CLN3_MOUSE
ID CLN3_MOUSE Reviewed; 438 AA.
AC Q61124; O35934; P70400;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Battenin {ECO:0000305};
DE AltName: Full=Protein CLN3;
DE Flags: Precursor;
GN Name=Cln3 {ECO:0000312|MGI:MGI:107537};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Teratocarcinoma;
RX PubMed=8812504; DOI=10.1006/geno.1996.0410;
RA Lee R.L., Johnson K.R., Lerner T.J.;
RT "Isolation and chromosomal mapping of a mouse homolog of the Batten disease
RT gene CLN3.";
RL Genomics 35:617-619(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=9151313; DOI=10.1055/s-2007-973658;
RA Taschner P.E.M., de Vos N., Breuning M.H.;
RT "Cross-species homology of the CLN3 gene.";
RL Neuropediatrics 28:18-20(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RA Katz M.L., Gao C.-L., Prabhakaram M., Shibuya H., Liu P.-C., Johnson G.S.;
RT "Immunochemical localization of the Batten disease (CLN3) protein in
RT retina.";
RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=10440905;
RX DOI=10.1002/(sici)1097-4547(19990815)57:4<551::aid-jnr15>3.0.co;2-r;
RA Katz M.L., Shibuya H., Liu P.C., Kaur S., Gao C.L., Johnson G.S.;
RT "A mouse gene knockout model for juvenile ceroid-lipofuscinosis (Batten
RT disease).";
RL J. Neurosci. Res. 57:551-556(1999).
RN [6]
RP FUNCTION.
RX PubMed=10191118; DOI=10.1006/mgme.1999.2834;
RA Puranam K.L., Guo W.X., Qian W.H., Nikbakht K., Boustany R.M.;
RT "CLN3 defines a novel antiapoptotic pathway operative in neurodegeneration
RT and mediated by ceramide.";
RL Mol. Genet. Metab. 66:294-308(1999).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=10527801; DOI=10.1006/nbdi.1999.0267;
RA Mitchison H.M., Bernard D.J., Greene N.D., Cooper J.D., Junaid M.A.,
RA Pullarkat R.K., de Vos N., Breuning M.H., Owens J.W., Mobley W.C.,
RA Gardiner R.M., Lake B.D., Taschner P.E., Nussbaum R.L.;
RT "Targeted disruption of the Cln3 gene provides a mouse model for Batten
RT disease. The Batten Mouse Model Consortium [corrected].";
RL Neurobiol. Dis. 6:321-334(1999).
RN [8]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=11590129; DOI=10.1093/hmg/10.19.2123;
RA Luiro K., Kopra O., Lehtovirta M., Jalanko A.;
RT "CLN3 protein is targeted to neuronal synapses but excluded from synaptic
RT vesicles: new clues to Batten disease.";
RL Hum. Mol. Genet. 10:2123-2131(2001).
RN [9]
RP DISRUPTION PHENOTYPE.
RX PubMed=12374761; DOI=10.1093/hmg/11.22.2709;
RA Cotman S.L., Vrbanac V., Lebel L.A., Lee R.L., Johnson K.A., Donahue L.R.,
RA Teed A.M., Antonellis K., Bronson R.T., Lerner T.J., MacDonald M.E.;
RT "Cln3(Deltaex7/8) knock-in mice with the common JNCL mutation exhibit
RT progressive neurologic disease that begins before birth.";
RL Hum. Mol. Genet. 11:2709-2721(2002).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15588329; DOI=10.1186/1471-2202-5-57;
RA Fossale E., Wolf P., Espinola J.A., Lubicz-Nawrocka T., Teed A.M., Gao H.,
RA Rigamonti D., Cattaneo E., MacDonald M.E., Cotman S.L.;
RT "Membrane trafficking and mitochondrial abnormalities precede subunit c
RT deposition in a cerebellar cell model of juvenile neuronal ceroid
RT lipofuscinosis.";
RL BMC Neurosci. 5:57-57(2004).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=16714284; DOI=10.1074/jbc.m602180200;
RA Cao Y., Espinola J.A., Fossale E., Massey A.C., Cuervo A.M.,
RA MacDonald M.E., Cotman S.L.;
RT "Autophagy is disrupted in a knock-in mouse model of juvenile neuronal
RT ceroid lipofuscinosis.";
RL J. Biol. Chem. 281:20483-20493(2006).
