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Q9UBY8 (CLN8_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein CLN8
Gene names
Name:CLN8
Synonyms:C8orf61
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length286 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Could play a role in cell proliferation during neuronal differentiation and in protection against cell death. Ref.8

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein. Endoplasmic reticulum-Golgi intermediate compartment membrane; Multi-pass membrane protein Ref.4.

Post-translational modification

Does not seem to be N-glycosylated.

Involvement in disease

Ceroid lipofuscinosis, neuronal, 8 (CLN8) [MIM:600143]: A form of neuronal ceroid lipofuscinosis with onset in childhood. Neuronal ceroid lipofuscinoses are progressive neurodegenerative, lysosomal storage diseases characterized by intracellular accumulation of autofluorescent liposomal material, and clinically by seizures, dementia, visual loss, and/or cerebral atrophy. The lipopigment patterns observed most often in neuronal ceroid lipofuscinosis type 8 comprise mixed combinations of granular, curvilinear, and fingerprint profiles.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9

Ceroid lipofuscinosis, neuronal, 8, Northern epilepsy variant (CLN8NE) [MIM:610003]: A form of neuronal ceroid lipofuscinosis clinically characterized by epilepsy that presents between 5 and 10 years of age with frequent tonic-clonic seizures followed by progressive mental retardation. Visual loss is not a prominent feature. Intracellular accumulation of autofluorescent material results in curvilinear and granular profiles on ultrastructural analysis.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.9

Sequence similarities

Contains 1 TLC (TRAM/LAG1/CLN8) domain.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
Membrane
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
Epilepsy
Mental retardation
Neurodegeneration
Neuronal ceroid lipofuscinosis
   DomainTransmembrane
Transmembrane helix
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processL-glutamate uptake involved in synaptic transmission

Inferred from electronic annotation. Source: Ensembl

adult walking behavior

Inferred from electronic annotation. Source: Ensembl

age-dependent response to oxidative stress

Inferred from electronic annotation. Source: Ensembl

associative learning

Inferred from electronic annotation. Source: Ensembl

cell death

Inferred from electronic annotation. Source: UniProtKB-KW

cellular protein catabolic process

Inferred from electronic annotation. Source: Ensembl

ceramide biosynthetic process

Non-traceable author statement PubMed 12151215. Source: UniProtKB

ceramide metabolic process

Inferred from mutant phenotype PubMed 16086686. Source: UniProtKB

cholesterol metabolic process

Inferred from mutant phenotype PubMed 16086686. Source: UniProtKB

lipid biosynthetic process

Non-traceable author statement PubMed 12151215. Source: UniProtKB

lipid transport

Non-traceable author statement PubMed 12151215. Source: UniProtKB

lysosome organization

Inferred from electronic annotation. Source: Ensembl

mitochondrial membrane organization

Inferred from electronic annotation. Source: Ensembl

musculoskeletal movement

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of proteolysis

Non-traceable author statement PubMed 12151215. Source: UniProtKB

negative regulation of transferase activity

Inferred from electronic annotation. Source: Ensembl

nervous system development

Inferred from mutant phenotype Ref.1. Source: UniProtKB

neurofilament cytoskeleton organization

Inferred from electronic annotation. Source: Ensembl

neuromuscular process controlling balance

Inferred from electronic annotation. Source: Ensembl

neuromuscular process controlling posture

Inferred from electronic annotation. Source: Ensembl

phospholipid metabolic process

Inferred from mutant phenotype PubMed 16086686. Source: UniProtKB

photoreceptor cell maintenance

Inferred from electronic annotation. Source: Ensembl

protein catabolic process

Non-traceable author statement PubMed 10740217. Source: UniProtKB

regulation of cell size

Inferred from electronic annotation. Source: Ensembl

retina development in camera-type eye

Inferred from electronic annotation. Source: Ensembl

social behavior

Inferred from electronic annotation. Source: Ensembl

somatic motor neuron differentiation

Inferred from electronic annotation. Source: Ensembl

visual perception

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentendoplasmic reticulum

Inferred from direct assay Ref.4. Source: UniProtKB

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

endoplasmic reticulum-Golgi intermediate compartment

Inferred from direct assay Ref.4. Source: UniProtKB

endoplasmic reticulum-Golgi intermediate compartment membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Non-traceable author statement Ref.1Ref.4. Source: UniProtKB

mitochondrion

Inferred from electronic annotation. Source: GOC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 286286Protein CLN8
PRO_0000185537

Regions

Transmembrane21 – 4121Helical; Potential
Transmembrane62 – 8423Helical; Potential
Transmembrane103 – 12321Helical; Potential
Transmembrane131 – 15121Helical; Potential
Transmembrane226 – 24621Helical; Potential
Domain62 – 262201TLC
Motif283 – 2864ER-retrieval signal

