CLN3
entrez
1201
canonical
uniprot
Q13286
canonical
ensembl
ENSG00000188603
resolver
ensembl
ENSG00000261832
resolver
ensp
ENSP00000350523
resolver
ensp
ENSP00000353073
resolver
ensp
ENSP00000353116
resolver
ensp
ENSP00000454253
resolver
ensp
ENSP00000455387
resolver
ensp
ENSP00000490105
resolver
enst
ENST00000357857
resolver
enst
ENST00000567963
resolver
enst
ENST00000568224
resolver
genesymbol
CLN3
resolver
genesymbol_syn
BTS
resolver
hgnc
HGNC:2074
resolver
uniprot
A0ACM8QBQ0
resolver
uniprot
B2R7J1
resolver
uniprot
B4DFF3
resolver
uniprot
B4DMY6
resolver
uniprot
B4DXL3
resolver
uniprot
H3BPM8
resolver
uniprot
K7N7C6
resolver
uniprot
O00668
resolver
uniprot
O95089
resolver
uniprot
Q2TA70
resolver
uniprot
Q549S9
resolver
uniprot
Q9UP09
resolver
uniprot
Q9UP11
resolver
uniprot
Q9UP12
resolver
uniprot
Q9UP13
resolver
uniprot
Q9UP14
resolver
uniprot_entry
A0ACM8QBQ0_HUMAN
resolver
uniprot_entry
B4DFF3_HUMAN
resolver
uniprot_entry
B4DMY6_HUMAN
resolver
uniprot_entry
CLN3_HUMAN
resolver
uniprot_entry
K7N7C6_HUMAN
resolver
uniprot_entry
Q2TA70_HUMAN
resolver
uniprot_sec
B2R7J1
resolver
uniprot_sec
B4DXL3
resolver
uniprot_sec
H3BPM8
resolver
uniprot_sec
O00668
resolver
uniprot_sec
O95089
resolver
uniprot_sec
Q549S9
resolver
uniprot_sec
Q9UP09
resolver
uniprot_sec
Q9UP11
resolver
uniprot_sec
Q9UP12
resolver
uniprot_sec
Q9UP13
resolver
uniprot_sec
Q9UP14
resolver
amino_acid_sequence
MGGCAGSRRRFSDSEGEETVPEPRLPLLDHQGAHWKNAVGFWLLGLCNNFSYVVMLSAAHDILSHKRTSGNQSHVDPGPTPIPHNSSSRFDCNSVSTAAVLLADILPTLVIKLLAPLGLHLLPYSPRVLVSGICAAGSFVLVAFSHSVGTSLCGVVFASISSGLGEVTFLSLTAFYPRAVISWWSSGTGGAGLLGALSYLGLTQAGLSPQQTLLSMLGIPALLLASYFLLLTSPEAQDPGGEEEAESAARQPLIRTEAPESKPGSSSSLSLRERWTVFKGLLWYIVPLVVVYFAEYFINQGLFELLFFWNTSLSHAQQYRWYQMLYQAGVFASRSSLRCCRIRFTWALALLQCLNLVFLLADVWFGFLPSIYLVFLIILYEGLLGGAAYVNTFHNIALETSDEHREFAMAATCISDTLGISLSGLLALPLHDFLCQLS
uniprot
proteins
disease_involvement
DISEASE: Ceroid lipofuscinosis, neuronal, 3 (CLN3) [MIM:204200]: A form of neuronal ceroid lipofuscinosis. Neuronal ceroid lipofuscinoses are progressive neurodegenerative, lysosomal storage diseases characterized by intracellular accumulation of autofluorescent liposomal material, and clinically by seizures, dementia, visual loss, and/or cerebral atrophy. The hallmark of CLN3 is the ultrastructural pattern of lipopigment with a fingerprint profile, which can have 3 different appearances: pure within a lysosomal residual body; in conjunction with curvilinear or rectilinear profiles; and as a small component within large membrane-bound lysosomal vacuoles. The combination of fingerprint profiles within lysosomal vacuoles is a regular feature of blood lymphocytes from patients with neuronal ceroid lipofuscinosis type 3. {ECO:0000269|PubMed:10332042, ECO:0000269|PubMed:10924275, ECO:0000269|PubMed:14699076, ECO:0000269|PubMed:17482562, ECO:0000269|PubMed:21990111, ECO:0000269|PubMed:22261744, ECO:0000269|PubMed:9311735, ECO:0000269|PubMed:9490299}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Retinitis pigmentosa 101 (RP101) [MIM:621548]: A form of retinitis pigmentosa, a retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. RP101 is an autosomal recessive form characterized by macular edema, mild intraretinal pigment migration, and widespread atrophy in advanced disease. Disease onset ranges from the first to fourth decades of life. {ECO:0000269|PubMed:28542676, ECO:0000269|PubMed:29049447, ECO:0000269|PubMed:33507216}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Mediates microtubule-dependent, anterograde transport connecting the Golgi network, endosomes, autophagosomes, lysosomes and plasma membrane, and participates in several cellular processes such as regulation of lysosomal pH, lysosome protein degradation, receptor-mediated endocytosis, autophagy, transport of proteins and lipids from the TGN, apoptosis and synaptic transmission (PubMed:10924275, PubMed:15471887, PubMed:18317235, PubMed:18817525, PubMed:20850431, PubMed:22261744). Facilitates the proteins transport from trans-Golgi network (TGN)-to other membrane compartments such as transport of microdomain-associated proteins to the plasma membrane, IGF2R transport to the lysosome where it regulates the CTSD release leading to regulation of CTSD maturation and thereby APP intracellular processing (PubMed:10924275, PubMed:18817525). Moreover regulates CTSD activity in response to osmotic stress (PubMed:23840424, PubMed:28390177). Also binds galactosylceramide and transports it from the trans Golgi to the rafts, which may have immediate and downstream