CLN5
entrez
1203
canonical
uniprot
O75503
canonical
ensembl
ENSG00000102805
resolver
ensp
ENSP00000366673
resolver
ensp
ENSP00000489711
resolver
ensp
ENSP00000489809
resolver
ensp
ENSP00000490181
resolver
enst
ENST00000377453
resolver
enst
ENST00000636183
resolver
enst
ENST00000636780
resolver
enst
ENST00000637537
resolver
genesymbol
CLN5
resolver
genesymbol_syn
BMPS
resolver
hgnc
HGNC:2076
resolver
uniprot
A0A1B0GTI0
resolver
uniprot
A0A1B0GTR6
resolver
uniprot
B3KQK7
resolver
uniprot_entry
A0A1B0GTR6_HUMAN
resolver
uniprot_entry
CLN5_HUMAN
resolver
uniprot_sec
A0A1B0GTI0
resolver
uniprot_sec
B3KQK7
resolver
activity_regulation
ACTIVITY REGULATION: Anionic phospholipids activate bis(monoacylglycero)phosphate (BMP) synthase activity (PubMed:37708259). Amiodarone, a cationic amphiphilic drug inhibits BMP synthase activity towards liposomal lysophosphatidylglycerol (PubMed:37708259). Palmostatin B inhibits palmitoyl protein thioesterase activity (PubMed:35427157). {ECO:0000269|PubMed:35427157, ECO:0000269|PubMed:37708259}.
uniprot
proteins
amino_acid_sequence
MAQEVDTAQGAEMRRGAGAARGRASWCWALALLWLAVVPGWSRVSGIPSRRHWPVPYKRFDFRPKPDPYCQAKYTFCPTGSPIPVMEGDDDIEVFRLQAPVWEFKYGDLLGHLKIMHDAIGFRSTLTGKNYTMEWYELFQLGNCTFPHLRPEMDAPFWCNQGAACFFEGIDDVHWKENGTLVQVATISGNMFNQMAKWVKQDNETGIYYETWNVKASPEKGAETWFDSYDCSKFVLRTFNKLAEFGAEFKNIETNYTRIFLYSGEPTYLGNETSVFGPTGNKTLGLAIKRFYYPFKPHLPTKEFLLSLLQIFDAVIVHKQFYLFYNFEYWFLPMKFPFIKITYEEIPLPIRNKTLSGL
uniprot
proteins
disease_involvement
DISEASE: Ceroid lipofuscinosis, neuronal, 5 (CLN5) [MIM:256731]: 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 lipopigment patterns observed most often in neuronal ceroid lipofuscinosis type 5 comprise mixed combinations of granular, curvilinear, and fingerprint profiles. {ECO:0000269|PubMed:15728307, ECO:0000269|PubMed:16814585, ECO:0000269|PubMed:17607606, ECO:0000269|PubMed:19309691, ECO:0000269|PubMed:20052765, ECO:0000269|PubMed:21990111, ECO:0000269|PubMed:24038957, ECO:0000269|PubMed:24058541, ECO:0000269|PubMed:26342652, ECO:0000269|PubMed:35427157, ECO:0000269|PubMed:37708259, ECO:0000269|PubMed:9662406}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
2.3.1.-
uniprot
proteins
ec_number
3.1.2.22
uniprot
proteins
function
FUNCTION: [Bis(monoacylglycero)phosphate synthase CLN5, secreted form]: Catalyzes the synthesis of bis(monoacylglycero)phosphate (BMP) via transacylation of 2 molecules of lysophosphatidylglycerol (LPG) (PubMed:37708259). BMP also known as lysobisphosphatidic acid plays a key role in the formation of intraluminal vesicles and in maintaining intracellular cholesterol homeostasis (PubMed:37708259). Can use only LPG as the exclusive lysophospholipid acyl donor for base exchange and displays BMP synthase activity towards various LPGs (LPG 14:0, LPG 16:0, LPG 18:0, LPG 18:1) with a higher preference for longer chain lengths (PubMed:37708259). Plays a role in influencing the retrograde trafficking of lysosomal sorting receptors SORT1 and IGF2R from the endosomes to the trans-Golgi network by controlling the recruitment of retromer complex to the endosomal membrane (PubMed:22431521). Regulates the localization and activation of RAB7A which is required to recruit the retromer complex to the endosomal membrane (PubMed:22431521). {ECO:0000269|PubMed:22431521, ECO:0000269|PubMed:37708259}.; FUNCTION: Exhibits palmitoyl protein thioesterase (S-depalmitoylation) activity in vitro and most likely plays a role in protein S-depalmitoylation. {ECO:0000269|PubMed:35427157}.