RN [12]
RP INTERACTION WITH KCNIP3.
RX PubMed=17189291; DOI=10.1093/hmg/ddl466;
RA Chang J.W., Choi H., Kim H.J., Jo D.G., Jeon Y.J., Noh J.Y., Park W.J.,
RA Jung Y.K.;
RT "Neuronal vulnerability of CLN3 deletion to calcium-induced cytotoxicity is
RT mediated by calsenilin.";
RL Hum. Mol. Genet. 16:317-326(2007).
RN [13]
RP DISRUPTION PHENOTYPE.
RX PubMed=17855597; DOI=10.1523/jneurosci.1710-07.2007;
RA Eliason S.L., Stein C.S., Mao Q., Tecedor L., Ding S.L., Gaines D.M.,
RA Davidson B.L.;
RT "A knock-in reporter model of Batten disease.";
RL J. Neurosci. 27:9826-9834(2007).
RN [14]
RP FUNCTION.
RX PubMed=18621045; DOI=10.1016/j.yexcr.2008.06.016;
RA Uusi-Rauva K., Luiro K., Tanhuanpaeae K., Kopra O., Martin-Vasallo P.,
RA Kyttaelae A., Jalanko A.;
RT "Novel interactions of CLN3 protein link Batten disease to dysregulation of
RT fodrin-Na+, K+ ATPase complex.";
RL Exp. Cell Res. 314:2895-2905(2008).
RN [15]
RP DISRUPTION PHENOTYPE.
RX PubMed=17962032; DOI=10.1016/j.nbd.2007.08.017;
RA Katz M.L., Johnson G.S., Tullis G.E., Lei B.;
RT "Phenotypic characterization of a mouse model of juvenile neuronal ceroid
RT lipofuscinosis.";
RL Neurobiol. Dis. 29:242-253(2008).
RN [16]
RP INTERACTION WITH CLN5, AND SUBCELLULAR LOCATION.
RX PubMed=19941651; DOI=10.1186/1471-2121-10-83;
RA Lyly A., von Schantz C., Heine C., Schmiedt M.L., Sipilae T., Jalanko A.,
RA Kyttaelae A.;
RT "Novel interactions of CLN5 support molecular networking between neuronal
RT ceroid lipofuscinosis proteins.";
RL BMC Cell Biol. 10:83-83(2009).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [18]
RP FUNCTION.
RX PubMed=19284480; DOI=10.1111/j.1365-2990.2008.00984.x;
RA Chan C.H., Ramirez-Montealegre D., Pearce D.A.;
RT "Altered arginine metabolism in the central nervous system (CNS) of the
RT Cln3-/- mouse model of juvenile Batten disease.";
RL Neuropathol. Appl. Neurobiol. 35:189-207(2009).
RN [19]
RP INDUCTION, AND FUNCTION.
RX PubMed=20219947; DOI=10.1152/ajpcell.00272.2009;
RA Stein C.S., Yancey P.H., Martins I., Sigmund R.D., Stokes J.B.,
RA Davidson B.L.;
RT "Osmoregulation of ceroid neuronal lipofuscinosis type 3 in the renal
RT medulla.";
RL Am. J. Physiol. 298:C1388-C1400(2010).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [21]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24227717; DOI=10.1523/jneurosci.0498-13.2013;
RA Tecedor L., Stein C.S., Schultz M.L., Farwanah H., Sandhoff K.,
RA Davidson B.L.;
RT "CLN3 loss disturbs membrane microdomain properties and protein transport
RT in brain endothelial cells.";
RL J. Neurosci. 33:18065-18079(2013).
RN [22]
RP FUNCTION.
RX PubMed=24792215; DOI=10.1371/journal.pone.0096647;
RA Schultz M.L., Tecedor L., Stein C.S., Stamnes M.A., Davidson B.L.;
RT "CLN3 deficient cells display defects in the ARF1-Cdc42 pathway and actin-
RT dependent events.";
RL PLoS ONE 9:E96647-E96647(2014).
RN [23]
RP FUNCTION.
RX PubMed=26450516; DOI=10.1093/hmg/ddv406;
RA Wavre-Shapton S.T., Calvi A.A., Turmaine M., Seabra M.C., Cutler D.F.,
RA Futter C.E., Mitchison H.M.;
RT "Photoreceptor phagosome processing defects and disturbed autophagy in
RT retinal pigment epithelium of Cln3Deltaex1-6 mice modelling juvenile
RT neuronal ceroid lipofuscinosis (Batten disease).";
RL Hum. Mol. Genet. 24:7060-7074(2015).
