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battenin; protein CLN3; Batten disease protein (CLN3, BTS)
Structure:
- belongs to the battenin family
- highly glycosylated
Compartment:
- lysosome membrane; multi-pass membrane protein
Alternative splicing:
- named isoforms=5
- additional isoforms seem to exist
- at least some isoforms may be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay
Pathology:
- defects in CLN3 are the cause of neuronal ceroid lipofuscinosis type 3 (Batten disease)
Related
neuronal ceroid lipofuscinosis
General
ceroid-lipofuscinosis neuronal protein
glycoprotein
phosphoprotein
transmembrane 8 protein
Properties
SIZE: entity length = 438 aa
MW = 48 kD
COMPARTMENT: lysosome
MOTIF: Ser phosphorylation site {S12}
Ser phosphorylation site {S14}
transmembrane domain {38-58}
N-glycosylation site {N71}
N-glycosylation site {N85}
transmembrane domain {99-119}
transmembrane domain {128-148}
transmembrane domain {180-200}
transmembrane domain {212-232}
transmembrane domain {278-298}
N-glycosylation site {N310}
transmembrane domain {358-378}
transmembrane domain {407-427}
Database Correlations
OMIM correlations
MORBIDMAP 607042
UniProt Q13286
Pfam PF02487
Entrez Gene 1201
Kegg hsa:1201
References
- UniProt :accession Q13286
- NCL CLN3; Note: neural ceroid lipofuscinoses mutation db
http://www.ucl.ac.uk/ncl/cln3.shtml
- mutations of the CLN3 gene
Retina International's scientific newsletter
http://www.retina-international.com/sci-news/cln3mut.htm
- GeneReviews
http://www.ncbi.nlm.nih.gov/sites/genetests/lab/gene/CLN3