Natural variations

Natural variant161L → M in CLN8; associated with M-170 on the same allele. Ref.5
VAR_026554
Natural variant241R → G in CLN8NE. Ref.1 Ref.9
VAR_013174
Natural variant301A → P in CLN8. Ref.6
VAR_060573
Natural variant611Missing in CLN8. Ref.8
VAR_060574
Natural variant701R → H in CLN8. Ref.9
VAR_066920
Natural variant761Q → R in CLN8. Ref.9
VAR_066921
Natural variant921H → Y.
Corresponds to variant rs34030778 [ dbSNP | Ensembl ].
VAR_031704
Natural variant1071I → S in CLN8. Ref.9
VAR_066922
Natural variant1251N → S in CLN8. Ref.9
Corresponds to variant rs142269885 [ dbSNP | Ensembl ].
VAR_066923
Natural variant1391H → Y in CLN8. Ref.9
VAR_066924
Natural variant1551A → V. Ref.1
VAR_013175
Natural variant1581Y → C in CLN8. Ref.6 Ref.7
VAR_058438
Natural variant1701T → M in CLN8; associated with M-16 on the same allele. Ref.5
Corresponds to variant rs188259026 [ dbSNP | Ensembl ].
VAR_026555
Natural variant1941Q → R in CLN8. Ref.6
VAR_060575
Natural variant2041R → C in CLN8. Ref.5
VAR_026556
Natural variant2131Missing in CLN8. Ref.9
VAR_066925
Natural variant2211G → S in CLN8. Ref.9
VAR_066926
Natural variant2291P → A in CLN8. Ref.9
Corresponds to variant rs150047904 [ dbSNP | Ensembl ].
VAR_066927
Natural variant2371G → R in CLN8. Ref.7 Ref.9
VAR_058439
Natural variant2631W → C in CLN8. Ref.5
Corresponds to variant rs28940569 [ dbSNP | Ensembl ].
VAR_026557
Natural variant2691E → V in CLN8. Ref.9
VAR_066928

Experimental info

Mutagenesis283 – 2842KK → RR: Localizes to the Golgi complex. Ref.4
Sequence conflict2251S → N in AAF13115. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9UBY8 [UniParc].

Last modified April 17, 2007. Version 3.
Checksum: 1A5995B13E14DCDC

FASTA28632,787
        10         20         30         40         50         60 
MNPASDGGTS ESIFDLDYAS WGIRSTLMVA GFVFYLGVFV VCHQLSSSLN ATYRSLVARE 

        70         80         90        100        110        120 
KVFWDLAATR AVFGVQSTAA GLWALLGDPV LHADKARGQQ NWCWFHITTA TGFFCFENVA 

       130        140        150        160        170        180 
VHLSNLIFRT FDLFLVIHHL FAFLGFLGCL VNLQAGHYLA MTTLLLEMST PFTCVSWMLL 

       190        200        210        220        230        240 
KAGWSESLFW KLNQWLMIHM FHCRMVLTYH MWWVCFWHWD GLVSSLYLPH LTLFLVGLAL 

       250        260        270        280 
LTLIINPYWT HKKTQQLLNP VDWNFAQPEA KSRPEGNGQL LRKKRP 

« Hide

References

« Hide 'large scale' references
[1]"The neuronal ceroid lipofuscinoses in human EPMR and mnd mutant mice are associated with mutations in CLN8."
Ranta S., Zhang Y., Ross B., Lonka L., Takkunen E., Messer A., Sharp J., Wheeler R., Kusumi K., Mole S., Liu W., Soares M.B., Bonaldo M.F., Hirvasniemi A., de la Chapelle A., Gilliam T.C., Lehesjoki A.-E.
Nat. Genet. 23:233-236(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT CLN8NE GLY-24, VARIANT VAL-155.
[2]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Uterus.
[4]"The neuronal ceroid lipofuscinosis CLN8 membrane protein is a resident of the endoplasmic reticulum."
Lonka L., Kyttaelae A., Ranta S., Jalanko A., Lehesjoki A.-E.
Hum. Mol. Genet. 9:1691-1697(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF 283-LYS-LYS-284.
[5]"Variant late infantile neuronal ceroid lipofuscinosis in a subset of Turkish patients is allelic to Northern epilepsy."
Ranta S., Topcu M., Tegelberg S., Tan H., Uestuebuetuen A., Saatci I., Dufke A., Enders H., Pohl K., Alembik Y., Mitchell W.A., Mole S.E., Lehesjoki A.-E.
Hum. Mutat. 23:300-305(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CLN8 MET-16; MET-170; CYS-204 AND CYS-263.
[6]"Novel mutations in CLN8 in Italian variant late infantile neuronal ceroid lipofuscinosis: Another genetic hit in the Mediterranean."
Cannelli N., Cassandrini D., Bertini E., Striano P., Fusco L., Gaggero R., Specchio N., Biancheri R., Vigevano F., Bruno C., Simonati A., Zara F., Santorelli F.M.
Neurogenetics 7:111-117(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CLN8 PRO-30; CYS-158 AND ARG-194.
[7]"Mutations in CLN7/MFSD8 are a common cause of variant late-infantile neuronal ceroid lipofuscinosis."
Kousi M., Siintola E., Dvorakova L., Vlaskova H., Turnbull J., Topcu M., Yuksel D., Gokben S., Minassian B.A., Elleder M., Mole S.E., Lehesjoki A.-E.
Brain 132:810-819(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CLN8 CYS-158 AND ARG-237.
[8]"A novel CLN8 mutation in late-infantile-onset neuronal ceroid lipofuscinosis (LINCL) reveals aspects of CLN8 neurobiological function."
Vantaggiato C., Redaelli F., Falcone S., Perrotta C., Tonelli A., Bondioni S., Morbin M., Riva D., Saletti V., Bonaglia M.C., Giorda R., Bresolin N., Clementi E., Bassi M.T.
Hum. Mutat. 30:1104-1116(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CLN8 LYS-61 DEL, FUNCTION.
[9]"Update of the mutation spectrum and clinical correlations of over 360 mutations in eight genes that underlie the neuronal ceroid lipofuscinoses."
Kousi M., Lehesjoki A.E., Mole S.E.
Hum. Mutat. 33:42-63(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CLN8 HIS-70; ARG-76; SER-107; SER-125; TYR-139; TRP-213 DEL; SER-221; ALA-229; ARG-237 AND VAL-269, VARIANT CLN8NE GLY-24.