RN [24]
RP FUNCTION.
RX PubMed=25878248; DOI=10.1074/jbc.m114.621706;
RA Chandrachud U., Walker M.W., Simas A.M., Heetveld S., Petcherski A.,
RA Klein M., Oh H., Wolf P., Zhao W.N., Norton S., Haggarty S.J.,
RA Lloyd-Evans E., Cotman S.L.;
RT "Unbiased Cell-based Screening in a Neuronal Cell Model of Batten Disease
RT Highlights an Interaction between Ca2+ Homeostasis, Autophagy, and CLN3
RT Protein Function.";
RL J. Biol. Chem. 290:14361-14380(2015).
RN [25]
RP FUNCTION.
RX PubMed=29135436; DOI=10.7554/elife.28685;
RA Gruenewald B., Lange M.D., Werner C., O'Leary A., Weishaupt A., Popp S.,
RA Pearce D.A., Wiendl H., Reif A., Pape H.C., Toyka K.V., Sommer C., Geis C.;
RT "Defective synaptic transmission causes disease signs in a mouse model of
RT juvenile neuronal ceroid lipofuscinosis.";
RL Elife 6:0-0(2017).
RN [26]
RP FUNCTION.
RX PubMed=29780879; DOI=10.1523/eneuro.0387-17.2018;
RA Studniarczyk D., Needham E.L., Mitchison H.M., Farrant M., Cull-Candy S.G.;
RT "Altered Cerebellar Short-Term Plasticity but No Change in Postsynaptic
RT AMPA-Type Glutamate Receptors in a Mouse Model of Juvenile Batten
RT Disease.";
RL ENeuro 5:0-0(2018).
CC -!- FUNCTION: Mediates microtubule-dependent, anterograde transport
CC connecting the Golgi network, endosomes, autophagosomes, lysosomes and
CC plasma membrane, and participates in several cellular processes such as
CC regulation of lysosomal pH, lysosome protein degradation, receptor-
CC mediated endocytosis, autophagy, transport of proteins and lipids from
CC the TGN, apoptosis and synaptic transmission (PubMed:10191118,
CC PubMed:24227717, PubMed:15588329, PubMed:29780879, PubMed:26450516,
CC PubMed:16714284, PubMed:25878248, PubMed:17855597). Facilitates the
CC proteins transport from trans-Golgi network (TGN)-to other membrane
CC compartments such as transport of microdomain-associated proteins to
CC the plasma membrane, IGF2R transport to the lysosome where it regulates
CC the CTSD release leading to regulation of CTSD maturation and thereby
CC APP intracellular processing (PubMed:24227717). Moreover regulates CTSD
CC activity in response to osmotic stress (By similarity). Also binds
CC galactosylceramide and transports it from the trans Golgi to the rafts,
CC which may have immediate and downstream effects on cell survival by
CC modulating ceramide synthesis (PubMed:10191118). At the plasma
CC membrane, regulates actin-dependent events including filopodia
CC formation, cell migration, and pinocytosis through ARF1-CDC42 pathway
CC and also the cytoskeleton organization through interaction with MYH10
CC and fodrin leading to the regulation of the plasma membrane association
CC of Na+, K+ ATPase complex (PubMed:18621045, PubMed:24792215). Regulates
CC synaptic transmission in the amygdala, hippocampus, and cerebellum
CC through regulation of synaptic vesicles density and their proximity to
CC active zones leading to modulation of short-term plasticity and age-
CC dependent anxious behavior, learning and memory (PubMed:29135436,
CC PubMed:29780879). Regulates autophagic vacuoles (AVs) maturation by
CC modulating the trafficking between endocytic and
CC autophagolysosomal/lysosomal compartments, which involves vesicle
CC fusion leading to regulation of degradation process (PubMed:16714284,
CC PubMed:25878248, PubMed:26450516). Participates also in cellular
CC homeostasis of compounds such as, water, ions, amino acids, proteins
CC and lipids in several tissue namely in brain and kidney through
CC regulation of their transport and synthesis (PubMed:19284480,
CC PubMed:20219947, PubMed:25878248). {ECO:0000250|UniProtKB:Q13286,
CC ECO:0000269|PubMed:10191118, ECO:0000269|PubMed:15588329,
CC ECO:0000269|PubMed:16714284, ECO:0000269|PubMed:17855597,
CC ECO:0000269|PubMed:18621045, ECO:0000269|PubMed:19284480,
CC ECO:0000269|PubMed:20219947, ECO:0000269|PubMed:24227717,
CC ECO:0000269|PubMed:24792215, ECO:0000269|PubMed:25878248,
CC ECO:0000269|PubMed:26450516, ECO:0000269|PubMed:29135436,
CC ECO:0000269|PubMed:29780879}.
