CTNS_CAEBR
ID CTNS_CAEBR Reviewed; 403 AA.
AC A8WN56;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Cystinosin homolog {ECO:0000250|UniProtKB:Q09500};
GN Name=ctns-1; ORFNames=CBG00747;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
CC -!- FUNCTION: Cystine/H(+) symporter that mediates export of cystine, the
CC oxidized dimer of cysteine, from lysosomes (By similarity). May play a
CC role in the degradation of engulfed apoptotic cells (By similarity).
CC {ECO:0000250|UniProtKB:O60931, ECO:0000250|UniProtKB:Q09500}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(out) + L-cystine(out) = H(+)(in) + L-cystine(in);
CC Xref=Rhea:RHEA:66172, ChEBI:CHEBI:15378, ChEBI:CHEBI:35491;
CC Evidence={ECO:0000250|UniProtKB:O60931};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66173;
CC Evidence={ECO:0000250|UniProtKB:O60931};
CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:Q09500};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q09500}. Cytoplasmic
CC vesicle, phagosome {ECO:0000250|UniProtKB:Q09500}. Note=During
CC degradation of apoptotic cells when lysosomes fuse to phagosomes,
CC located to phagosomal surfaces until the cell corpse is fully degraded.
CC {ECO:0000250|UniProtKB:Q09500}.
CC -!- SIMILARITY: Belongs to the cystinosin family. {ECO:0000255}.
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DR EMBL; HE600999; CAP21911.3; -; Genomic_DNA.
DR RefSeq; XP_002630311.1; XM_002630265.1.
DR AlphaFoldDB; A8WN56; -.
DR STRING; 6238.CBG00747; -.
DR EnsemblMetazoa; CBG00747a.1; CBG00747a.1; WBGene00024090.
DR GeneID; 8571826; -.
DR KEGG; cbr:CBG_00747; -.
DR CTD; 8571826; -.
DR WormBase; CBG00747a; CBP05802; WBGene00024090; Cbr-ctns-1.
DR eggNOG; KOG3145; Eukaryota.
DR HOGENOM; CLU_046327_1_0_1; -.
DR InParanoid; A8WN56; -.
DR OMA; WSAFYAN; -.
DR OrthoDB; 1138417at2759; -.
DR Proteomes; UP000008549; Chromosome II.
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:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0045335; C:phagocytic vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0005774; C:vacuolar membrane; IBA:GO_Central.
DR GO; GO:0015184; F:L-cystine transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0015811; P:L-cystine transport; IBA:GO_Central.
DR GO; GO:0007040; P:lysosome organization; IEA:EnsemblMetazoa.
DR GO; GO:0006909; P:phagocytosis; ISS:UniProtKB.
DR InterPro; IPR005282; LC_transporter.
DR InterPro; IPR006603; PQ-loop_rpt.
DR PANTHER; PTHR13131; PTHR13131; 1.
DR Pfam; PF04193; PQ-loop; 2.
DR SMART; SM00679; CTNS; 2.
DR TIGRFAMs; TIGR00951; 2A43; 1.
PE 3: Inferred from homology;
KW Cytoplasmic vesicle; Glycoprotein; Lysosome; Membrane; Reference proteome;
KW Repeat; Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..403
FT /note="Cystinosin homolog"
FT /id="PRO_0000355035"
FT TOPO_DOM 1..122
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 144..162
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 184..206
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 228..237
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 259..260
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 261..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 284..294
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 295..315
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 316..336
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 337..357
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 358..403
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 124..190
FT /note="PQ-loop 1"
FT /evidence="ECO:0000255"
FT DOMAIN 266..326
FT /note="PQ-loop 2"
FT /evidence="ECO:0000255"
FT REGION 374..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..391
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 403 AA; 45401 MW; E40FA3BFFB916796 CRC64;
MKLPVSILFF ISVSQILAFN NVIVTQKEVE IGVGETASIT FQIKNHTSST LNQTRIQLSQ
SPYITNPDVV LVDNWWANVT VSGERPVAGE ILEALNCTTD GEEVCSLDLL DAYSRITVIR
SHWLAILIQI VGWTYFAAWS VSFYPQMYLN FKRKSVVGLN FDFLSLNLVG FGAYAMFNLL
MYYNSHVKNI YSMENPRSPP PVLLNDVVFA VHAFLACFVT ILQCIFYERD QQRISTKCII
LIIGLVSFGF VSVVVTVLNK ITILDFVVSL SYIKMAVTCC KYFPQAYFNY QRKSTVGWSI
GNILLDFTGG SLDILQMVLQ AINVNDWSAF YANPVKFGLG FVSIFFDIIF MIQHYALYPD
AEVPHNEYHG VDNPDPDSIV RDAEHGAADN ESMESTDPII VHD
