CLN5_MOUSE
ID CLN5_MOUSE Reviewed; 341 AA.
AC Q3UMW8; Q8C054; Q8R152;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Ceroid-lipofuscinosis neuronal protein 5 homolog;
DE Short=Protein CLN5;
DE Contains:
DE RecName: Full=Ceroid-lipofuscinosis neuronal protein 5 homolog, secreted form;
GN Name=Cln5;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Lung, and Olfactory bulb;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6-341.
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP INTERACTION WITH PPT1; TPP1; CLN3; CLN6; CLN8; ATP5F1A AND ATP5F1B.
RX PubMed=19941651; DOI=10.1186/1471-2121-10-83;
RA Lyly A., von Schantz C., Heine C., Schmiedt M.L., Sipilae T., Jalanko A.,
RA Kyttaelae A.;
RT "Novel interactions of CLN5 support molecular networking between neuronal
RT ceroid lipofuscinosis proteins.";
RL BMC Cell Biol. 10:83-83(2009).
RN [4]
RP SUBCELLULAR LOCATION (SECRETED FORM).
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 [5]
RP PROTEOLYTIC CLEAVAGE AT C-TERMINUS, AND TISSUE SPECIFICITY.
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. {ECO:0000250|UniProtKB:O75503}.
CC -!- SUBUNIT: Interacts with PPT1, TPP1, CLN3, CLN6, CLN8, ATP5F1A and
CC ATP5F1B (PubMed:19941651). Interacts with SORT1, RAB5A and RAB7A (By
CC similarity). {ECO:0000250|UniProtKB:O75503,
CC ECO:0000269|PubMed:19941651}.
CC -!- SUBCELLULAR LOCATION: [Ceroid-lipofuscinosis neuronal protein 5
CC homolog, secreted form]: Lysosome {ECO:0000269|PubMed:20052765}.
CC -!- SUBCELLULAR LOCATION: [Ceroid-lipofuscinosis neuronal protein 5
CC homolog]: Membrane {ECO:0000250|UniProtKB:O75503}; Single-pass type II
CC membrane protein {ECO:0000250|UniProtKB:O75503}. Note=An amphipathic
CC anchor region facilitates its association with the membrane.
CC {ECO:0000250|UniProtKB:O75503}.
CC -!- TISSUE SPECIFICITY: Heart, kidney, liver, spleen, muscle and rectum (at
CC protein level). {ECO:0000269|PubMed:26342652}.
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 homolog]: The type II
CC membrane signal anchor is proteolytically cleaved to produce a mature
CC form that is transported to the lysosomes (Ceroid-lipofuscinosis
CC neuronal protein 5 homolog, secreted form).
CC {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 (PubMed:26342652).
CC {ECO:0000269|PubMed:26342652}.
CC -!- SIMILARITY: Belongs to the CLN5 family. {ECO:0000305}.
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DR EMBL; AK032293; BAC27797.1; -; mRNA.
DR EMBL; AK144635; BAE25980.1; -; mRNA.
DR EMBL; BC025487; AAH25487.1; -; mRNA.
DR CCDS; CCDS27314.1; -.
DR RefSeq; NP_001028414.1; NM_001033242.1.
DR AlphaFoldDB; Q3UMW8; -.
DR SMR; Q3UMW8; -.
DR STRING; 10090.ENSMUSP00000022721; -.
DR GlyConnect; 2208; 1 N-Linked glycan (1 site).
DR GlyGen; Q3UMW8; 7 sites, 1 N-linked glycan (1 site).
DR PhosphoSitePlus; Q3UMW8; -.
DR SwissPalm; Q3UMW8; -.
DR EPD; Q3UMW8; -.
DR MaxQB; Q3UMW8; -.
DR PaxDb; Q3UMW8; -.
DR PRIDE; Q3UMW8; -.
DR ProteomicsDB; 281645; -.
DR Ensembl; ENSMUST00000022721; ENSMUSP00000022721; ENSMUSG00000022125.