effects on cell survival by modulating ceramide synthesis (PubMed:18317235). At the plasma membrane, regulates actin-dependent events including filopodia formation, cell migration, and pinocytosis through ARF1-CDC42 pathway and also the cytoskeleton organization through interaction with MYH10 and fodrin leading to the regulation of the plasma membrane association of Na+, K+ ATPase complex (PubMed:20850431). Regulates synaptic transmission in the amygdala, hippocampus, and cerebellum through regulation of synaptic vesicles density and their proximity to active zones leading to modulation of short-term plasticity and age-dependent anxious behavior, learning and memory (By similarity). Regulates autophagic vacuoles (AVs) maturation by modulating the trafficking between endocytic and autophagolysosomal/lysosomal compartments, which involves vesicle fusion leading to regulation of degradation process (By similarity). Also participates in cellular homeostasis of compounds such as, water, ions, amino acids, proteins and lipids in several tissue namely in brain and kidney through regulation of their transport and synthesis (PubMed:17482562). {ECO:0000250|UniProtKB:Q61124, ECO:0000269|PubMed:10924275, ECO:0000269|PubMed:15471887, ECO:0000269|PubMed:17482562, ECO:0000269|PubMed:18317235, ECO:0000269|PubMed:18817525, ECO:0000269|PubMed:20850431, ECO:0000269|PubMed:22261744, ECO:0000269|PubMed:23840424, ECO:0000269|PubMed:28390177}.
uniprot
proteins
mass_dalton
47623
uniprot
proteins
mutagenesis
MUTAGEN 242..244; /note="EEE->AAA: Loss of lysosomal targeting; when associated with A-409 and A-419. Loss of lysosomal localization; when associated with A-246."; /evidence="ECO:0000269|PubMed:14699076, ECO:0000269|PubMed:15469932"; MUTAGEN 246; /note="E->A: Loss of lysosomal localization; when associated with 242-A--A-244."; /evidence="ECO:0000269|PubMed:15469932"; MUTAGEN 253..254; /note="LI->AA: Does not affect lysosomal localization in AP3D1 or AP2A2 or AP1G1 deficient cells. Abolishes the interaction of AP3D1, AP2A2 and AP1G1. Loss of lysosomal localization."; /evidence="ECO:0000269|PubMed:15469932, ECO:0000269|PubMed:15598649"; MUTAGEN 253; /note="L->A: Loss of lysosomal targeting; when associated with A-254. Does not affect interaction with CLN5; when associated with A-254. Does not affect interaction with CLN5; when associated with A-254; A-409 and A-419. Loss of lysosomal targeting; when associated with A-254; A-409 and A-409."; /evidence="ECO:0000269|PubMed:14699076"; MUTAGEN 254; /note="I->A: Loss of lysosomal targeting. Does not affect interaction with CLN5; when associated with A-253. Does not affect interaction with CLN5; when associated with A-253; A-409 and A-419. Loss of lysosomal targeting; when associated with A-253; A-409 and A-409."; /evidence="ECO:0000269|PubMed:14699076"; MUTAGEN 310; /note="N->Q: Does not affect glycosylation."; /evidence="ECO:0000269|PubMed:12706816"; MUTAGEN 409; /note="M->A: Does not affect lysosomal targeting; when associated with A-419. Loss of lysosomal targeting; when associated with A-253 and A-254. Loss of lysosomal targeting; when associated with 242-A--A-244 and A-419. Does not affect interaction with CLN5; when associated with A-419. Does not affect interaction with CLN5; when associated with A-253; A-254 and A-419. Loss of lysosomal targeting; when associated with A-253; A-254 and A-419. Loss of lysosomal localization in AP3D1 or AP1G1 deficient cells; when associated with A-419."; /evidence="ECO:0000269|PubMed:14699076, ECO:0000269|PubMed:15598649"; MUTAGEN 419; /note="G->A: Does not affect lysosomal targeting; when associated with A-409. Loss of lysosomal targeting; when associated with A-253 and A-254. Loss of lysosomal targeting; when associated with 242-A--A-244 and A-409. Does not affect interaction with CLN5; when associated with A-409. Does not affect interaction with CLN5; when associated with A-253; A-254 and A-409. Loss of lysosomal targeting; when associated with A-253; A-254 and A-409. Loss of lysosomal localization in AP3D1 or AP1G1 deficient cells; when associated with A-409."; /evidence="ECO:0000269|PubMed:14699076, ECO:0000269|PubMed:15598649
uniprot
proteins
post_translational_modification
PTM: Highly glycosylated. {ECO:0000269|PubMed:10924275, ECO:0000269|PubMed:12706816, ECO:0000269|PubMed:17286803}.; PTM: Farnesylation is important for trafficking to lysosomes. {ECO:0000269|PubMed:17286803}.; PTM: Phosphorylated on both serine and threonine residues by PKA, PKG and CK2. {ECO:0000269|PubMed:9878558}.
