenesis
226 – 226
R -> Q. Slightly increases endoproteolytic processing.
Mutagenesis
227 – 227
I -> G. Reduced processing.
Mutagenesis
229 – 229
K -> A. Completely blocks endoproteolytic processing; when associated with A-226. Completely processed after 6 days of expression, and releases a C-terminal fragment with similar electrophoretic mobility to that obtained by processing wild-type myocilin; when associated with A-226.
Mutagenesis
230 – 230
E -> A. Impairs endoproteolytic processing; when associated with A-226. Completely processed after 6 days of expression, and released a C-terminal fragment with similar electrophoretic mobility to that obtained by processing wild-type myocilin; when associated with A-226.
Literature citations
Myocilin Gly252Arg mutation and glaucoma of intermediate severity in Caucasian individuals.
Hewitt A.W.; Bennett S.L.; Richards J.E.; Dimasi D.P.; Booth A.P.; Inglehearn C.; Anwar R.; Yamamoto T.; Fingert J.H.; Heon E.; Craig J.E.; Mackey D.A.;
Arch. Ophthalmol. 125:98-104(2007)
Cited for: VARIANTS GLC1A VAL-244 AND ARG-252;
Disclaimer:
Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. They are not in any way intended to be used as a substitute for professional medical advice, diagnostic, treatment or care.