Variant position: 106 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 580 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 SNQLAVTFREENTIAFRHLF LLGYSDGADDTFAAYTREQLY
Mouse SNQLVVTFREENTIAFRHLF LLGYSDGSDDTFAAYTQEQLY
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
1 – 580 Mucolipin-1
87 – 298 Extracellular
109 – 109 Y -> G. Abolishes formation and extrusion of tubulo-vesicular structures and decreases lysosomal exocytosis when overexpressed.
110 – 110 S -> C. Modulates ion conduction; when associoated with C-112 and C-113.
111 – 111 D -> Q. Modulates inhibition by Ca(2+) at different pH levels but does not abolish channel inward rectification; when associated with Q-114 and Q-115.
112 – 112 G -> C. Modulates ion conduction; when associoated with C-110 and C-113.
113 – 113 A -> C. Modulates ion conduction; when associoated with C-110 and C-112.
114 – 114 D -> Q. Modulates inhibition by Ca(2+) at different pH levels but does not abolish channel inward rectification; when associated with Q-111 and Q-115.
115 – 115 D -> Q. Modulates inhibition by Ca(2+) at different pH levels but does not abolish channel inward rectification; when associated with Q-111 and Q-114.
The cation channel mucolipin-1 is a bifunctional protein that facilitates membrane remodeling via its serine lipase domain.
LaPlante J.M.; Falardeau J.L.; Brown E.M.; Slaugenhaupt S.A.; Vassilev P.M.;
Exp. Cell Res. 317:691-705(2011)
Cited for: FUNCTION; MUTAGENESIS OF TYR-109; CHARACTERIZATION OF VARIANTS ML4 PRO-106 AND LEU-465;
Structural basis of dual Ca(2+)/pH regulation of the endolysosomal TRPML1 channel.
Li M.; Zhang W.K.; Benvin N.M.; Zhou X.; Su D.; Li H.; Wang S.; Michailidis I.E.; Tong L.; Li X.; Yang J.;
Nat. Struct. Mol. Biol. 24:205-213(2017)
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 84-296; EXTRACELLULAR/LUMENAL PORE-FORMING DOMAIN; SUBUNIT; ACTIVITY REGULATION; MUTAGENESIS OF SER-110; ASP-111; GLY-112; ALA-113; ASP-114; ASP-115; LEU-144; ARG-146 AND VAL-432; CHARACTERIZATION OF VARIANTS ML4 PRO-106 AND PRO-232;
The neurogenetics of mucolipidosis type IV.
Altarescu G.; Sun M.; Moore D.F.; Smith J.A.; Wiggs E.A.; Solomon B.I.; Patronas N.J.; Frei K.P.; Gupta S.; Kaneski C.R.; Quarrell O.W.; Slaugenhaupt S.A.; Goldin E.; Schiffmann R.;
Cited for: VARIANTS ML4 PRO-106; TYR-362; PHE-408 DEL AND PRO-447;
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