CC -!- SUBUNIT: Homooligomer (PubMed:11590129). Interacts with DCTN1, KIF3A,
CC RAB7A and RILP (By similarity). Interacts with CLN5 (PubMed:19941651).
CC Interacts with KCNIP3 (PubMed:17189291). {ECO:0000250|UniProtKB:Q13286,
CC ECO:0000269|PubMed:11590129, ECO:0000269|PubMed:17189291,
CC ECO:0000269|PubMed:19941651}.
CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:15588329};
CC Multi-pass membrane protein {ECO:0000255}. Late endosome
CC {ECO:0000250|UniProtKB:Q13286}. Lysosome {ECO:0000269|PubMed:11590129,
CC ECO:0000269|PubMed:16714284, ECO:0000269|PubMed:19941651}. Membrane
CC raft {ECO:0000269|PubMed:24227717}. Golgi apparatus, trans-Golgi
CC network {ECO:0000269|PubMed:24227717}. Synapse, synaptosome
CC {ECO:0000269|PubMed:11590129}. Early endosome membrane
CC {ECO:0000269|PubMed:15588329}. Late endosome membrane
CC {ECO:0000269|PubMed:15588329}. Cytoplasmic vesicle, autophagosome
CC {ECO:0000269|PubMed:16714284}. Note=Excluded from the synaptic
CC vesicles. {ECO:0000269|PubMed:11590129}.
CC -!- TISSUE SPECIFICITY: Expressed throughout the brain, such as, in the
CC cerebral cortex, hippocampus, cerebellum and several different cerebral
CC nuclei (at protein level). In the cerebral cortex, expressed in all
CC cortical layers. In the hippocampus, expressed in the granule cells in
CC the dentate gyrus and the pyramidal cells of the hippocampus proper. In
CC the cerebellum expressed in the granular and molecular layers, and in
CC the Purkinje cell layer. {ECO:0000269|PubMed:11590129}.
CC -!- INDUCTION: Expression is osmoregulated in renal medullary cells.
CC {ECO:0000269|PubMed:20219947}.
CC -!- PTM: Highly glycosylated. {ECO:0000250|UniProtKB:Q13286}.
CC -!- PTM: Farnesylation is important for trafficking to lysosomes.
CC {ECO:0000250|UniProtKB:Q13286}.
CC -!- DISRUPTION PHENOTYPE: Embryos are viable and fertile and by 12 months
CC of age do not exhibit obvious clinical signs but have significantly
CC shortened life spans (PubMed:10527801, PubMed:17962032). Mice show
CC elevation of lysosomal enzymes in brain and accumulation of
CC autofluorescent storage material in neurons, retina and other cell
CC types that increases with age (PubMed:10527801, PubMed:10440905,
CC PubMed:17962032, PubMed:17855597). They also show neuropathological
CC abnormalities with loss of certain cortical interneurons and
CC hypertrophy of many interneuron populations in the hippocampus
CC (PubMed:10527801). Moreover display progressive neurological deficits,
CC including impaired motor function, decreased overall activity,
CC acquisition of resting tremors, and increased susceptibility to
CC pentilentetrazole-induced seizures (PubMed:17855597). Mice exhibit
CC progressively impaired inner retinal function, altered pupillary light
CC reflexes, losses of inner retinal neurons, and reduced brain mass. Mice
CC show behavioral changes including reduced spontaneous activity levels
CC and impaired learning and memory (PubMed:17962032). Cln3 hypomorphic
CC mutant mice, harboring the ~1 kb common juvenile neuronal ceroid
CC lipofuscinosis (JNCL) mutation, express multiple Cln3 mRNA splice
CC variants and mutant battenin protein. Homozygous Cln3 mice exhibit a
CC progressive JNCL-like disease, with perinatal onset of subunit c of ATP
CC synthasedeposition in many cell types and later onset of neuronal
CC dysfunction and behavioral deficits (PubMed:12374761). Can serve as an
CC animal model for studying neuronal ceroid lipofuscinosis 3/Batten
CC disease (PubMed:10527801, PubMed:10440905, PubMed:17962032,
CC PubMed:12374761). {ECO:0000269|PubMed:10440905,
CC ECO:0000269|PubMed:10527801, ECO:0000269|PubMed:12374761,
CC ECO:0000269|PubMed:17855597, ECO:0000269|PubMed:17962032}.
