CLN5_BOVIN
ID CLN5_BOVIN Reviewed; 358 AA.
AC Q1ZYR0;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, 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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INVOLVEMENT IN NCL.
RX PubMed=16935476; DOI=10.1016/j.bbadis.2006.07.008;
RA Houweling P.J., Cavanagh J.A.L., Palmer D.N., Frugier T., Mitchell N.L.,
RA Windsor P.A., Raadsma H.W., Tammen I.;
RT "Neuronal ceroid lipofuscinosis in Devon cattle is caused by a single base
RT duplication (c.662dupG) in the bovine CLN5 gene.";
RL Biochim. Biophys. Acta 1762:890-897(2006).
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 Australian Devon cattle.
CC -!- SIMILARITY: Belongs to the CLN5 family. {ECO:0000305}.
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DR EMBL; DQ421787; ABD83352.1; -; mRNA.
DR RefSeq; NP_001039764.1; NM_001046299.1.
DR AlphaFoldDB; Q1ZYR0; -.
DR SMR; Q1ZYR0; -.
DR STRING; 9913.ENSBTAP00000025093; -.
DR PaxDb; Q1ZYR0; -.
DR PRIDE; Q1ZYR0; -.
DR Ensembl; ENSBTAT00000025093; ENSBTAP00000025093; ENSBTAG00000018846.
DR GeneID; 529186; -.
DR KEGG; bta:529186; -.
DR CTD; 1203; -.
DR VEuPathDB; HostDB:ENSBTAG00000018846; -.
DR VGNC; VGNC:107252; CLN5.
DR eggNOG; ENOG502QPQ5; Eukaryota.
DR GeneTree; ENSGT00390000010065; -.
DR HOGENOM; CLU_050387_0_0_1; -.
DR InParanoid; Q1ZYR0; -.
DR OMA; FRPHQSF; -.
DR OrthoDB; 1227965at2759; -.
DR TreeFam; TF330864; -.
DR Proteomes; UP000009136; Chromosome 12.
DR Bgee; ENSBTAG00000018846; Expressed in liver and 107 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..358
FT /note="Ceroid-lipofuscinosis neuronal protein 5"
FT /id="PRO_0000330469"
FT CHAIN ?..358
FT /note="Ceroid-lipofuscinosis neuronal protein 5, secreted
FT form"
FT /id="PRO_0000438007"
FT TOPO_DOM 1..29
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O75503"
FT TRANSMEM 30..46
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 47..358
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:O75503"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 303..342
FT /note="Membrane-anchoring"
FT /evidence="ECO:0000250|UniProtKB:O75503"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 254
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 270
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 352
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 358 AA; 41227 MW; 610C482FEEB0422D CRC64;
MAQVGSAGPG ACGRRGAGAG AGPERTTWRW APALLWLATA AAVAGDPSRR QWPVPYKRFS
FRPEPDPYCQ AKYTFCPTGS PIPVMKDDDV IEVFRLQAPV WEFKYGDLLG HLKIMHDAIG
FRSTLTEKNY TMEWYELFQL GNCTFPHLRP EMNAPFWCNQ GAACFFEGID DSHWKENGTL
VLVATISGGM FNRMAKWVKQ DNETGIYYET WTVQASPERG AERWFESYDC SKFVLRTYEK
LAELGADFKK IETNYTRIFL YSGEPTYLGN ETSVFGPTGN KTLALAIKKF YYPFKPHLST
KEFLLSLLQI FDAVVIHREF YLFYNFEYWF LPMKYPFIKI TYEEIPLPNR KNRTLSGL
