Variant position: 446 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 MRFCCCVAVIYLGYCFCGWI VLGPYHVKFRSLSMVSECLFS
Mouse MRFCCCVAVIYLGYCFCGWI VLGPYHVKFRSLSMVSECLFS
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
428 – 448 Helical; Name=5
432 – 432 V -> P. Mediates localization to the plasma membrane and strong inwardly rectifying current.
417 – 447
Mucolipidosis type IV is caused by mutations in a gene encoding a novel transient receptor potential channel.
Sun M.; Goldin E.; Stahl S.; Falardeau J.L.; Kennedy J.C.; Acierno J.S. Jr.; Bove C.; Kaneski C.R.; Nagle J.; Bromley M.C.; Colman M.; Schiffmann R.; Slaugenhaupt S.A.;
Hum. Mol. Genet. 9:2471-2478(2000)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]; TISSUE SPECIFICITY; VARIANTS ML4 TYR-362; PHE-408 DEL AND LEU-446;
Molecular pathophysiology of mucolipidosis type IV: pH dysregulation of the mucolipin-1 cation channel.
Raychowdhury M.K.; Gonzalez-Perrett S.; Montalbetti N.; Timpanaro G.A.; Chasan B.; Goldmann W.H.; Stahl S.; Cooney A.; Goldin E.; Cantiello H.F.;
Hum. Mol. Genet. 13:617-627(2004)
Cited for: FUNCTIONAL CHARACTERIZATION; SUBUNIT; CHARACTERIZATION OF VARIANTS ML4 TYR-362; PHE-408 DEL AND LEU-446;
The type IV mucolipidosis-associated protein TRPML1 is an endolysosomal iron release channel.
Dong X.P.; Cheng X.; Mills E.; Delling M.; Wang F.; Kurz T.; Xu H.;
Cited for: FUNCTION; MUTAGENESIS OF VAL-432; CHARACTERIZATION OF VARIANTS ML4 PRO-232; TYR-362; CYS-403 AND LEU-446;
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.