CLN5_CANLF
ID CLN5_CANLF Reviewed; 350 AA.
AC Q5JZQ9; Q5D6C2;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Ceroid-lipofuscinosis neuronal protein 5;
DE Short=Protein CLN5;
DE Contains:
DE RecName: Full=Ceroid-lipofuscinosis neuronal protein 5, secreted form;
GN Name=CLN5;
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 [MRNA].
RX PubMed=15958790; DOI=10.1093/jhered/esi088;
RA Drogemuller C., Wohlke A., Distl O.;
RT "Characterization of candidate genes for neuronal ceroid lipofuscinosis in
RT dog.";
RL J. Hered. 96:735-738(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 51-350, AND INVOLVEMENT IN NCL.
RX PubMed=16033706; DOI=10.1016/j.ygeno.2005.06.005;
RA Melville S.A., Wilson C.L., Chiang C.S., Studdert V.P., Lingaas F.,
RA Wilton A.N.;
RT "A mutation in canine CLN5 causes neuronal ceroid lipofuscinosis in Border
RT collie dogs.";
RL Genomics 86:287-294(2005).
CC -!- FUNCTION: Plays a role in influencing the retrograde trafficking of
CC lysosomal sorting receptors SORT1 and IGF2R from the endosomes to the
CC trans-Golgi network by controlling the recruitment of retromer complex
CC to the endosomal membrane. Regulates the localization and activation of
CC RAB7A which is required to recruit the retromer complex to the
CC endosomal membrane. {ECO:0000250|UniProtKB:O75503}.
CC -!- SUBUNIT: Interacts with SORT1, RAB5A and RAB7A. Interacts with PPT1,
CC TPP1, CLN3, CLN6, CLN8, ATP5F1A and ATP5F1B.
CC {ECO:0000250|UniProtKB:O75503, ECO:0000250|UniProtKB:Q3UMW8}.
CC -!- SUBCELLULAR LOCATION: [Ceroid-lipofuscinosis neuronal protein 5,
CC secreted form]: Lysosome {ECO:0000250|UniProtKB:O75503}.
CC -!- SUBCELLULAR LOCATION: [Ceroid-lipofuscinosis neuronal protein 5]:
CC Membrane {ECO:0000250|UniProtKB:O75503}; Single-pass type II membrane
CC protein {ECO:0000250|UniProtKB:O75503}. Note=An amphipathic anchor
CC region facilitates its association with the membrane.
CC {ECO:0000250|UniProtKB:O75503}.
CC -!- PTM: N-glycosylated with both high mannose and complex type sugars.
CC Glycosylation is important for proper folding and trafficking to the
CC lysosomes. {ECO:0000250|UniProtKB:O75503}.
CC -!- PTM: [Ceroid-lipofuscinosis neuronal protein 5]: The type II membrane
CC signal anchor is proteolytically cleaved to produce a mature form that
CC is transported to the lysosomes (Ceroid-lipofuscinosis neuronal protein
CC 5, secreted form). {ECO:0000250|UniProtKB:O75503}.
CC -!- PTM: Can undergo proteolytic cleavage at the C-terminus, probably by a
CC cysteine protease and may involve the removal of approximately 10-15
CC residues from the C-terminal end. {ECO:0000250|UniProtKB:O75503}.
CC -!- DISEASE: Note=Defects in CLN5 are the cause of neuronal ceroid
CC lipofuscinosis (NCL). NCL is characterized by brain atrophy and the
CC accumulation of lysosome derived fluorescent storage bodies in neurons
CC and most other cells. NCL is found in Border collie dogs.
CC -!- SIMILARITY: Belongs to the CLN5 family. {ECO:0000305}.
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DR EMBL; AJ875417; CAI44938.1; -; mRNA.
DR EMBL; AH014663; AAX10107.1; -; Genomic_DNA.
DR RefSeq; NP_001011556.1; NM_001011556.1.
