Primary Information |
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BoMiProt ID | Bomi4641 |
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Protein Name | Ceroid-lipofuscinosis neuronal protein 5/Protein CLN5 |
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Organism | Bos taurus |
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Uniprot ID | Q1ZYR0 |
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Milk Fraction | Whey |
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Ref Sequence ID | NP_001039764.1 |
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Aminoacid Length | 358 |
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Molecular Weight | 41227 |
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FASTA Sequence |
Download |
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Gene Name | CLN5 |
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Gene ID | 529186 |
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Protein Existence Status | reviewed |
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Secondary Information |
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Protein Function | role in lysosome fusiom,regulates localization of Rab7 to endosomal membranes and its activation enable retrograde trafficking of the lysosomal sorting receptors,also recruitment of Vps26 into endosomes. |
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Biochemical Properties | consists of 407 amino acids with an N-terminal signal sequence that is cleaved in the ER co-translationally.contains a C-terminal amphipathic helix region that is tightly associated with the membrane |
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PTMs | N glycosylation |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| >sp|Q1ZYR0|CLN5_BOVIN Ceroid-lipofuscinosis neuronal protein 5 OS=Bos taurus OX=9913 GN=CLN5 PE=2 SV=1
MAQVGSAGPGACGRRGAGAGAGPERTTWRWAPALLWLATAAAVAGDPSRRQWPVPYKRFS
FRPEPDPYCQAKYTFCPTGSPIPVMKDDDVIEVFRLQAPVWEFKYGDLLGHLKIMHDAIG
FRSTLTEKN*129YTMEWYELFQLGN*142CTFPHLRPEMNAPFWCNQGAACFFEGIDDSHWKEN*177GTL
VLVATISGGMFNRMAKWVKQDN*202ETGIYYETWTVQASPERGAERWFESYDCSKFVLRTYEK
LAELGADFKKIETN*254YTRIFLYSGEPTYLGN*270ETSVFGPTGN*280KTLALAIKKFYYPFKPHLST
KEFLLSLLQIFDAVVIHREFYLFYNFEYWFLPMKYPFIKITYEEIPLPNRKN*352RTLSGL
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Predicted Disorder Regions | (1-25) |
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DisProt Annotation | |
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TM Helix Prediction | No TM helices |
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Significance of PTMs | In human CLN5 there are eight N-glycosylation consensus sites (N-X-T/S) present (Asparagine residues on position 179, 192, 227, 252, 304, 320, 330, and 401) and all are utilized, with roles involving proper folding, lysosomal targeting and function.N-glycosylated with both high mannose and complex type sugars,which is imp for proper folding and trafficking to the lysosomes.Proteolytic cleavage at the C terminal which takes place beyond the endoplasmic reticulum, and can occur as early as from the trans Golgi network.The N-terminal portion of CLN5 contains the signal peptide, which is cleaved co-translationally during biosynthesis in the ER. |
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Bibliography | 1.De Silva B, Adams J, Lee SY. Proteolytic processing of the neuronal ceroid lipofuscinosis related lysosomal protein CLN5. Exp Cell Res. 2015 Oct 15;338(1):45-53. doi: 10.1016/j.yexcr.2015.08.021. Epub 2015 Sep 3. PMID: 26342652; PMCID: PMC4589533. 2.Mamo A, Jules F, Dumaresq-Doiron K, Costantino S, Lefrancois S. The role of ceroid lipofuscinosis neuronal protein 5 (CLN5) in endosomal sorting. Mol Cell Biol. 2012 May;32(10):1855-66. doi: 10.1128/MCB.06726-11. Epub 2012 Mar 19. PMID: 22431521; PMCID: PMC3347407. |