CLN5_SHEEP
ID CLN5_SHEEP Reviewed; 361 AA.
AC A2TJ54;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 25-MAY-2022, entry version 44.
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 Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=17988881; DOI=10.1016/j.nbd.2007.09.006;
RA Frugier T., Mitchell N.L., Tammen I., Houweling P.J., Arthur D.G.,
RA Kay G.W., van Diggelen O.P., Jolly R.D., Palmer D.N.;
RT "A new large animal model of CLN5 neuronal ceroid lipofuscinosis in
RT Borderdale sheep is caused by a nucleotide substitution at a consensus
RT splice site (c.571+1G>>>A) leading to excision of exon 3.";
RL Neurobiol. Dis. 29:306-315(2008).
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 New Zealand Borderdale sheep.
CC -!- SIMILARITY: Belongs to the CLN5 family. {ECO:0000305}.
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DR EMBL; EF204938; ABM91779.1; -; mRNA.
DR RefSeq; NP_001076064.1; NM_001082595.1.
DR AlphaFoldDB; A2TJ54; -.
DR SMR; A2TJ54; -.
DR STRING; 9940.ENSOARP00000017190; -.
DR GeneID; 100034668; -.
DR KEGG; oas:100034668; -.
DR CTD; 1203; -.
DR eggNOG; ENOG502QPQ5; Eukaryota.
DR OrthoDB; 1227965at2759; -.
DR Proteomes; UP000002356; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0005537; F:mannose binding; ISS:UniProtKB.
DR GO; GO:0070085; P:glycosylation; 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 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..361
FT /note="Ceroid-lipofuscinosis neuronal protein 5"
FT /id="PRO_0000330472"
FT CHAIN ?..361
FT /note="Ceroid-lipofuscinosis neuronal protein 5, secreted
FT form"
FT /id="PRO_0000438011"
FT TOPO_DOM 1..30
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O75503"
FT TRANSMEM 31..48
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 49..361
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:O75503"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 306..345
FT /note="Membrane-anchoring"
FT /evidence="ECO:0000250|UniProtKB:O75503"
FT CARBOHYD 132
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 257
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 283
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 355
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 361 AA; 41315 MW; D376EBFCEB4BCCBB CRC64;
MAQAGGAGAG AWGRRGAGAG AGPERAPWRW APALLWLAAA TAAAAAAGDP SRRQWPVPYK
RFSFRPEPDP YCQAKYTFCP TGSPIPVMKD DDVIEVFRLQ APVWEFKYGD LLGHLKIMHD
AIGFRSTLTE KNYTMEWYEL FQLGNCTFPH LRPEMNAPFW CNQGAACFFE GIDDNHWKEN
GTLVLVATIS GGMFNKMAKW VKQDNETGIY YETWTVQASP KKEAEKWFES YDCSKFVLRT
YEKLAELGAD FKKIETNYTR IFLYSGEPTY LGNETSVFGP TGNKTLALAI KKFYYPFKPH
LSTKEFLLSL LQIFDAVVIH REFYLFYNFE YWFLPMKSPF IKITYEEIPL PNRKNRTLSG
L
