Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-01221
Entry Name
UniProt Accession
Theoretical PI
5.93
Molecular Weight
47622.99
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Battenin
Protein Synonyms/Alias
Batten disease protein; Protein CLN3;
Gene Name
CLN3
Gene Synonyms/Alias
BTS;
Created Date
01-NOV-1997
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
435
Canonical
LPLHDFLCQLS****
[1][2]
S-Farnesylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Pullarkat RK, Morris GN. Farnesylation of Batten disease CLN3 protein.Neuropediatrics. 1997 Feb;28(1):42-4.[PMID:9151320]
[2] Storch S, Pohl S, Quitsch A, Falley K, Braulke T. C-terminal prenylation ofthe CLN3 membrane glycoprotein is required for efficient endosomal sorting tolysosomes. Traffic. 2007 Apr;8(4):431-44. Epub 2007 Feb 7.[PMID:17286803]
Functional Description
Involved in microtubule-dependent, anterograde transport of late endosomes and lysosomes.
Sequence Annotation
Topological domain: 1 37 Cytoplasmic.
Transmembrane: 38 58 Helical.
Topological domain: 59 127 Lumenal.
Transmembrane: 128 148 Helical.
Topological domain: 149 151 Cytoplasmic.
Transmembrane: 152 172 Helical.
Topological domain: 173 182 Lumenal.
Transmembrane: 183 203 Helical.
Topological domain: 204 277 Cytoplasmic.
Transmembrane: 278 298 Helical.
Topological domain: 299 346 Lumenal.
Transmembrane: 347 367 Helical.
Topological domain: 368 438 Cytoplasmic.
Modified residue: 12 12 Phosphoserine.
Modified residue: 14 14 Phosphoserine.
Modified residue: 435 435 Cysteine methyl ester.
Protein Length
438 AA.
Protein Sequence
(Canonical)
MGGCAGSRRR FSDSEGEETV PEPRLPLLDH QGAHWKNAVG FWLLGLCNNF SYVVMLSAAH  60
DILSHKRTSG NQSHVDPGPT PIPHNSSSRF DCNSVSTAAV LLADILPTLV IKLLAPLGLH  120
LLPYSPRVLV SGICAAGSFV LVAFSHSVGT SLCGVVFASI SSGLGEVTFL SLTAFYPRAV  180
ISWWSSGTGG AGLLGALSYL GLTQAGLSPQ QTLLSMLGIP ALLLASYFLL LTSPEAQDPG  240
GEEEAESAAR QPLIRTEAPE SKPGSSSSLS LRERWTVFKG LLWYIVPLVV VYFAEYFINQ  300
GLFELLFFWN TSLSHAQQYR WYQMLYQAGV FASRSSLRCC RIRFTWALAL LQCLNLVFLL  360
ADVWFGFLPS IYLVFLIILY EGLLGGAAYV NTFHNIALET SDEHREFAMA ATCISDTLGI  420
SLSGLLALPL HDFLCQLS                                                438
FASTA
(Canonical)
>LipidDB-9606-01221|Q13286
MGGCAGSRRRFSDSEGEETVPEPRLPLLDHQGAHWKNAVGFWLLGLCNNFSYVVMLSAAH
DILSHKRTSGNQSHVDPGPTPIPHNSSSRFDCNSVSTAAVLLADILPTLVIKLLAPLGLH
LLPYSPRVLVSGICAAGSFVLVAFSHSVGTSLCGVVFASISSGLGEVTFLSLTAFYPRAV
ISWWSSGTGGAGLLGALSYLGLTQAGLSPQQTLLSMLGIPALLLASYFLLLTSPEAQDPG
GEEEAESAARQPLIRTEAPESKPGSSSSLSLRERWTVFKGLLWYIVPLVVVYFAEYFINQ
GLFELLFFWNTSLSHAQQYRWYQMLYQAGVFASRSSLRCCRIRFTWALALLQCLNLVFLL
ADVWFGFLPSIYLVFLIILYEGLLGGAAYVNTFHNIALETSDEHREFAMAATCISDTLGI
SLSGLLALPLHDFLCQLS
Gene Ontology
GO:0005776; C:autophagic vacuole; ISS:UniProtKB
GO:0005901; C:caveola; IDA:UniProtKB
GO:0005737; C:cytoplasm; IDA:UniProtKB
GO:0005769; C:early endosome; IDA:UniProtKB
GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB
GO:0005794; C:Golgi apparatus; IDA:UniProtKB
GO:0000139; C:Golgi membrane; IDA:UniProtKB
GO:0005795; C:Golgi stack; IDA:UniProtKB
GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:UniProtKB
GO:0016021; C:integral component of membrane; IDA:UniProtKB
GO:0005770; C:late endosome; IDA:UniProtKB
GO:0005765; C:lysosomal membrane; IDA:UniProtKB
GO:0005764; C:lysosome; IDA:UniProtKB
GO:0045121; C:membrane raft; IDA:UniProtKB
GO:0005739; C:mitochondrion; TAS:ProtInc
GO:0043005; C:neuron projection; IDA:UniProtKB
GO:0005634; C:nucleus; IDA:UniProtKB
GO:0005886; C:plasma membrane; IDA:UniProtKB
GO:0008021; C:synaptic vesicle; IDA:UniProtKB
GO:0005802; C:trans-Golgi network; IDA:UniProtKB
GO:0051082; F:unfolded protein binding; TAS:ProtInc
GO:0001508; P:action potential; ISS:UniProtKB
GO:0042987; P:amyloid precursor protein catabolic process; IDA:UniProtKB
GO:0015809; P:arginine transport; IDA:UniProtKB
GO:0008306; P:associative learning; ISS:UniProtKB
GO:0000046; P:autophagic vacuole fusion; ISS:UniProtKB
GO:0008219; P:cell death; IEA:UniProtKB-KW
GO:0006520; P:cellular amino acid metabolic process; ISS:UniProtKB
GO:0006672; P:ceramide metabolic process; IDA:UniProtKB
GO:0051480; P:cytosolic calcium ion homeostasis; ISS:UniProtKB
GO:0006681; P:galactosylceramide metabolic process; IMP:UniProtKB
GO:0001575; P:globoside metabolic process; IMP:UniProtKB
GO:0006678; P:glucosylceramide metabolic process; IMP:UniProtKB
GO:0035235; P:ionotropic glutamate receptor signaling pathway; ISS:UniProtKB
GO:0007042; P:lysosomal lumen acidification; IMP:UniProtKB
GO:0035752; P:lysosomal lumen pH elevation; IDA:UniProtKB
GO:0007040; P:lysosome organization; ISS:UniProtKB
GO:0016236; P:macroautophagy; NAS:UniProtKB
GO:0061024; P:membrane organization; ISS:UniProtKB
GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB
GO:0043086; P:negative regulation of catalytic activity; ISS:UniProtKB
GO:0016242; P:negative regulation of macroautophagy; ISS:UniProtKB
GO:0043524; P:negative regulation of neuron apoptotic process; ISS:UniProtKB
GO:0045861; P:negative regulation of proteolysis; ISS:UniProtKB
GO:0050885; P:neuromuscular process controlling balance; ISS:UniProtKB
GO:0042133; P:neurotransmitter metabolic process; ISS:UniProtKB
GO:0030163; P:protein catabolic process; NAS:UniProtKB
GO:0016485; P:protein processing; ISS:UniProtKB
GO:0006898; P:receptor-mediated endocytosis; IMP:UniProtKB
GO:0006684; P:sphingomyelin metabolic process; IMP:UniProtKB
GO:0007034; P:vacuolar transport; IBA:RefGenome
GO:0047496; P:vesicle transport along microtubule; IMP:UniProtKB
Interpro
InterPro; IPR003492; Battenin_disease_Cln3
InterPro; IPR018460; Battenin_disease_Cln3_subgr
InterPro; IPR016196; MFS_dom_general_subst_transpt
Pfam
Pfam; PF02487; CLN3;
SMART
PROSITE
PRINTS
PRINTS; PR01315; BATTENIN;