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O75503 (CLN5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 117. 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·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ceroid-lipofuscinosis neuronal protein 5

Short name=Protein CLN5
Gene names
Name:CLN5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length358 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Subcellular location

Lysosome Ref.4.

Tissue specificity

Ubiquitous.

Post-translational modification

Glycosylated. Ref.4

Involvement in disease

Ceroid lipofuscinosis, neuronal, 5 (CLN5) [MIM:256731]: A form of neuronal ceroid lipofuscinosis. 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 5 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

Sequence similarities

Belongs to the CLN5 family.

Sequence caution

The sequence AAC27614.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Cellular componentLysosome
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
Epilepsy
Neurodegeneration
Neuronal ceroid lipofuscinosis
   DomainSignal
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbrain development

Inferred from expression pattern PubMed 10992246. Source: UniProtKB

cell death

Inferred from electronic annotation. Source: UniProtKB-KW

glycosylation

Inferred from direct assay PubMed 16399764. Source: UniProtKB

lysosomal lumen acidification

Inferred from mutant phenotype PubMed 11722572. Source: UniProtKB

neurogenesis

Inferred from expression pattern PubMed 10992246. Source: UniProtKB

neuron maturation

Non-traceable author statement PubMed 10992246. Source: UniProtKB

protein catabolic process

Non-traceable author statement PubMed 10740217. Source: UniProtKB

signal peptide processing

Inferred from direct assay PubMed 20052765. Source: UniProtKB

visual perception

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentGolgi apparatus

Inferred from direct assay PubMed 12134079. Source: UniProtKB

endoplasmic reticulum

Inferred from direct assay PubMed 12134079. Source: UniProtKB

integral component of membrane

Inferred from direct assay PubMed 12134079. Source: UniProtKB

lysosomal membrane

Inferred from direct assay PubMed 12134079. Source: UniProtKB

lysosome

Inferred from direct assay Ref.4. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from direct assay PubMed 10992246. Source: UniProtKB

vacuolar lumen

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionmannose binding

Inferred from direct assay PubMed 16399764. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 12134079. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

KRT8P057871EBI-1043514,EBI-297852

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4646 Potential
Chain47 – 358312Ceroid-lipofuscinosis neuronal protein 5
PRO_0000089860

Amino acid modifications

Glycosylation1301N-linked (GlcNAc...) Potential
Glycosylation1431N-linked (GlcNAc...) Potential
Glycosylation1781N-linked (GlcNAc...) Potential
Glycosylation2031N-linked (GlcNAc...) Potential
Glycosylation2551N-linked (GlcNAc...) Potential
Glycosylation2711N-linked (GlcNAc...) Potential
Glycosylation2811N-linked (GlcNAc...) Potential
Glycosylation3521N-linked (GlcNAc...) Potential

Natural variations

Natural variant261W → R in CLN5. Ref.9
VAR_066895
Natural variant631R → H in CLN5. Ref.5 Ref.9
VAR_042700
Natural variant631R → P in CLN5. Ref.6
VAR_042702
Natural variant771C → Y in CLN5. Ref.9
VAR_066896
Natural variant1431N → S in CLN5. Ref.9
VAR_066897
Natural variant1491L → P in CLN5. Ref.9
VAR_066898
Natural variant1561P → S in CLN5. Ref.9
VAR_066899
Natural variant1581W → R in CLN5. Ref.9
VAR_066900
Natural variant1581W → S in CLN5. Ref.9
VAR_066901
Natural variant1931N → K in CLN5. Ref.9
VAR_066902
Natural variant2091Y → D in CLN5. Ref.7 Ref.9
VAR_042701
Natural variant2191E → A.
Corresponds to variant rs11842935 [ dbSNP | Ensembl ].
VAR_059031
Natural variant2301D → N in CLN5. Ref.1 Ref.6
VAR_005137
Natural variant3191K → R. Ref.1
Corresponds to variant rs1800209 [ dbSNP | Ensembl ].
VAR_005138
Natural variant3251Y → C in CLN5. Ref.9
VAR_066903
Natural variant3301W → C in CLN5; retained in the endoplasmic reticulum rather than reaching the lysosome. Ref.8
VAR_059032

Experimental info

Sequence conflict571Y → C in BAG52069. Ref.2
Sequence conflict921I → T in BAG52069. Ref.2

Sequences

Sequence LengthMass (Da)Tools
O75503 [UniParc].

Last modified April 29, 2008. Version 2.
Checksum: 07E49D4913685190

FASTA35841,497
        10         20         30         40         50         60 
MAQEVDTAQG AEMRRGAGAA RGRASWCWAL ALLWLAVVPG WSRVSGIPSR RHWPVPYKRF 

        70         80         90        100        110        120 
DFRPKPDPYC QAKYTFCPTG SPIPVMEGDD DIEVFRLQAP VWEFKYGDLL GHLKIMHDAI 

       130        140        150        160        170        180 
GFRSTLTGKN YTMEWYELFQ LGNCTFPHLR PEMDAPFWCN QGAACFFEGI DDVHWKENGT 

       190        200        210        220        230        240 
LVQVATISGN MFNQMAKWVK QDNETGIYYE TWNVKASPEK GAETWFDSYD CSKFVLRTFN 

       250        260        270        280        290        300 
KLAEFGAEFK NIETNYTRIF LYSGEPTYLG NETSVFGPTG NKTLGLAIKR FYYPFKPHLP 

       310        320        330        340        350 
TKEFLLSLLQ IFDAVIVHKQ FYLFYNFEYW FLPMKFPFIK ITYEEIPLPI RNKTLSGL 

« Hide

References

« Hide 'large scale' references
[1]"CLN5, a novel gene encoding a putative transmembrane protein mutated in Finnish variant late infantile neuronal ceroid lipofuscinosis."
Savukoski M., Klockars T., Holmberg V., Santavuori P., Lander E.S., Peltonen L.
Nat. Genet. 19:286-288(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT CLN5 ASN-230, VARIANT ARG-319.
Tissue: Fetal brain.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Placenta.
[3]"The DNA sequence and analysis of human chromosome 13."
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"Lysosomal localization of the neuronal ceroid lipofuscinosis CLN5 protein."
Isosomppi J., Vesa J., Jalanko A., Peltonen L.
Hum. Mol. Genet. 11:885-891(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, GLYCOSYLATION.
[5]"A CLN5 mutation causing an atypical neuronal ceroid lipofuscinosis of juvenile onset."
Pineda-Trujillo N., Cornejo W., Carrizosa J., Wheeler R.B., Munera S., Valencia A., Agudelo-Arango J., Cogollo A., Anderson G., Bedoya G., Mole S.E., Ruiz-Linares A.
Neurology 64:740-742(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CLN5 HIS-63.
[6]"Two novel CLN5 mutations in a Portuguese patient with vLINCL: insights into molecular mechanisms of CLN5 deficiency."
Bessa C., Teixeira C.A., Mangas M., Dias A., Sa Miranda M.C., Guimaraes A., Ferreira J.C., Canas N., Cabral P., Ribeiro M.G.
Mol. Genet. Metab. 89:245-253(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CLN5 PRO-63 AND ASN-230.
[7]"Revelation of a novel CLN5 mutation in early juvenile neuronal ceroid lipofuscinosis."
Cannelli N., Nardocci N., Cassandrini D., Morbin M., Aiello C., Bugiani M., Criscuolo L., Zara F., Striano P., Granata T., Bertini E., Simonati A., Santorelli F.M.
Neuropediatrics 38:46-49(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CLN5 ASP-209.
[8]"Retention of lysosomal protein CLN5 in the endoplasmic reticulum causes neuronal ceroid lipofuscinosis in Asian sibship."
Lebrun A.-H., Storch S., Rueschendorf F., Schmiedt M.-L., Kyttaelae A., Mole S.E., Kitzmueller C., Saar K., Mewasingh L.D., Boda V., Kohlschuetter A., Ullrich K., Braulke T., Schulz A.
Hum. Mutat. 30:E651-E661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CLN5 CYS-330, CHARACTERIZATION OF VARIANT CLN5 CYS-330.
[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 CLN5 ARG-26; HIS-63; TYR-77; SER-143; PRO-149; SER-156; ARG-158; SER-158; LYS-193; ASP-209 AND CYS-325.
+Additional computationally mapped references.

Web resources

NCL CLN5

Neural Ceroid Lipofuscinoses mutation db

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF068227 mRNA. Translation: AAC27614.1. Different initiation.
AK075109 mRNA. Translation: BAG52069.1.
AC001226 Genomic DNA. No translation available.
RefSeqNP_006484.1. NM_006493.2.
UniGeneHs.30213.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107614. 36 interactions.
IntActO75503. 3 interactions.
MINTMINT-4656296.
STRING9606.ENSP00000366673.

PTM databases

PhosphoSiteO75503.

Proteomic databases

MaxQBO75503.
PaxDbO75503.
PeptideAtlasO75503.
PRIDEO75503.

Protocols and materials databases

DNASU1203.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000377453; ENSP00000366673; ENSG00000102805.
GeneID1203.
KEGGhsa:1203.
UCSCuc001vkc.3. human.

Organism-specific databases

CTD1203.
GeneCardsGC13P077564.
GeneReviewsCLN5.
HGNCHGNC:2076. CLN5.
HPAHPA041788.
MIM256731. phenotype.
608102. gene.
neXtProtNX_O75503.
Orphanet228360. CLN5 disease.
PharmGKBPA26603.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG45312.
HOGENOMHOG000060233.
HOVERGENHBG005345.
InParanoidO75503.
KOK12390.
OrthoDBEOG77DJ65.
PhylomeDBO75503.
TreeFamTF330864.

Gene expression databases

ArrayExpressO75503.
BgeeO75503.
CleanExHS_CLN5.
GenevestigatorO75503.

Family and domain databases

InterProIPR026138. CLN5.
[Graphical view]
PANTHERPTHR15380. PTHR15380. 1 hit.
PfamPF15014. CLN5. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCLN5. human.
GeneWikiCLN5.
GenomeRNAi1203.
NextBio35469383.
PROO75503.
SOURCESearch...

Entry information

Entry nameCLN5_HUMAN
AccessionPrimary (citable) accession number: O75503
Secondary accession number(s): B3KQK7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: April 29, 2008
Last modified: July 9, 2014
This is version 117 of the entry and version 2 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 13

Human chromosome 13: entries, gene names and cross-references to MIM