CC -!- SIMILARITY: Belongs to the battenin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U47106; AAC52957.1; -; mRNA.
DR EMBL; U68064; AAB07595.1; -; mRNA.
DR EMBL; U92811; AAB69983.1; -; mRNA.
DR EMBL; BC058753; AAH58753.1; -; mRNA.
DR EMBL; BC080759; AAH80759.1; -; mRNA.
DR CCDS; CCDS21833.1; -.
DR RefSeq; NP_001139783.1; NM_001146311.2.
DR RefSeq; NP_034037.3; NM_009907.4.
DR RefSeq; XP_006507351.1; XM_006507288.3.
DR RefSeq; XP_006507352.1; XM_006507289.2.
DR RefSeq; XP_006507353.1; XM_006507290.1.
DR RefSeq; XP_006507355.1; XM_006507292.1.
DR RefSeq; XP_006507356.1; XM_006507293.3.
DR RefSeq; XP_017177452.1; XM_017321963.1.
DR AlphaFoldDB; Q61124; -.
DR STRING; 10090.ENSMUSP00000081636; -.
DR TCDB; 2.A.57.5.1; the equilibrative nucleoside transporter (ent) family.
DR GlyGen; Q61124; 3 sites.
DR iPTMnet; Q61124; -.
DR PhosphoSitePlus; Q61124; -.
DR MaxQB; Q61124; -.
DR PaxDb; Q61124; -.
DR PeptideAtlas; Q61124; -.
DR PRIDE; Q61124; -.
DR ProteomicsDB; 283527; -.
DR Antibodypedia; 26372; 190 antibodies from 29 providers.
DR DNASU; 12752; -.
DR Ensembl; ENSMUST00000032962; ENSMUSP00000032962; ENSMUSG00000030720.
DR Ensembl; ENSMUST00000084589; ENSMUSP00000081636; ENSMUSG00000030720.
DR Ensembl; ENSMUST00000116269; ENSMUSP00000111973; ENSMUSG00000030720.
DR GeneID; 12752; -.
DR KEGG; mmu:12752; -.
DR UCSC; uc009jrx.2; mouse.
DR CTD; 1201; -.
DR MGI; MGI:107537; Cln3.
DR VEuPathDB; HostDB:ENSMUSG00000030720; -.
DR eggNOG; KOG3880; Eukaryota.
DR GeneTree; ENSGT00390000003249; -.
DR HOGENOM; CLU_029663_0_1_1; -.
DR InParanoid; Q61124; -.
DR OMA; WLCNWQV; -.
DR OrthoDB; 1037817at2759; -.
DR PhylomeDB; Q61124; -.
DR TreeFam; TF314055; -.
DR BioGRID-ORCS; 12752; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Cln3; mouse.
DR PRO; PR:Q61124; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q61124; protein.
DR Bgee; ENSMUSG00000030720; Expressed in granulocyte and 234 other tissues.
DR ExpressionAtlas; Q61124; baseline and differential.
DR Genevisible; Q61124; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0044754; C:autolysosome; IDA:UniProtKB.
DR GO; GO:0005776; C:autophagosome; IDA:MGI.
DR GO; GO:0005901; C:caveola; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005769; C:early endosome; IDA:MGI.
DR GO; GO:0031901; C:early endosome membrane; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0005795; C:Golgi stack; ISS:UniProtKB.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0005770; C:late endosome; IDA:MGI.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0055037; C:recycling endosome; ISS:UniProtKB.
DR GO; GO:0008021; C:synaptic vesicle; ISS:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR GO; GO:0005773; C:vacuole; IBA:GO_Central.
DR GO; GO:0048306; F:calcium-dependent protein binding; IPI:MGI.
