CLN3_CANLF
ID CLN3_CANLF Reviewed; 438 AA.
AC Q29611;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=Battenin {ECO:0000250|UniProtKB:Q13286};
DE AltName: Full=Protein CLN3;
DE Flags: Precursor;
GN Name=CLN3 {ECO:0000250|UniProtKB:Q13286};
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=9590435;
RX DOI=10.1002/(sici)1097-4547(19980501)52:3<268::aid-jnr3>3.0.co;2-b;
RA Shibuya H., Liu P.-C., Katz M.L., Siakotos A.N., Nonneman D.J.,
RA Johnson G.S.;
RT "Coding sequence and exon/intron organization of the canine CLN3 (Batten
RT disease) gene and its exclusion as the locus for ceroid-lipofuscinosis in
RT English setter dogs.";
RL J. Neurosci. Res. 52:268-275(1998).
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. Facilitates the proteins
CC transport from trans-Golgi network (TGN)-to other membrane compartments
CC such as transport of microdomain-associated proteins to the plasma
CC membrane, IGF2R transport to the lysosome where it regulates the CTSD
CC release leading to regulation of CTSD maturation and thereby APP
CC intracellular processing (By similarity). 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. At the plasma membrane, regulates actin-
CC dependent events including filopodia formation, cell migration, and
CC pinocytosis through ARF1-CDC42 pathway and also the cytoskeleton
CC organization through interaction with MYH10 and fodrin leading to the
CC regulation of the plasma membrane association of Na+, K+ ATPase
CC complex. Regulates synaptic transmission in the amygdala, hippocampus,
CC and cerebellum through regulation of synaptic vesicles density and
CC their proximity to active zones leading to modulation of short-term
CC plasticity and age-dependent anxious behavior, learning and memory.
CC Regulates autophagic vacuoles (AVs) maturation by modulating the
CC trafficking between endocytic and autophagolysosomal/lysosomal
CC compartments, which involves vesicle fusion leading to regulation of
CC degradation process. Participates also in cellular homeostasis of
CC compounds such as, water, ions, amino acids, proteins and lipids in
CC several tissue namely in brain and kidney through regulation of their
CC transport and synthesis (By similarity). {ECO:0000250|UniProtKB:Q13286,
CC ECO:0000250|UniProtKB:Q61124}.
CC -!- SUBUNIT: Interacts with DCTN1, KIF3A, RAB7A and RILP. Interacts with
CC CLN5. {ECO:0000250|UniProtKB:Q13286}.
CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:Q13286};
CC Multi-pass membrane protein {ECO:0000255}. Late endosome
CC {ECO:0000250|UniProtKB:Q13286}. Lysosome
CC {ECO:0000250|UniProtKB:Q13286}.
CC -!- PTM: Highly glycosylated. {ECO:0000250|UniProtKB:Q13286}.
CC -!- PTM: Farnesylation is important for trafficking to lysosomes.
CC {ECO:0000250|UniProtKB:Q13286}.
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; L76281; AAB05546.1; -; Genomic_DNA.
DR EMBL; L76282; AAB05547.1; -; Genomic_DNA.
DR EMBL; AF033661; AAB86972.1; -; Genomic_DNA.
DR EMBL; AF033656; AAB86972.1; JOINED; Genomic_DNA.
DR EMBL; AF033657; AAB86972.1; JOINED; Genomic_DNA.
DR EMBL; AF033658; AAB86972.1; JOINED; Genomic_DNA.
DR EMBL; AF033659; AAB86972.1; JOINED; Genomic_DNA.
DR EMBL; AF033660; AAB86972.1; JOINED; Genomic_DNA.
DR AlphaFoldDB; Q29611; -.
DR STRING; 9612.ENSCAFP00000025242; -.
DR PaxDb; Q29611; -.
DR eggNOG; KOG3880; Eukaryota.
DR InParanoid; Q29611; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0044754; C:autolysosome; ISS:UniProtKB.
DR GO; GO:0005901; C:caveola; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; ISS: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; ISS:UniProtKB.
