CLN3_DICDI
ID CLN3_DICDI Reviewed; 421 AA.
AC Q54F25;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Battenin;
DE AltName: Full=Protein CLN3 homolog;
GN Name=cln3; ORFNames=DDB_G0291157;
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: Lysosome membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the battenin family. {ECO:0000305}.
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DR EMBL; AAFI02000175; EAL61862.1; -; Genomic_DNA.
DR RefSeq; XP_635365.1; XM_630273.1.
DR AlphaFoldDB; Q54F25; -.
DR SMR; Q54F25; -.
DR STRING; 44689.DDB0233983; -.
DR PaxDb; Q54F25; -.
DR EnsemblProtists; EAL61862; EAL61862; DDB_G0291157.
DR GeneID; 8628013; -.
DR KEGG; ddi:DDB_G0291157; -.
DR dictyBase; DDB_G0291157; cln3.
DR eggNOG; KOG3880; Eukaryota.
DR HOGENOM; CLU_029663_1_2_1; -.
DR InParanoid; Q54F25; -.
DR OMA; WLCNWQV; -.
DR PhylomeDB; Q54F25; -.
DR PRO; PR:Q54F25; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0000331; C:contractile vacuole; IDA:dictyBase.
DR GO; GO:0030139; C:endocytic vesicle; IDA:dictyBase.
DR GO; GO:0005794; C:Golgi apparatus; IDA:dictyBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005773; C:vacuole; IBA:GO_Central.
DR GO; GO:0031152; P:aggregation involved in sorocarp development; IMP:dictyBase.
DR GO; GO:0098609; P:cell-cell adhesion; IMP:dictyBase.
DR GO; GO:0031589; P:cell-substrate adhesion; IMP:dictyBase.
DR GO; GO:0009992; P:cellular water homeostasis; IMP:dictyBase.
DR GO; GO:0006972; P:hyperosmotic response; IMP:dictyBase.
DR GO; GO:0006971; P:hypotonic response; IMP:dictyBase.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:dictyBase.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:dictyBase.
DR GO; GO:0050709; P:negative regulation of protein secretion; IMP:dictyBase.
DR GO; GO:0006907; P:pinocytosis; IMP:dictyBase.
DR GO; GO:0050714; P:positive regulation of protein secretion; IMP:dictyBase.
DR GO; GO:0051453; P:regulation of intracellular pH; IBA:GO_Central.
DR GO; GO:0050708; P:regulation of protein secretion; IMP:dictyBase.
DR GO; GO:0031156; P:regulation of sorocarp development; IMP:dictyBase.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR003492; Battenin_disease_Cln3.
DR InterPro; IPR036259; MFS_trans_sf.
DR PANTHER; PTHR10981; PTHR10981; 1.
DR Pfam; PF02487; CLN3; 1.
DR PRINTS; PR01315; BATTENIN.
DR SUPFAM; SSF103473; SSF103473; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Lysosome; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..421
FT /note="Battenin"
FT /id="PRO_0000328031"
FT TRANSMEM 13..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 74..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 248..268
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 284..304
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 313..333
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 338..358
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 382..402
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 190..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 199
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 421 AA; 46557 MW; 710D6AF8FFB00605 CRC64;
MGKDYTFIRN WISFHFMGNI NNFSYCVVNA ASGNLSAYFH NSKNIGIILW ANIAFGLVSR
LVNTFLIENV NSKLKIVVNC LFMSIGLIGV ALSVYVNFGF CIAAIAFVGI ASSFGESVIL
SYMKKFPAEL VNGWSSGTGI AGVCGSLFYI AMVAAGLSNS TIFYMMLPTV AVYFLLFFFG
LKVPNHLEED RTDNHNNSNN SSNNSKYTEK QSLVKKDQLI EDIDDGGGAE VAPPGETKKQ
RYIRCARLVW FNAVNLALVY FFEYVASVGG ADLALKKDPN NDNFFIANAF AIFSFCYQLG
VLISRSSLQF VKIKHIGVIT ILQGINMVFW IIQAKYKMVT SVWVLFILMV YCGLLGGASY
VNVFYLILHQ KNIPNEDREL CINYAALLVT VGITLAACFI LVMDHTFLAS EVPKTDSSSS
T