DR GO; GO:0051861; F:glycolipid binding; ISS:UniProtKB.
DR GO; GO:0120146; F:sulfatide binding; ISS:UniProtKB.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:MGI.
DR GO; GO:0001508; P:action potential; IMP:MGI.
DR GO; GO:0006865; P:amino acid transport; IMP:MGI.
DR GO; GO:0042987; P:amyloid precursor protein catabolic process; ISS:UniProtKB.
DR GO; GO:0008306; P:associative learning; IMP:MGI.
DR GO; GO:0097352; P:autophagosome maturation; IMP:MGI.
DR GO; GO:0061909; P:autophagosome-lysosome fusion; IMP:UniProtKB.
DR GO; GO:0043534; P:blood vessel endothelial cell migration; IMP:MGI.
DR GO; GO:0009992; P:cellular water homeostasis; IMP:UniProtKB.
DR GO; GO:0006897; P:endocytosis; IMP:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0046474; P:glycerophospholipid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0046836; P:glycolipid transport; ISS:UniProtKB.
DR GO; GO:0090160; P:Golgi to lysosome transport; ISS:UniProtKB.
DR GO; GO:0035235; P:ionotropic glutamate receptor signaling pathway; IMP:MGI.
DR GO; GO:1903826; P:L-arginine transmembrane transport; ISS:UniProtKB.
DR GO; GO:0007611; P:learning or memory; IMP:UniProtKB.
DR GO; GO:0007042; P:lysosomal lumen acidification; ISS:UniProtKB.
DR GO; GO:0035752; P:lysosomal lumen pH elevation; ISS:UniProtKB.
DR GO; GO:1905146; P:lysosomal protein catabolic process; IMP:UniProtKB.
DR GO; GO:0007040; P:lysosome organization; IMP:MGI.
DR GO; GO:0016236; P:macroautophagy; IMP:MGI.
DR GO; GO:0061024; P:membrane organization; IMP:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0043086; P:negative regulation of catalytic activity; IMP:MGI.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IDA:MGI.
DR GO; GO:0045861; P:negative regulation of proteolysis; IMP:MGI.
DR GO; GO:0050885; P:neuromuscular process controlling balance; IMP:MGI.
DR GO; GO:0042133; P:neurotransmitter metabolic process; IMP:MGI.
DR GO; GO:0090384; P:phagosome-lysosome docking; IMP:UniProtKB.
DR GO; GO:0090385; P:phagosome-lysosome fusion; IMP:UniProtKB.
DR GO; GO:0044857; P:plasma membrane raft organization; IMP:UniProtKB.
DR GO; GO:2001288; P:positive regulation of caveolin-mediated endocytosis; IMP:UniProtKB.
DR GO; GO:0042998; P:positive regulation of Golgi to plasma membrane protein transport; IMP:UniProtKB.
DR GO; GO:0048549; P:positive regulation of pinocytosis; IMP:UniProtKB.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:MGI.
DR GO; GO:0072657; P:protein localization to membrane; IMP:MGI.
DR GO; GO:0072659; P:protein localization to plasma membrane; IMP:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IMP:MGI.
DR GO; GO:0016485; P:protein processing; IMP:MGI.
DR GO; GO:0006898; P:receptor-mediated endocytosis; ISS:UniProtKB.
DR GO; GO:1900079; P:regulation of arginine biosynthetic process; IMP:UniProtKB.
DR GO; GO:1901096; P:regulation of autophagosome maturation; IMP:UniProtKB.
DR GO; GO:0016243; P:regulation of autophagosome size; IMP:UniProtKB.
DR GO; GO:0010506; P:regulation of autophagy; IMP:UniProtKB.
DR GO; GO:0106049; P:regulation of cellular response to osmotic stress; ISS:UniProtKB.
DR GO; GO:0051493; P:regulation of cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IDA:MGI.
DR GO; GO:0010762; P:regulation of fibroblast migration; ISS:UniProtKB.
DR GO; GO:0051489; P:regulation of filopodium assembly; IMP:MGI.
DR GO; GO:0010468; P:regulation of gene expression; ISO:MGI.
DR GO; GO:0051453; P:regulation of intracellular pH; IBA:GO_Central.
DR GO; GO:1905244; P:regulation of modification of synaptic structure; IMP:UniProtKB.
DR GO; GO:1905162; P:regulation of phagosome maturation; IMP:UniProtKB.