Web resources

NCL CLN8

Neural Ceroid Lipofuscinoses mutation db

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF123757 mRNA. Translation: AAF13115.1.
AF123758 mRNA. Translation: AAF13116.1.
AF123759 mRNA. Translation: AAF13117.1.
AF123760 mRNA. Translation: AAF13118.1.
AF123761 mRNA. Translation: AAF13119.1.
BT007049 mRNA. Translation: AAP35698.1.
BC007725 mRNA. Translation: AAH07725.1.
CCDSCCDS5956.1.
RefSeqNP_061764.2. NM_018941.3.
XP_005266078.1. XM_005266021.2.
XP_005266079.1. XM_005266022.1.
XP_005266080.1. XM_005266023.1.
XP_005266081.1. XM_005266024.2.
XP_005266082.1. XM_005266025.1.
XP_005266083.1. XM_005266026.2.
XP_005266084.1. XM_005266027.2.
XP_006725816.1. XM_006725753.1.
XP_006725817.1. XM_006725754.1.
XP_006725818.1. XM_006725755.1.
XP_006725819.1. XM_006725756.1.
XP_006725820.1. XM_006725757.1.
XP_006725821.1. XM_006725758.1.
XP_006725822.1. XM_006725759.1.
UniGeneHs.127675.

3D structure databases

ProteinModelPortalQ9UBY8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108369. 31 interactions.
MINTMINT-4723430.
STRING9606.ENSP00000328182.

Polymorphism databases

DMDM145559455.

Proteomic databases

MaxQBQ9UBY8.
PaxDbQ9UBY8.
PRIDEQ9UBY8.

Protocols and materials databases

DNASU2055.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000331222; ENSP00000328182; ENSG00000182372.
GeneID2055.
KEGGhsa:2055.
UCSCuc003wpo.4. human.

Organism-specific databases

CTD2055.
GeneCardsGC08P001699.
GeneReviewsCLN8.
HGNCHGNC:2079. CLN8.
MIM600143. phenotype.
607837. gene.
610003. phenotype.
neXtProtNX_Q9UBY8.
Orphanet228354. CLN8 disease.
1947. Progressive epilepsy - intellectual disability, Finnish type.
PharmGKBPA26606.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG239251.
HOGENOMHOG000111792.
HOVERGENHBG028338.
InParanoidQ9UBY8.
KOK12360.
OMALTYHMWW.
OrthoDBEOG7MSMPD.
PhylomeDBQ9UBY8.
TreeFamTF331146.

Gene expression databases

BgeeQ9UBY8.
CleanExHS_CLN8.
GenevestigatorQ9UBY8.

Family and domain databases

InterProIPR006634. TLC-dom.
[Graphical view]
PfamPF03798. TRAM_LAG1_CLN8. 1 hit.
[Graphical view]
SMARTSM00724. TLC. 1 hit.
[Graphical view]
PROSITEPS50922. TLC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCLN8. human.
GeneWikiCLN8.
GenomeRNAi2055.
NextBio8357.
PROQ9UBY8.
SOURCESearch...

Entry information

Entry nameCLN8_HUMAN
AccessionPrimary (citable) accession number: Q9UBY8
Secondary accession number(s): Q86U71, Q96I95
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: April 17, 2007
Last modified: July 9, 2014
This is version 125 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM