Glmp
entrez
56700
canonical
uniprot
Q9JHJ3
canonical
ensembl
ENSMUSG00000001418
resolver
ensp
ENSMUSP00000135398
resolver
enst
ENSMUST00000177005
resolver
genesymbol
Glmp
resolver
uniprot
Q3TUF5
resolver
uniprot
Q3UBV7
resolver
uniprot
Q8C6H7
resolver
uniprot_entry
GLMP_MOUSE
resolver
uniprot_sec
Q3TUF5
resolver
uniprot_sec
Q3UBV7
resolver
uniprot_sec
Q8C6H7
resolver
amino_acid_sequence
MFRCWGPHWGWVPCAPTPWLLLSLLVCSAPFGLQGEETRQVSMEVISGWPNPQNLLHIRAVGSNSTLHYVWSSLGPPAVVLVATNTTQSVLSVNWSLLLSPDPAGALMVLPKSSIQFSSALVFTRLLEFDSTNASEGAQPPGKPYPPYSLAKFSWNNITNSLDLANLSADFQGRPVDDPTGAFANGSLTFKVQAFSRSGRPAQPPRLLHTADVCQLEVALVGASPRGNHSLFGLEVATLGQGPDCPSVNERNSIDDEYAPAVFQLNQLLWGSSPSGFMQWRPVAFSEEERARESALPCQASTLHSTLASSLPHSPIVQAFFGSQNNFCAFNLTFGAPTGPGYWDQYYLCWSMLLGMGFPPVDIFSPLVLGIMAVALGAPGLMFLGGGLFLLLRHRRYSEYQSIN
uniprot
proteins
function
FUNCTION: Required to protect lysosomal transporter MFSD1 from lysosomal proteolysis and for MFSD1 lysosomal localization. {ECO:0000269|PubMed:31661432, ECO:0000269|PubMed:32959924}.
uniprot
proteins
mass_dalton
43804
uniprot
proteins
mutagenesis
MUTAGEN 85; /note="N->A: Reduced glycosylation."; /evidence="ECO:0000269|PubMed:32959924"; MUTAGEN 94; /note="N->A: Reduced glycosylation."; /evidence="ECO:0000269|PubMed:32959924"; MUTAGEN 133; /note="N->A: Reduced glycosylation."; /evidence="ECO:0000269|PubMed:32959924"; MUTAGEN 157; /note="N->A: Reduced glycosylation."; /evidence="ECO:0000269|PubMed:32959924"; MUTAGEN 166; /note="N->A: No effect on glycosylation."; /evidence="ECO:0000269|PubMed:32959924"; MUTAGEN 185; /note="N->A: Reduced glycosylation."; /evidence="ECO:0000269|PubMed:32959924"; MUTAGEN 228; /note="N->A: Reduced glycosylation."; /evidence="ECO:0000269|PubMed:32959924"; MUTAGEN 331; /note="N->A: Reduced glycosylation."; /evidence="ECO:0000269|PubMed:32959924"; MUTAGEN 400; /note="Y->A: Abolishes lysosomal localization and results in mislocalization to the cell surface. Localizes to lysosomes when expressed with wild-type MFSD1."; /evidence="ECO:0000269|PubMed:19489740, ECO:0000269|PubMed:32959924
uniprot
proteins
post_translational_modification
PTM: Highly N-glycosylated (PubMed:19349973, PubMed:19489740). N-glycosylation is essential for GLMP stability and for MFSD1 lysosomal localization (PubMed:32959924). {ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:19489740, ECO:0000269|PubMed:32959924}.
uniprot
proteins
protein_family
GLMP family
uniprot
proteins
pubmed
11444019
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
19349973
uniprot
proteins
pubmed
19489740
uniprot
proteins
pubmed
24487409
uniprot
proteins
pubmed
26047317
uniprot
proteins
pubmed
26707125
uniprot
proteins
pubmed
27141234
uniprot
proteins
pubmed
31661432
uniprot
proteins
pubmed
32959924
uniprot
proteins
sequence_length
404
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:19489740, ECO:0000269|PubMed:31661432}; Single-pass type I membrane protein {ECO:0000255}; Lumenal side {ECO:0000305}.
uniprot
proteins
transmembrane_region
TRANSMEM 371..391; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins