ID   CLN8_CANLF              Reviewed;         288 AA.
AC   Q5JZQ7; Q2VUD9;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Protein CLN8;
GN   Name=CLN8;
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].
RA   Droegemueller C., Woehlke A., Distl O.;
RT   "Characterization of candidate genes for neuronal ceroid lipofuscinosis in
RT   Tibetan terrier dogs.";
RL   Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], INVOLVEMENT IN NCL, AND VARIANT NCL
RP   PRO-164.
RX   PubMed=15629147; DOI=10.1016/j.bbrc.2004.12.038;
RA   Katz M.L., Khan S., Awano T., Shahid S.A., Siakotos A.N., Johnson G.S.;
RT   "A mutation in the CLN8 gene in English Setter dogs with neuronal ceroid-
RT   lipofuscinosis.";
RL   Biochem. Biophys. Res. Commun. 327:541-547(2005).
CC   -!- FUNCTION: Could play a role in cell proliferation during neuronal
CC       differentiation and in protection against cell death.
CC       {ECO:0000250|UniProtKB:Q9UBY8}.
CC   -!- SUBUNIT: Interacts with CLN5. Interacts with CLN3 (By similarity).
CC       {ECO:0000250|UniProtKB:Q9QUK3, ECO:0000250|UniProtKB:Q9UBY8}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q9UBY8}; Multi-pass membrane protein
CC       {ECO:0000255}. Endoplasmic reticulum-Golgi intermediate compartment
CC       membrane {ECO:0000250|UniProtKB:Q9UBY8}; Multi-pass membrane protein
CC       {ECO:0000255}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9UBY8}.
CC   -!- DISEASE: Note=Defects in CLN8 are a cause of a form of neuronal ceroid
CC       lipofuscinosis (NCL) in English setters. {ECO:0000269|PubMed:15629147}.
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DR   EMBL; AJ875419; CAI44940.1; -; mRNA.
DR   EMBL; AY785294; AAW34405.1; -; Genomic_DNA.
DR   EMBL; AY785293; AAW34405.1; JOINED; Genomic_DNA.
DR   RefSeq; NP_001012343.1; NM_001012343.1.
DR   RefSeq; XP_005640493.1; XM_005640436.2.
DR   AlphaFoldDB; Q5JZQ7; -.
DR   STRING; 9615.ENSCAFP00000024048; -.
DR   PaxDb; Q5JZQ7; -.
DR   Ensembl; ENSCAFT00030029025; ENSCAFP00030025303; ENSCAFG00030015756.
DR   Ensembl; ENSCAFT00040023273; ENSCAFP00040020187; ENSCAFG00040012616.
DR   Ensembl; ENSCAFT00845033703; ENSCAFP00845026384; ENSCAFG00845019093.
DR   GeneID; 488558; -.
DR   KEGG; cfa:488558; -.
DR   CTD; 2055; -.
DR   VEuPathDB; HostDB:ENSCAFG00845019093; -.
DR   eggNOG; KOG4561; Eukaryota.
DR   GeneTree; ENSGT01010000222313; -.
DR   HOGENOM; CLU_951678_0_0_1; -.
DR   InParanoid; Q5JZQ7; -.
DR   OMA; FFRTFDL; -.
DR   OrthoDB; 1354968at2759; -.
DR   TreeFam; TF331146; -.
DR   Proteomes; UP000002254; Chromosome 37.
DR   Bgee; ENSCAFG00000016330; Expressed in mucosa of urinary bladder and 47 other tissues.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; ISS:UniProtKB.
DR   GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0097001; F:ceramide binding; ISS:UniProtKB.
DR   GO; GO:0006672; P:ceramide metabolic process; ISS:UniProtKB.
DR   GO; GO:0008203; P:cholesterol metabolic process; ISS:UniProtKB.
DR   GO; GO:0055088; P:lipid homeostasis; IBA:GO_Central.
DR   GO; GO:0007399; P:nervous system development; ISS:UniProtKB.
DR   GO; GO:0006644; P:phospholipid metabolic process; ISS:UniProtKB.
DR   InterPro; IPR006634; TLC-dom.
DR   Pfam; PF03798; TRAM_LAG1_CLN8; 1.
DR   SMART; SM00724; TLC; 1.
DR   PROSITE; PS50922; TLC; 1.
PE   1: Evidence at protein level;
KW   Disease variant; Endoplasmic reticulum; Membrane; Neurodegeneration;
KW   Neuronal ceroid lipofuscinosis; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..288
FT                   /note="Protein CLN8"
FT                   /id="PRO_0000185536"
FT   TRANSMEM        25..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        71..91
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        103..123
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        131..151
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        225..245
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          62..262
FT                   /note="TLC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00205"
FT   REGION          269..288
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           285..288
FT                   /note="ER-retrieval signal"
FT                   /evidence="ECO:0000250"
FT   VARIANT         164
FT                   /note="L -> P (in NCL)"
FT                   /evidence="ECO:0000269|PubMed:15629147"
SQ   SEQUENCE   288 AA;  32639 MW;  77E7AFFA22BB6B34 CRC64;
     MTPMSDGGTS ESIFDLDYTS WKIRSTLAVA GFVFYLGVFV VCHQLSSSLN ATYRSLVARE
     KVFWNLAATR AVFGVQSTAA GLWALLVDPV LHADKARGQQ NWCWFHIATA TGFFFFENVA
     VHLSNVLFRT FDLFLAIHHL FAFLGFLGSV VNLGAGHYLA MSTLLLEAST PFTCISWMLL
     KAGWSESLFW KLNQWLMIHM FHCRMVLTYH MWWVCFWHWD GLVSSLYLPH LALFLVGLGL
     LTLVINPYWT HKKTQQLLNP VDWNFAQPAP RSSRPAGANG QVPQKKGQ