DR AlphaFoldDB; Q5JZQ9; -.
DR SMR; Q5JZQ9; -.
DR STRING; 9615.ENSCAFP00000007554; -.
DR PaxDb; Q5JZQ9; -.
DR Ensembl; ENSCAFT00030014466; ENSCAFP00030012616; ENSCAFG00030007821.
DR Ensembl; ENSCAFT00040016641; ENSCAFP00040014421; ENSCAFG00040008928.
DR Ensembl; ENSCAFT00845046325; ENSCAFP00845036378; ENSCAFG00845026181.
DR GeneID; 485498; -.
DR KEGG; cfa:485498; -.
DR CTD; 1203; -.
DR VEuPathDB; HostDB:ENSCAFG00845026181; -.
DR eggNOG; ENOG502QPQ5; Eukaryota.
DR GeneTree; ENSGT00390000010065; -.
DR HOGENOM; CLU_050387_0_0_1; -.
DR InParanoid; Q5JZQ9; -.
DR OMA; FRPHQSF; -.
DR OrthoDB; 1227965at2759; -.
DR TreeFam; TF330864; -.
DR Proteomes; UP000002254; Chromosome 22.
DR Bgee; ENSCAFG00000005071; Expressed in saliva-secreting gland and 49 other tissues.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0005775; C:vacuolar lumen; IEA:Ensembl.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IBA:GO_Central.
DR GO; GO:0005537; F:mannose binding; ISS:UniProtKB.
DR GO; GO:0007420; P:brain development; ISS:UniProtKB.
DR GO; GO:0070085; P:glycosylation; ISS:UniProtKB.
DR GO; GO:0007042; P:lysosomal lumen acidification; ISS:UniProtKB.
DR GO; GO:0007040; P:lysosome organization; IBA:GO_Central.
DR GO; GO:0022008; P:neurogenesis; ISS:UniProtKB.
DR GO; GO:1904426; P:positive regulation of GTP binding; ISS:UniProtKB.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISS:UniProtKB.
DR GO; GO:0006465; P:signal peptide processing; ISS:UniProtKB.
DR GO; GO:0007601; P:visual perception; IEA:Ensembl.
DR InterPro; IPR026138; CLN5.
DR PANTHER; PTHR15380; PTHR15380; 1.
DR Pfam; PF15014; CLN5; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Lysosome; Membrane; Neurodegeneration;
KW Neuronal ceroid lipofuscinosis; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..350
FT /note="Ceroid-lipofuscinosis neuronal protein 5"
FT /id="PRO_0000330470"
FT CHAIN ?..350
FT /note="Ceroid-lipofuscinosis neuronal protein 5, secreted
FT form"
FT /id="PRO_0000438008"
FT TOPO_DOM 1..25
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O75503"
FT TRANSMEM 26..42
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..350
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:O75503"
FT REGION 296..335
FT /note="Membrane-anchoring"
FT /evidence="ECO:0000250|UniProtKB:O75503"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 170
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 247
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 273
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 344
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 350 AA; 40389 MW; B73864B1EF89B2B2 CRC64;
MAQAGSADPG VGGHWAAGPR CAPWRWALAL LWLATAAGGP SRRQWPVPYK RFSFRPEPDP
YCQAKYTFCP TGSPIPVMKG DDVIEVFRLQ TPVWEFKYGN LLGHLKIMHD AIGFKSTLTG
KNYTMEWYEL FQLGNCTFPH LRPEMNAPFW CNQGAACFFE GIDDIHWKEN GTLVLVATIS
GNTFNQMAKW VKRDNETGIY YETWTVQASP TKGAETWFES YDCSKFVLRT YKKLAELGAE
FKKIETNYTR IFLYSGEPTY LGNETSIFGP TGNKTLALAI KRFYYPFKPH LSTKEFLLSI
LQIFDAVIIH REFYLFYNFE YWFLPMKFPF IKITYEEIPL PKRNETLSGL