DR GO; GO:1903076; P:regulation of protein localization to plasma membrane; IMP:UniProtKB.
DR GO; GO:0070613; P:regulation of protein processing; ISS:UniProtKB.
DR GO; GO:0048172; P:regulation of short-term neuronal synaptic plasticity; IMP:UniProtKB.
DR GO; GO:0032228; P:regulation of synaptic transmission, GABAergic; IMP:UniProtKB.
DR GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; IMP:UniProtKB.
DR GO; GO:0036359; P:renal potassium excretion; IMP:UniProtKB.
DR GO; GO:0047496; P:vesicle transport along microtubule; ISS:UniProtKB.
DR InterPro; IPR003492; Battenin_disease_Cln3.
DR InterPro; IPR018460; Battenin_disease_Cln3_subgr.
DR InterPro; IPR036259; MFS_trans_sf.
DR PANTHER; PTHR10981; PTHR10981; 1.
DR Pfam; PF02487; CLN3; 1.
DR PIRSF; PIRSF015974; CLN3_BTN1; 1.
DR PRINTS; PR01315; BATTENIN.
DR SUPFAM; SSF103473; SSF103473; 1.
PE 1: Evidence at protein level;
KW Cytoplasmic vesicle; Endosome; Glycoprotein; Golgi apparatus; Lipoprotein;
KW Lysosome; Membrane; Methylation; Phosphoprotein; Prenylation;
KW Reference proteome; Synapse; Synaptosome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..435
FT /note="Battenin"
FT /id="PRO_0000089859"
FT PROPEP 436..438
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:Q13286"
FT /id="PRO_0000422292"
FT TOPO_DOM 1..37
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q13286, ECO:0000255"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 59..127
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 149..151
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 173..182
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 204..277
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q13286, ECO:0000255"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 299..346
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q13286, ECO:0000255"
FT TRANSMEM 347..367
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 368..438
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q13286, ECO:0000255"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 67..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 242..244
FT /note="Lysosomal targeting motif"
FT /evidence="ECO:0000250|UniProtKB:Q13286"
FT MOTIF 253..254
FT /note="Lysosomal targeting motif. Required for AP1G1, AP2A2
FT and AP3D1 interaction"
FT /evidence="ECO:0000250|UniProtKB:Q13286"
FT MOTIF 409..419
FT /note="Lysosomal targeting motif"
FT /evidence="ECO:0000250|UniProtKB:Q13286"
FT COMPBIAS 9..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 435
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250|UniProtKB:Q13286"
FT LIPID 435
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q13286"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 310
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 79
FT /note="P -> R (in Ref. 1; AAC52957)"
FT /evidence="ECO:0000305"
FT CONFLICT 120
FT /note="H -> Y (in Ref. 2; AAB07595)"
FT /evidence="ECO:0000305"
FT CONFLICT 237
FT /note="L -> W (in Ref. 1; AAC52957)"
FT /evidence="ECO:0000305"
FT CONFLICT 317..318
FT /note="QQ -> HE (in Ref. 1; AAC52957)"
FT /evidence="ECO:0000305"
FT CONFLICT 380
FT /note="Y -> H (in Ref. 1; AAC52957)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 438 AA; 47657 MW; 2A06D2CE4728C1AC CRC64;
MGSSAGSWRR LEDSEREETD SEPQAPRLDS RSVLWKNAVG FWILGLCNNF SYVVMLSAAH
DILKQEQASG NQSHVEPGPT PTPHNSSSRF DCNSISTAAV LLADILPTLV IKLLAPLGLH
LLPYSPRVLV SGVCSAGSFV LVAFSQSVGL SLCGVVLASI SSGLGEVTFL SLTAFYPSAV
ISWWSSGTGG AGLLGSLSYL GLTQAGLSPQ HTLLSMLGIP VLLLASYFLL LTSPEPLDPG
GENEAETAAR QPLIGTETPE SKPGASWDLS LQERWTVFKG LLWYIIPLVL VYFAEYFINQ
GLFELLFFRN TSLSHAQQYR WYQMLYQAGV FASRSSLQCC RIRFTWVLAL LQCLNLALLL
ADVCLNFLPS IYLIFIIILY EGLLGGAAYV NTFHNIALET SDKHREFAME AACISDTLGI
SLSGVLALPL HDFLCHLP