uniprot
proteins
mass_dalton
41497
uniprot
proteins
mutagenesis
MUTAGEN 101; /note="V->S: Significant decrease in palmitoyl protein thioesterase activity."; /evidence="ECO:0000269|PubMed:35427157"; MUTAGEN 115; /note="I->S: Significant decrease in palmitoyl protein thioesterase activity."; /evidence="ECO:0000269|PubMed:35427157"; MUTAGEN 117; /note="H->A: Significant decrease in palmitoyl protein thioesterase activity."; /evidence="ECO:0000269|PubMed:35427157"; MUTAGEN 130; /note="N->Q: Loss of glycosylation. Retained in the endoplasmic reticulum rather than reaching the lysosome."; /evidence="ECO:0000269|PubMed:24058541"; MUTAGEN 143; /note="N->Q: Loss of glycosylation. Effectively transported to the lysosome."; /evidence="ECO:0000269|PubMed:24058541"; MUTAGEN 178; /note="N->Q: Loss of glycosylation. Effectively transported to the lysosome."; /evidence="ECO:0000269|PubMed:24058541"; MUTAGEN 203; /note="N->Q: Loss of glycosylation. Retained in the endoplasmic reticulum rather than reaching the lysosome."; /evidence="ECO:0000269|PubMed:24058541"; MUTAGEN 231; /note="C->S: Significant decrease in bis(monoacylglycero)phosphate synthase and palmitoyl protein thioesterase activities. No alterations in secondary structure and thermal stability."; /evidence="ECO:0000269|PubMed:35427157, ECO:0000269|PubMed:37708259"; MUTAGEN 255; /note="N->Q: Loss of glycosylation. Retained in the endoplasmic reticulum rather than reaching the lysosome."; /evidence="ECO:0000269|PubMed:24058541"; MUTAGEN 259; /note="I->S: Significant decrease in palmitoyl protein thioesterase activity."; /evidence="ECO:0000269|PubMed:35427157"; MUTAGEN 271; /note="N->Q: Loss of glycosylation. Retained in the endoplasmic reticulum rather than reaching the lysosome."; /evidence="ECO:0000269|PubMed:24058541"; MUTAGEN 281; /note="N->Q: Loss of glycosylation. Partially retained in the endoplasmic reticulum."; /evidence="ECO:0000269|PubMed:24058541"; MUTAGEN 318..319; /note="HK->EE: Weakens vesicular bis(monoacylglycero)phosphate binding. No alterations in secondary structure and thermal stability."; /evidence="ECO:0000269|PubMed:37708259"; MUTAGEN 352; /note="N->Q: Loss of glycosylation. Retained in the Golgi apparatus rather than reaching the lysosome."; /evidence="ECO:0000269|PubMed:24058541
uniprot
proteins
post_translational_modification
PTM: N-glycosylated with both high mannose and complex type sugars. Glycosylation is important for proper folding and trafficking to the lysosomes. {ECO:0000269|PubMed:11971870, ECO:0000269|PubMed:20052765, ECO:0000269|PubMed:24038957, ECO:0000269|PubMed:24058541, ECO:0000269|PubMed:37708259}.; PTM: [Bis(monoacylglycero)phosphate synthase CLN5]: The type II membrane signal anchor is proteolytically cleaved to produce a mature form that is transported to the lysosomes (Bis(monoacylglycero)phosphate synthase CLN5, secreted form) (PubMed:20052765, PubMed:24038957, PubMed:28442266). {ECO:0000269|PubMed:20052765, ECO:0000269|PubMed:24038957, ECO:0000269|PubMed:28442266}.; PTM: Can undergo proteolytic cleavage at the C-terminus, probably by a cysteine protease and may involve the removal of approximately 10-15 residues from the C-terminal end (PubMed:26342652). {ECO:0000269|PubMed:26342652}.; PTM: Ubiquitinated by the E3 ubiquitin ligase complex at least composed of CUL3, KCTD7 and RBX1 leading to proteasomal degradation. {ECO:0000269|PubMed:35921411}.
uniprot
proteins
protein_family
CLN5 family
uniprot
proteins
pubmed
11971870
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15057823
uniprot
proteins
pubmed
15728307
uniprot
proteins
pubmed
16814585
uniprot
proteins
pubmed
17607606
uniprot
proteins
pubmed
19309691
uniprot
proteins
pubmed
20052765
uniprot
proteins
pubmed
21990111
uniprot
proteins
pubmed
22431521
uniprot
proteins
pubmed
24038957
uniprot
proteins
pubmed
24058541
uniprot
proteins
pubmed
26342652
uniprot
proteins
pubmed
28442266
uniprot
proteins
pubmed
35427157
uniprot
proteins
pubmed
35921411
uniprot
proteins
pubmed
37708259
uniprot
proteins
pubmed
9662406
uniprot
proteins
sequence_length
358
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Bis(monoacylglycero)phosphate synthase CLN5, secreted form]: Lysosome {ECO:0000269|PubMed:11971870, ECO:0000269|PubMed:20052765, ECO:0000269|PubMed:22431521, ECO:0000269|PubMed:24038957, ECO:0000269|PubMed:24058541, ECO:0000269|PubMed:28442266, ECO:0000269|PubMed:37708259}.; SUBCELLULAR LOCATION: [Bis(monoacylglycero)phosphate synthase CLN5]: Membrane {ECO:0000269|PubMed:24038957, ECO:0000269|PubMed:28442266}; Single-pass type II membrane protein {ECO:0000269|PubMed:24038957, ECO:0000269|PubMed:28442266}. Note=An amphipathic anchor region facilitates its association with the membrane. {ECO:0000269|PubMed:24038957}.
uniprot
proteins
transmembrane_region
TRANSMEM 24..40; /note="Helical; Signal-anchor for type II membrane protein"; /evidence="ECO:0000255
uniprot
proteins