ID   CLN5C_DICDI             Reviewed;         439 AA.
AC   Q54C37;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 59.
DE   RecName: Full=Cln5-like protein 3;
DE   Flags: Precursor;
GN   Name=cln5lc; ORFNames=DDB_G0293236;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the CLN5 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AAFI02000200; EAL60817.1; -; Genomic_DNA.
DR   RefSeq; XP_629229.1; XM_629227.1.
DR   AlphaFoldDB; Q54C37; -.
DR   PaxDb; Q54C37; -.
DR   EnsemblProtists; EAL60817; EAL60817; DDB_G0293236.
DR   GeneID; 8629111; -.
DR   KEGG; ddi:DDB_G0293236; -.
DR   dictyBase; DDB_G0293236; -.
DR   eggNOG; ENOG502RHN2; Eukaryota.
DR   HOGENOM; CLU_062132_0_0_1; -.
DR   InParanoid; Q54C37; -.
DR   PhylomeDB; Q54C37; -.
DR   PRO; PR:Q54C37; -.
DR   Proteomes; UP000002195; Chromosome 6.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005765; C:lysosomal membrane; IBA:GO_Central.
DR   GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IBA:GO_Central.
DR   GO; GO:0007040; P:lysosome organization; IBA:GO_Central.
DR   InterPro; IPR026138; CLN5.
DR   PANTHER; PTHR15380; PTHR15380; 1.
DR   Pfam; PF15014; CLN5; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Membrane; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..439
FT                   /note="Cln5-like protein 3"
FT                   /id="PRO_0000330476"
FT   TRANSMEM        371..391
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        93
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        112
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        122
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        138
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        168
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        219
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        268
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        289
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        304
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        359
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   439 AA;  49298 MW;  EF3A8B372661CEAD CRC64;
     MKNMLNIILT LTIIFIGLIK ISISSDSGSS ENGIYFYTYD TICEFTNSIR DDDQYELYYV
     QAPLMYAIYG DLFEKINAYH SGVGFYNLNG GPNISIDYFA GPTLEDALIP QNITKDSQGN
     YNLTWNTYGL IEVTNYINET YWSKRELIMY GLTGLQVKQY LSWAPIYNQT HPVYNLFSIA
     SADASGSGDN GYLETILHNL GIGGGGGGSG SENLIVYQNS STCDDFVWAS FNTIYQLGGT
     LVGMQSNPPK DQITLFTTDE PTIVDYNNIT QRNQLASFYI NLMGIANKNE SALQIFQELI
     SLFNGTFYCY IDGVYYELHL SKPTPISFTY QPSPMPTGQR NSNSIETLNN CYSKSSTDNQ
     SFFNRFSKIQ IIFISIAIGF GVVIILYISI GIMVNKSRGK SGTNLIPNKK LWTSIGSKFK
     RDNNKNNYKP LLYNENTIQ