DR GO; GO:0051861; F:glycolipid binding; ISS:UniProtKB.
DR GO; GO:0120146; F:sulfatide binding; ISS:UniProtKB.
DR GO; GO:0042987; P:amyloid precursor protein catabolic process; ISS:UniProtKB.
DR GO; GO:0061909; P:autophagosome-lysosome fusion; ISS:UniProtKB.
DR GO; GO:0009992; P:cellular water homeostasis; ISS:UniProtKB.
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:1903826; P:L-arginine transmembrane transport; ISS:UniProtKB.
DR GO; GO:0007611; P:learning or memory; ISS: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; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0090384; P:phagosome-lysosome docking; ISS:UniProtKB.
DR GO; GO:0090385; P:phagosome-lysosome fusion; ISS:UniProtKB.
DR GO; GO:0044857; P:plasma membrane raft organization; ISS:UniProtKB.
DR GO; GO:2001288; P:positive regulation of caveolin-mediated endocytosis; ISS:UniProtKB.
DR GO; GO:0042998; P:positive regulation of Golgi to plasma membrane protein transport; ISS:UniProtKB.
DR GO; GO:0048549; P:positive regulation of pinocytosis; ISS:UniProtKB.
DR GO; GO:0006898; P:receptor-mediated endocytosis; ISS:UniProtKB.
DR GO; GO:1900079; P:regulation of arginine biosynthetic process; ISS:UniProtKB.
DR GO; GO:1901096; P:regulation of autophagosome maturation; ISS: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:0010762; P:regulation of fibroblast migration; ISS:UniProtKB.
DR GO; GO:1905244; P:regulation of modification of synaptic structure; ISS:UniProtKB.
DR GO; GO:1905162; P:regulation of phagosome maturation; ISS:UniProtKB.
DR GO; GO:1903076; P:regulation of protein localization to plasma membrane; ISS:UniProtKB.
DR GO; GO:0070613; P:regulation of protein processing; ISS:UniProtKB.
DR GO; GO:0048172; P:regulation of short-term neuronal synaptic plasticity; ISS:UniProtKB.
DR GO; GO:0032228; P:regulation of synaptic transmission, GABAergic; ISS:UniProtKB.
DR GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; ISS:UniProtKB.
DR GO; GO:0036359; P:renal potassium excretion; ISS:UniProtKB.
DR GO; GO:0047496; P:vesicle transport along microtubule; ISS:UniProtKB.
DR Gene3D; 1.20.1250.20; -; 1.
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 3: Inferred from homology;
KW Endosome; Glycoprotein; Lipoprotein; Lysosome; Membrane; Methylation;
KW Phosphoprotein; Prenylation; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..435
FT /note="Battenin"
FT /id="PRO_0000089856"
FT PROPEP 436..438
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:Q13286"
FT /id="PRO_0000422289"
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..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 68..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..267
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 COMPBIAS 251..267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13286"
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"
SQ SEQUENCE 438 AA; 47933 MW; 7964662FCDB33879 CRC64;
MGGCAGSRRR LLDSEEEETA PEPRPPRSYH KGALWKNVMG FWLLGLCNNF SYVVMLSAAH
DILSHQRASG NQSHVDPDPP PTAHNSSSRF DCNSVSTAAV LLADILPTLI IKLLAPLGLH
LLPYSPRVLV SGICAAGSFI LVAFSHSVGT SLCGVVLASI SSGVGEVTFL SLTAFYPRAV
ISWWSSGTGG AGLMGALSYL GLTQAGLSPQ HTLLSMLGIP ALMLASYFFL LTSPEPQDPG
GEEEAETSAR QPLIDSETPE SKPDSSSNLS LQERWTVFKG LLWYIVPLVL VYFAEYFINQ
GLFELLFFRN TSLNHAQQYR WYQMLYQAGV FVSRSSLHCC RIRFTWVLAL LQCLNLAFLL
VDVWFSFLPS IYLVFLIILY EGLLGGAAYV NTFHNIALET SDQHREFAMA AACISDTLGI
SLSGLLALPL HDFLCHLS