DR GeneID; 211286; -.
DR KEGG; mmu:211286; -.
DR UCSC; uc007uwg.1; mouse.
DR CTD; 1203; -.
DR MGI; MGI:2442253; Cln5.
DR VEuPathDB; HostDB:ENSMUSG00000022125; -.
DR eggNOG; ENOG502QPQ5; Eukaryota.
DR GeneTree; ENSGT00390000010065; -.
DR HOGENOM; CLU_050387_0_0_1; -.
DR InParanoid; Q3UMW8; -.
DR OMA; FRPHQSF; -.
DR OrthoDB; 1227965at2759; -.
DR PhylomeDB; Q3UMW8; -.
DR TreeFam; TF330864; -.
DR BioGRID-ORCS; 211286; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Cln5; mouse.
DR PRO; PR:Q3UMW8; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q3UMW8; protein.
DR Bgee; ENSMUSG00000022125; Expressed in placenta labyrinth and 251 other tissues.
DR ExpressionAtlas; Q3UMW8; baseline and differential.
DR Genevisible; Q3UMW8; MM.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0005775; C:vacuolar lumen; IDA:MGI.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IBA:GO_Central.
DR GO; GO:0005537; F:mannose binding; ISS:UniProtKB.
DR GO; GO:0007420; P:brain development; ISS:UniProtKB.
DR GO; GO:0070085; P:glycosylation; ISS:UniProtKB.
DR GO; GO:0007042; P:lysosomal lumen acidification; ISS:UniProtKB.
DR GO; GO:0007040; P:lysosome organization; IMP:MGI.
DR GO; GO:0022008; P:neurogenesis; ISS:UniProtKB.
DR GO; GO:1904426; P:positive regulation of GTP binding; ISO:MGI.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISO:MGI.
DR GO; GO:0006465; P:signal peptide processing; ISS:UniProtKB.
DR GO; GO:0007601; P:visual perception; IMP:MGI.
DR InterPro; IPR026138; CLN5.
DR PANTHER; PTHR15380; PTHR15380; 1.
DR Pfam; PF15014; CLN5; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Lysosome; Membrane; Neurodegeneration;
KW Neuronal ceroid lipofuscinosis; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..341
FT /note="Ceroid-lipofuscinosis neuronal protein 5 homolog"
FT /id="PRO_0000330471"
FT CHAIN ?..341
FT /note="Ceroid-lipofuscinosis neuronal protein 5 homolog,
FT secreted form"
FT /id="PRO_0000438010"
FT TOPO_DOM 1..13
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O75503"
FT TRANSMEM 14..30
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 31..341
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:O75503"
FT REGION 287..326
FT /note="Membrane-anchoring"
FT /evidence="ECO:0000250|UniProtKB:O75503"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 238
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 254
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 264
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 6..8
FT /note="PCG -> TRP (in Ref. 2; AAH25487)"
FT /evidence="ECO:0000305"
FT CONFLICT 42
FT /note="R -> H (in Ref. 1; BAC27797)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 341 AA; 39329 MW; 1969A4003CAF0E4D CRC64;
MLRGGPCGAH WRPALALALL GLATILGASP TSGQRWPVPY KRFSFRPKTD PYCQAKYTFC
PTGSPIPVMK DNDVIEVLRL QAPIWEFKYG DLLGHFKLMH DAVGFRSTLT GKNYTIEWYE
LFQLGNCTFP HLRPDKSAPF WCNQGAACFF EGIDDKHWKE NGTLSVVATI SGNTFNKVAE
WVKQDNETGI YYETWTVRAG PGQGAQTWFE SYDCSNFVLR TYKKLAEFGT EFKKIETNYT
KIFLYSGEPI YLGNETSIFG PKGNKTLALA IKKFYGPFRP YLSTKDFLMN FLKIFDTVII
HRQFYLFYNF EYWFLPMKPP FVKITYEETP LPTRHTTFTD L
