ID   B9PY74_TOXGV            Unreviewed;       447 AA.
AC   B9PY74; B6KQR3; B9QLC9; S7UIP2; S8FFK0;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   SubName: Full=Clusterin-associated protein 1 {ECO:0000313|EMBL:ESS29279.1};
GN   ORFNames=TGVEG_293850 {ECO:0000313|EMBL:ESS29279.1};
OS   Toxoplasma gondii (strain ATCC 50861 / VEG).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Sarcocystidae; Toxoplasma.
OX   NCBI_TaxID=432359 {ECO:0000313|EMBL:ESS29279.1, ECO:0000313|Proteomes:UP000002226};
RN   [1] {ECO:0000313|Proteomes:UP000002226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 50861 / VEG {ECO:0000313|Proteomes:UP000002226};
RA   Lorenzi H., Inman J., Amedeo P., Brunk B., Roos D., Caler E.;
RT   "Annotation of Toxoplasma gondii VEG.";
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the CLUAP1 family.
CC       {ECO:0000256|ARBA:ARBA00008340}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ESS29279.1}.
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DR   EMBL; AAYL02000309; ESS29279.1; -; Genomic_DNA.
DR   AlphaFoldDB; B9PY74; -.
DR   STRING; 432359.B9PY74; -.
DR   PaxDb; 5811-TGME49_093850; -.
DR   EnsemblProtists; ESS29279; ESS29279; TGVEG_293850.
DR   VEuPathDB; ToxoDB:TGVEG_293850; -.
DR   eggNOG; ENOG502QZQ8; Eukaryota.
DR   OMA; KPAYQSE; -.
DR   Proteomes; UP000002226; Partially assembled WGS sequence.
DR   GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR019366; Clusterin-associated_protein-1.
DR   PANTHER; PTHR21547; CLUSTERIN ASSOCIATED PROTEIN 1; 1.
DR   PANTHER; PTHR21547:SF0; CLUSTERIN-ASSOCIATED PROTEIN 1; 1.
DR   Pfam; PF10234; Cluap1; 1.
PE   3: Inferred from homology;
KW   Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW   Cilium biogenesis/degradation {ECO:0000256|ARBA:ARBA00022794};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002226};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          355..447
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          240..278
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          309..345
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        355..385
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        400..431
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   447 AA;  50256 MW;  99A7969630C727F9 CRC64;
     MASIYHIRHL NGLLMALGFT GSPLSFGLFS SGPRFLSVAD VLRWLALQCT GVKELPKRPL
     ENADDRVAFV EQISELLARH ASFCLDVETI YAAEGAAVKE LIRLARTLLN AVQSAINRPA
     LPATLEKQLQ TISTSTAVEL MPVSRGDCVG HSAGRPDGAC CIDQLAMAAK LQQLNLSRSA
     ASQLVDTAAS LLQAFERHSR PERVILRRRV RDFLLRLGLH LDSGADQELE HIQLQLAEQL
     RRAKADLLDT QHACLDLENE LTQDSDRAQK RLQSLQNLKP AFLEDHKKLM AELQETYDMY
     VACVRNERFL EMEAEKRQAK ARAGLLEQQK VLQNIQQKMK DEAANLLACR FDRGTSDDEE
     EGQKESVNLA RKRRSTRESQ ESKQEETENP FTASGRQLPA ETSRRRRPQR RGNGETTERR
     SSDDVEFSED MQGNGVRKGN QFTVAKR
//