CLN5_HUMAN
ID CLN5_HUMAN Reviewed; 358 AA.
AC O75503; B3KQK7;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 176.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], VARIANT CLN5 ASN-230, AND VARIANT ARG-319.
RC TISSUE=Fetal brain;
RX PubMed=9662406; DOI=10.1038/975;
RA Savukoski M., Klockars T., Holmberg V., Santavuori P., Lander E.S.,
RA Peltonen L.;
RT "CLN5, a novel gene encoding a putative transmembrane protein mutated in
RT Finnish variant late infantile neuronal ceroid lipofuscinosis.";
RL Nat. Genet. 19:286-288(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [4]
RP SUBCELLULAR LOCATION, AND GLYCOSYLATION.
RX PubMed=11971870; DOI=10.1093/hmg/11.8.885;
RA Isosomppi J., Vesa J., Jalanko A., Peltonen L.;
RT "Lysosomal localization of the neuronal ceroid lipofuscinosis CLN5
RT protein.";
RL Hum. Mol. Genet. 11:885-891(2002).
RN [5]
RP FUNCTION (SECRETED FORM), INTERACTION WITH SORT1; RAB5A AND RAB7A, AND
RP SUBCELLULAR LOCATION (SECRETED FORM).
RX PubMed=22431521; DOI=10.1128/mcb.06726-11;
RA Mamo A., Jules F., Dumaresq-Doiron K., Costantino S., Lefrancois S.;
RT "The role of ceroid lipofuscinosis neuronal protein 5 (CLN5) in endosomal
RT sorting.";
RL Mol. Cell. Biol. 32:1855-1866(2012).
RN [6]
RP VARIANT CLN5 HIS-63.
RX PubMed=15728307; DOI=10.1212/01.wnl.0000151974.44980.f1;
RA Pineda-Trujillo N., Cornejo W., Carrizosa J., Wheeler R.B., Munera S.,
RA Valencia A., Agudelo-Arango J., Cogollo A., Anderson G., Bedoya G.,
RA Mole S.E., Ruiz-Linares A.;
RT "A CLN5 mutation causing an atypical neuronal ceroid lipofuscinosis of
RT juvenile onset.";
RL Neurology 64:740-742(2005).
RN [7]
RP VARIANTS CLN5 PRO-63 AND ASN-230.
RX PubMed=16814585; DOI=10.1016/j.ymgme.2006.04.010;
RA Bessa C., Teixeira C.A., Mangas M., Dias A., Sa Miranda M.C., Guimaraes A.,
RA Ferreira J.C., Canas N., Cabral P., Ribeiro M.G.;
RT "Two novel CLN5 mutations in a Portuguese patient with vLINCL: insights
RT into molecular mechanisms of CLN5 deficiency.";
RL Mol. Genet. Metab. 89:245-253(2006).
RN [8]
RP VARIANT CLN5 ASP-209.
RX PubMed=17607606; DOI=10.1055/s-2007-981449;
RA Cannelli N., Nardocci N., Cassandrini D., Morbin M., Aiello C., Bugiani M.,
RA Criscuolo L., Zara F., Striano P., Granata T., Bertini E., Simonati A.,
RA Santorelli F.M.;
RT "Revelation of a novel CLN5 mutation in early juvenile neuronal ceroid
RT lipofuscinosis.";
RL Neuropediatrics 38:46-49(2007).
RN [9]
RP VARIANT CLN5 CYS-330, AND CHARACTERIZATION OF VARIANT CLN5 CYS-330.
RX PubMed=19309691; DOI=10.1002/humu.21010;
RA Lebrun A.-H., Storch S., Rueschendorf F., Schmiedt M.-L., Kyttaelae A.,
RA Mole S.E., Kitzmueller C., Saar K., Mewasingh L.D., Boda V.,
RA Kohlschuetter A., Ullrich K., Braulke T., Schulz A.;
RT "Retention of lysosomal protein CLN5 in the endoplasmic reticulum causes
RT neuronal ceroid lipofuscinosis in Asian sibship.";
RL Hum. Mutat. 30:E651-E661(2009).
RN [10]
RP CHARACTERIZATION OF VARIANTS CLN5 PRO-63; HIS-63 AND ASN-230, PROTEOLYTIC
RP CLEAVAGE, SUBCELLULAR LOCATION (SECRETED FORM), AND GLYCOSYLATION.
RX PubMed=20052765; DOI=10.1002/humu.21195;
RA Schmiedt M.L., Bessa C., Heine C., Ribeiro M.G., Jalanko A., Kyttaelae A.;
RT "The neuronal ceroid lipofuscinosis protein CLN5: new insights into
RT cellular maturation, transport, and consequences of mutations.";
RL Hum. Mutat. 31:356-365(2010).
RN [11]
RP VARIANTS CLN5 HIS-63; TYR-77; SER-143; PRO-149; SER-156; ARG-158; SER-158;
RP ASP-209 AND CYS-325, AND VARIANTS ARG-26 AND LYS-193.
RX PubMed=21990111; DOI=10.1002/humu.21624;
RA Kousi M., Lehesjoki A.E., Mole S.E.;
RT "Update of the mutation spectrum and clinical correlations of over 360
RT mutations in eight genes that underlie the neuronal ceroid
RT lipofuscinoses.";
RL Hum. Mutat. 33:42-63(2012).
RN [12]
RP CHARACTERIZATION OF VARIANT CLN5 ASN-230, SUBCELLULAR LOCATION (MEMBRANE
RP FORM), TOPOLOGY, PROTEOLYTIC CLEAVAGE, AND GLYCOSYLATION.
RX PubMed=24038957; DOI=10.1002/humu.22443;
RA Larkin H., Ribeiro M.G., Lavoie C.;
RT "Topology and membrane anchoring of the lysosomal storage disease-related
RT protein CLN5.";
RL Hum. Mutat. 34:1688-1697(2013).
RN [13]
RP CHARACTERIZATION OF VARIANTS CLN5 SER-143 AND ASN-230, GLYCOSYLATION AT
RP ASN-130; ASN-143; ASN-178; ASN-203; ASN-255; ASN-271; ASN-281 AND ASN-352,
RP MUTAGENESIS OF ASN-130; ASN-143; ASN-178; ASN-203; ASN-255; ASN-271;
RP ASN-281 AND ASN-352, AND SUBCELLULAR LOCATION (SECRETED FORM).
RX PubMed=24058541; DOI=10.1371/journal.pone.0074299;
RA Moharir A., Peck S.H., Budden T., Lee S.Y.;
RT "The role of N-glycosylation in folding, trafficking, and functionality of
RT lysosomal protein CLN5.";
RL PLoS ONE 8:E74299-E74299(2013).
RN [14]
RP CHARACTERIZATION OF VARIANT CLN5 ASN-230, AND PROTEOLYTIC CLEAVAGE AT
RP C-TERMINUS.
RX PubMed=26342652; DOI=10.1016/j.yexcr.2015.08.021;
RA De Silva B., Adams J., Lee S.Y.;
RT "Proteolytic processing of the neuronal ceroid lipofuscinosis related
RT lysosomal protein CLN5.";
RL Exp. Cell Res. 338:45-53(2015).
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 (PubMed:22431521). {ECO:0000269|PubMed:22431521}.
CC -!- SUBUNIT: Interacts with SORT1, RAB5A and RAB7A (PubMed:22431521).
CC Interacts with PPT1, TPP1, CLN3, CLN6, CLN8, ATP5F1A and ATP5F1B (By
CC similarity). {ECO:0000250|UniProtKB:Q3UMW8,
CC ECO:0000269|PubMed:22431521}.
CC -!- INTERACTION:
CC O75503; Q13286: CLN3; NbExp=2; IntAct=EBI-1043514, EBI-3248760;
CC -!- SUBCELLULAR LOCATION: [Ceroid-lipofuscinosis neuronal protein 5,
CC secreted form]: Lysosome {ECO:0000269|PubMed:11971870,
CC ECO:0000269|PubMed:20052765, ECO:0000269|PubMed:22431521,
CC ECO:0000269|PubMed:24038957, ECO:0000269|PubMed:24058541}.
CC -!- SUBCELLULAR LOCATION: [Ceroid-lipofuscinosis neuronal protein 5]:
CC Membrane {ECO:0000269|PubMed:24038957}; Single-pass type II membrane
CC protein {ECO:0000269|PubMed:24038957}. Note=An amphipathic anchor
CC region facilitates its association with the membrane.
CC {ECO:0000269|PubMed:24038957}.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
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:0000269|PubMed:11971870, ECO:0000269|PubMed:20052765,
CC ECO:0000269|PubMed:24038957, ECO:0000269|PubMed:24058541}.
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) (PubMed:24038957, PubMed:20052765).
CC {ECO:0000269|PubMed:20052765, ECO:0000269|PubMed:24038957}.
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 (PubMed:26342652).
CC {ECO:0000269|PubMed:26342652}.
CC -!- DISEASE: Ceroid lipofuscinosis, neuronal, 5 (CLN5) [MIM:256731]: A form
CC of neuronal ceroid lipofuscinosis. Neuronal ceroid lipofuscinoses are
CC progressive neurodegenerative, lysosomal storage diseases characterized
CC by intracellular accumulation of autofluorescent liposomal material,
CC and clinically by seizures, dementia, visual loss, and/or cerebral
CC atrophy. The lipopigment patterns observed most often in neuronal
CC ceroid lipofuscinosis type 5 comprise mixed combinations of granular,
CC curvilinear, and fingerprint profiles. {ECO:0000269|PubMed:15728307,
CC ECO:0000269|PubMed:16814585, ECO:0000269|PubMed:17607606,
CC ECO:0000269|PubMed:19309691, ECO:0000269|PubMed:20052765,
CC ECO:0000269|PubMed:21990111, ECO:0000269|PubMed:24038957,
CC ECO:0000269|PubMed:24058541, ECO:0000269|PubMed:26342652,
CC ECO:0000269|PubMed:9662406}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the CLN5 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC27614.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=NCL CLN5; Note=Neural Ceroid Lipofuscinoses mutation
CC db;
CC URL="https://www.ucl.ac.uk/ncl/cln5.shtml";
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DR EMBL; AF068227; AAC27614.1; ALT_INIT; mRNA.
DR EMBL; AK075109; BAG52069.1; -; mRNA.
DR EMBL; AC001226; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS9456.1; -.
DR RefSeq; NP_006484.1; NM_006493.2.
DR AlphaFoldDB; O75503; -.
DR SMR; O75503; -.
DR BioGRID; 107614; 83.
DR IntAct; O75503; 11.
DR MINT; O75503; -.
DR STRING; 9606.ENSP00000366673; -.
DR GlyConnect; 1108; 17 N-Linked glycans (4 sites).
DR GlyGen; O75503; 8 sites, 16 N-linked glycans (4 sites).
DR iPTMnet; O75503; -.
DR PhosphoSitePlus; O75503; -.
DR BioMuta; CLN5; -.
DR EPD; O75503; -.
DR jPOST; O75503; -.
DR MassIVE; O75503; -.
DR MaxQB; O75503; -.
DR PaxDb; O75503; -.
DR PeptideAtlas; O75503; -.
DR PRIDE; O75503; -.
DR ProteomicsDB; 50054; -.
DR Antibodypedia; 50072; 178 antibodies from 24 providers.
DR DNASU; 1203; -.
DR Ensembl; ENST00000377453.9; ENSP00000366673.5; ENSG00000102805.16.
DR Ensembl; ENST00000636183.2; ENSP00000490181.2; ENSG00000102805.16.
DR GeneID; 1203; -.
DR KEGG; hsa:1203; -.
DR MANE-Select; ENST00000377453.9; ENSP00000366673.5; NM_006493.4; NP_006484.2.
DR UCSC; uc058xoc.1; human.
DR CTD; 1203; -.
DR DisGeNET; 1203; -.
DR GeneCards; CLN5; -.
DR HGNC; HGNC:2076; CLN5.
DR HPA; ENSG00000102805; Low tissue specificity.
DR MalaCards; CLN5; -.
DR MIM; 256731; phenotype.
DR MIM; 608102; gene.
DR neXtProt; NX_O75503; -.
DR OpenTargets; ENSG00000102805; -.
DR Orphanet; 228360; CLN5 disease.
DR PharmGKB; PA26603; -.
DR VEuPathDB; HostDB:ENSG00000102805; -.
DR eggNOG; ENOG502QPQ5; Eukaryota.
DR GeneTree; ENSGT00390000010065; -.
DR HOGENOM; CLU_050387_0_0_1; -.
DR InParanoid; O75503; -.
DR OMA; FRPHQSF; -.
DR OrthoDB; 1227965at2759; -.
DR PhylomeDB; O75503; -.
DR TreeFam; TF330864; -.
DR PathwayCommons; O75503; -.
DR SignaLink; O75503; -.
DR BioGRID-ORCS; 1203; 7 hits in 1070 CRISPR screens.
DR ChiTaRS; CLN5; human.
DR GeneWiki; CLN5; -.
DR GenomeRNAi; 1203; -.
DR Pharos; O75503; Tbio.
DR PRO; PR:O75503; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; O75503; protein.
DR Bgee; ENSG00000102805; Expressed in left lobe of thyroid gland and 188 other tissues.
DR ExpressionAtlas; O75503; baseline and differential.
DR Genevisible; O75503; HS.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA: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; IDA:UniProtKB.
DR GO; GO:0007420; P:brain development; IEP:UniProtKB.
DR GO; GO:0070085; P:glycosylation; IDA:UniProtKB.
DR GO; GO:0007042; P:lysosomal lumen acidification; IMP:UniProtKB.
DR GO; GO:0007040; P:lysosome organization; IBA:GO_Central.
DR GO; GO:0022008; P:neurogenesis; IEP:UniProtKB.
DR GO; GO:0042551; P:neuron maturation; NAS:UniProtKB.
DR GO; GO:1904426; P:positive regulation of GTP binding; IMP:UniProtKB.
DR GO; GO:0030163; P:protein catabolic process; NAS:UniProtKB.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IMP:UniProtKB.
DR GO; GO:0006465; P:signal peptide processing; IDA: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 1: Evidence at protein level;
KW Disease variant; Epilepsy; Glycoprotein; Lysosome; Membrane;
KW Neurodegeneration; Neuronal ceroid lipofuscinosis; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..358
FT /note="Ceroid-lipofuscinosis neuronal protein 5"
FT /id="PRO_0000089860"
FT CHAIN ?..358
FT /note="Ceroid-lipofuscinosis neuronal protein 5, secreted
FT form"
FT /id="PRO_0000438009"
FT TOPO_DOM 1..23
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:24038957"
FT TRANSMEM 24..41
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 42..358
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:24038957"
FT REGION 304..343
FT /note="Membrane-anchoring"
FT /evidence="ECO:0000269|PubMed:24038957"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:24058541"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:24058541"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:24058541"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:24058541"
FT CARBOHYD 255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:24058541"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:24058541"
FT CARBOHYD 281
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:24058541"
FT CARBOHYD 352
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:24058541"
FT VARIANT 26
FT /note="W -> R (in dbSNP:rs199727787)"
FT /evidence="ECO:0000269|PubMed:21990111"
FT /id="VAR_066895"
FT VARIANT 63
FT /note="R -> H (in CLN5; retained in the endoplasmic
FT reticulum rather than reaching the lysosome;
FT dbSNP:rs104894386)"
FT /evidence="ECO:0000269|PubMed:15728307,
FT ECO:0000269|PubMed:20052765, ECO:0000269|PubMed:21990111"
FT /id="VAR_042700"
FT VARIANT 63
FT /note="R -> P (in CLN5; Retained in the endoplasmic
FT reticulum rather than reaching the lysosome;
FT dbSNP:rs104894386)"
FT /evidence="ECO:0000269|PubMed:16814585,
FT ECO:0000269|PubMed:20052765"
FT /id="VAR_042702"
FT VARIANT 77
FT /note="C -> Y (in CLN5; dbSNP:rs267606738)"
FT /evidence="ECO:0000269|PubMed:21990111"
FT /id="VAR_066896"
FT VARIANT 143
FT /note="N -> S (in CLN5; loss of glycosylation; effectively
FT transported to the lysosome; dbSNP:rs386833975)"
FT /evidence="ECO:0000269|PubMed:21990111,
FT ECO:0000269|PubMed:24058541"
FT /id="VAR_066897"
FT VARIANT 149
FT /note="L -> P (in CLN5; dbSNP:rs386833976)"
FT /evidence="ECO:0000269|PubMed:21990111"
FT /id="VAR_066898"
FT VARIANT 156
FT /note="P -> S (in CLN5; dbSNP:rs386833977)"
FT /evidence="ECO:0000269|PubMed:21990111"
FT /id="VAR_066899"
FT VARIANT 158
FT /note="W -> R (in CLN5; dbSNP:rs147065248)"
FT /evidence="ECO:0000269|PubMed:21990111"
FT /id="VAR_066900"
FT VARIANT 158
FT /note="W -> S (in CLN5; dbSNP:rs386833978)"
FT /evidence="ECO:0000269|PubMed:21990111"
FT /id="VAR_066901"
FT VARIANT 193
FT /note="N -> K (in dbSNP:rs138611001)"
FT /evidence="ECO:0000269|PubMed:21990111"
FT /id="VAR_066902"
FT VARIANT 209
FT /note="Y -> D (in CLN5; dbSNP:rs386833981)"
FT /evidence="ECO:0000269|PubMed:17607606,
FT ECO:0000269|PubMed:21990111"
FT /id="VAR_042701"
FT VARIANT 219
FT /note="E -> A (in dbSNP:rs11842935)"
FT /id="VAR_059031"
FT VARIANT 230
FT /note="D -> N (in CLN5; creates a new N-glycosylation site;
FT retained in the endoplasmic reticulum rather than reaching
FT the lysosome; dbSNP:rs28940280)"
FT /evidence="ECO:0000269|PubMed:16814585,
FT ECO:0000269|PubMed:20052765, ECO:0000269|PubMed:24038957,
FT ECO:0000269|PubMed:24058541, ECO:0000269|PubMed:26342652,
FT ECO:0000269|PubMed:9662406"
FT /id="VAR_005137"
FT VARIANT 319
FT /note="K -> R (in dbSNP:rs1800209)"
FT /evidence="ECO:0000269|PubMed:9662406"
FT /id="VAR_005138"
FT VARIANT 325
FT /note="Y -> C (in CLN5; dbSNP:rs148862100)"
FT /evidence="ECO:0000269|PubMed:21990111"
FT /id="VAR_066903"
FT VARIANT 330
FT /note="W -> C (in CLN5; retained in the endoplasmic
FT reticulum rather than reaching the lysosome;
FT dbSNP:rs386833968)"
FT /evidence="ECO:0000269|PubMed:19309691"
FT /id="VAR_059032"
FT MUTAGEN 130
FT /note="N->Q: Loss of glycosylation. Retained in the
FT endoplasmic reticulum rather than reaching the lysosome."
FT /evidence="ECO:0000269|PubMed:24058541"
FT MUTAGEN 143
FT /note="N->Q: Loss of glycosylation. Effectively transported
FT to the lysosome."
FT /evidence="ECO:0000269|PubMed:24058541"
FT MUTAGEN 178
FT /note="N->Q: Loss of glycosylation. Effectively transported
FT to the lysosome."
FT /evidence="ECO:0000269|PubMed:24058541"
FT MUTAGEN 203
FT /note="N->Q: Loss of glycosylation. Retained in the
FT endoplasmic reticulum rather than reaching the lysosome."
FT /evidence="ECO:0000269|PubMed:24058541"
FT MUTAGEN 255
FT /note="N->Q: Loss of glycosylation. Retained in the
FT endoplasmic reticulum rather than reaching the lysosome."
FT /evidence="ECO:0000269|PubMed:24058541"
FT MUTAGEN 271
FT /note="N->Q: Loss of glycosylation. Retained in the
FT endoplasmic reticulum rather than reaching the lysosome."
FT /evidence="ECO:0000269|PubMed:24058541"
FT MUTAGEN 281
FT /note="N->Q: Loss of glycosylation. Partially retained in
FT the endoplasmic reticulum."
FT /evidence="ECO:0000269|PubMed:24058541"
FT MUTAGEN 352
FT /note="N->Q: Loss of glycosylation. Retained in the Golgi
FT apparatus rather than reaching the lysosome."
FT /evidence="ECO:0000269|PubMed:24058541"
FT CONFLICT 57
FT /note="Y -> C (in Ref. 2; BAG52069)"
FT /evidence="ECO:0000305"
FT CONFLICT 92
FT /note="I -> T (in Ref. 2; BAG52069)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 358 AA; 41497 MW; 07E49D4913685190 CRC64;
MAQEVDTAQG AEMRRGAGAA RGRASWCWAL ALLWLAVVPG WSRVSGIPSR RHWPVPYKRF
DFRPKPDPYC QAKYTFCPTG SPIPVMEGDD DIEVFRLQAP VWEFKYGDLL GHLKIMHDAI
GFRSTLTGKN YTMEWYELFQ LGNCTFPHLR PEMDAPFWCN QGAACFFEGI DDVHWKENGT
LVQVATISGN MFNQMAKWVK QDNETGIYYE TWNVKASPEK GAETWFDSYD CSKFVLRTFN
KLAEFGAEFK NIETNYTRIF LYSGEPTYLG NETSVFGPTG NKTLGLAIKR FYYPFKPHLP
TKEFLLSLLQ IFDAVIVHKQ FYLFYNFEYW FLPMKFPFIK ITYEEIPLPI RNKTLSGL