uniprot
proteins
protein_family
Battenin family
uniprot
proteins
pubmed
10191115
uniprot
proteins
pubmed
10191116
uniprot
proteins
pubmed
10332042
uniprot
proteins
pubmed
10493829
uniprot
proteins
pubmed
10924275
uniprot
proteins
pubmed
12706816
uniprot
proteins
pubmed
14644441
uniprot
proteins
pubmed
14699076
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14759258
uniprot
proteins
pubmed
15240864
uniprot
proteins
pubmed
15469932
uniprot
proteins
pubmed
15471887
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15598649
uniprot
proteins
pubmed
15616553
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17189291
uniprot
proteins
pubmed
17237713
uniprot
proteins
pubmed
17286803
uniprot
proteins
pubmed
17482562
uniprot
proteins
pubmed
17897319
uniprot
proteins
pubmed
18317235
uniprot
proteins
pubmed
18621045
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
18817525
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
19941651
uniprot
proteins
pubmed
20015955
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20850431
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21990111
uniprot
proteins
pubmed
22261744
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23840424
uniprot
proteins
pubmed
25051496
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
28390177
uniprot
proteins
pubmed
28542676
uniprot
proteins
pubmed
29049447
uniprot
proteins
pubmed
33507216
uniprot
proteins
pubmed
34709357
uniprot
proteins
pubmed
7553855
uniprot
proteins
pubmed
9119403
uniprot
proteins
pubmed
9311735
uniprot
proteins
pubmed
9490299
uniprot
proteins
pubmed
9878558
uniprot
proteins
pubmed
9949212
uniprot
proteins
sequence_length
438
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:10332042, ECO:0000269|PubMed:14644441, ECO:0000269|PubMed:15471887, ECO:0000269|PubMed:15598649, ECO:0000269|PubMed:17286803, ECO:0000269|PubMed:17897319, ECO:0000269|PubMed:23840424}; Multi-pass membrane protein {ECO:0000269|PubMed:17286803, ECO:0000269|PubMed:17897319, ECO:0000269|PubMed:9949212}. Late endosome {ECO:0000269|PubMed:10332042, ECO:0000269|PubMed:15471887, ECO:0000269|PubMed:17286803, ECO:0000269|PubMed:23840424}. Lysosome {ECO:0000269|PubMed:10332042, ECO:0000269|PubMed:10924275, ECO:0000269|PubMed:14699076, ECO:0000269|PubMed:19941651, ECO:0000269|PubMed:9949212}. Golgi apparatus {ECO:0000269|PubMed:10332042, ECO:0000269|PubMed:15240864, ECO:0000269|PubMed:23840424}. Golgi apparatus membrane {ECO:0000269|PubMed:9949212}. Golgi apparatus, Golgi stack {ECO:0000269|PubMed:15240864}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:10332042, ECO:0000269|PubMed:15240864}. Cell membrane {ECO:0000269|PubMed:14644441, ECO:0000269|PubMed:15240864}. Recycling endosome {ECO:0000269|PubMed:15240864}. Membrane raft {ECO:0000269|PubMed:15240864, ECO:0000269|PubMed:23840424}. Membrane, caveola {ECO:0000269|PubMed:23840424}. Early endosome membrane {ECO:0000269|PubMed:23840424}. Synapse, synaptosome {ECO:0000250|UniProtKB:Q61124}. Late endosome membrane {ECO:0000250|UniProtKB:Q61124}. Cytoplasmic vesicle, autophagosome {ECO:0000250|UniProtKB:Q61124}. Note=CLN3 is not present in late endosomes/lysosomes in fibroblasts and neurons (PubMed:15240864). Trafficks from cell membrane to Golgi via endosomes (PubMed:15240864). Osmotic stress changes the subcellular localization of CLN3 (PubMed:23840424). Trafficks to intracellular compartments via the plasma membranet through AP3M1-dependent mechanisms (PubMed:14644441). Excluded from the synaptic vesicles (By similarity). {ECO:0000250|UniProtKB:Q61124, ECO:0000269|PubMed:14644441, ECO:0000269|PubMed:15240864, ECO:0000269|PubMed:23840424}.
uniprot
proteins
transmembrane_region
TRANSMEM 38..58; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 128..148; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 152..172; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 183..203; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 278..298; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 347..367; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins