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DCXH_TOXGV
ID   DCXH_TOXGV              Reviewed;         256 AA.
AC   B6KAS6; A0A0F7UX87; B9QC02; S7WFE6; S8F0J1;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Doublecortin domain-containing protein {ECO:0000303|PubMed:27932494};
DE            Short=TgDCX {ECO:0000303|PubMed:27932494};
GN   Name=DCX {ECO:0000303|PubMed:27932494};
GN   ORFNames=BN1205_078130 {ECO:0000312|EMBL:CEL74611.1},
GN   TGVEG_256030 {ECO:0000312|EMBL:ESS35450.1};
OS   Toxoplasma gondii (strain ATCC 50861 / VEG).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Sarcocystidae; Toxoplasma.
OX   NCBI_TaxID=432359 {ECO:0000312|Proteomes:UP000002226};
RN   [1] {ECO:0000312|EMBL:ESS35450.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 50861 / VEG {ECO:0000312|EMBL:ESS35450.1};
RA   Gandolfi B., Grahn R.A.;
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000312|Proteomes:UP000002226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 50861 / VEG {ECO:0000312|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.
RN   [3] {ECO:0000312|EMBL:CEL74611.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 50861 / VEG {ECO:0000312|EMBL:CEL74611.1};
RX   PubMed=25875305; DOI=10.1371/journal.pone.0124473;
RA   Ramaprasad A., Mourier T., Naeem R., Malas T.B., Moussa E., Panigrahi A.,
RA   Vermont S.J., Otto T.D., Wastling J., Pain A.;
RT   "Comprehensive Evaluation of Toxoplasma gondii VEG and Neospora caninum LIV
RT   Genomes with Tachyzoite Stage Transcriptome and Proteome Defines Novel
RT   Transcript Features.";
RL   PLoS ONE 10:e0124473-e0124473(2015).
RN   [4] {ECO:0000305}
RP   FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP   PHENOTYPE.
RC   STRAIN=RH {ECO:0000269|PubMed:27932494};
RX   PubMed=27932494; DOI=10.1091/mbc.e16-08-0587;
RA   Nagayasu E., Hwang Y.C., Liu J., Murray J.M., Hu K.;
RT   "Loss of a doublecortin (DCX)-domain protein causes structural defects in a
RT   tubulin-based organelle of Toxoplasma gondii and impairs host-cell
RT   invasion.";
RL   Mol. Biol. Cell 28:411-428(2017).
RN   [5] {ECO:0007744|PDB:6B4A}
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 148-243, FUNCTION, SUBCELLULAR
RP   LOCATION, DOMAIN, AND DISRUPTION PHENOTYPE.
RX   PubMed=32111164; DOI=10.1186/s12860-020-0249-5;
RA   Leung J.M., Nagayasu E., Hwang Y.C., Liu J., Pierce P.G., Phan I.Q.,
RA   Prentice R.A., Murray J.M., Hu K.;
RT   "A doublecortin-domain protein of Toxoplasma and its orthologues bind to
RT   and modify the structure and organization of tubulin polymers.";
RL   BMC Mol. Cell Biol. 21:8-8(2020).
CC   -!- FUNCTION: Specifically required in the formation and maintenance of the
CC       conoid fibers; the conoid is a component of the cytoskeletal apical
CC       complex, which is composed of a left-handed spiral of 14 fibers made
CC       from a nontubular tubulin polymer (PubMed:27932494). Promotes the
CC       organization, curvature, and stability of the conoid fibers, and
CC       probably bridges other conoid components to the tubulin core
CC       (PubMed:27932494, PubMed:32111164). {ECO:0000269|PubMed:27932494,
CC       ECO:0000269|PubMed:32111164}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000269|PubMed:27932494, ECO:0000269|PubMed:32111164}.
CC       Note=Localizes along the tubulin-containing conoid fibers; the conoid
CC       is a component of the cytoskeletal apical complex, which is composed of
CC       a left-handed spiral of 14 fibers made from a nontubular tubulin
CC       polymer (PubMed:27932494, PubMed:32111164). During early daughter
CC       development, localizes to the center of a five-petaled flower-like
CC       tubulin structure in the nascent daughter apical cytoskeleton
CC       (PubMed:27932494). {ECO:0000269|PubMed:27932494,
CC       ECO:0000269|PubMed:32111164}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in tachyzoites (at protein level).
CC       {ECO:0000269|PubMed:27932494}.
CC   -!- DOMAIN: The doublecortin is involved in the binding to microtubules;
CC       however, it is not sufficient by itself and requires the partial
CC       p25alpha domain. {ECO:0000269|PubMed:32111164}.
CC   -!- DOMAIN: The partial p25 alpha domain binds to microtubules.
CC       {ECO:0000269|PubMed:32111164}.
CC   -!- DISRUPTION PHENOTYPE: Reduced tachyzoite growth and host invasion
CC       (PubMed:27932494). Loss of tubulin at the apical complex
CC       (PubMed:27932494). Abnormal conoid morphology characterized by a
CC       shorter and less rectangular structure a weaker or absent basket-weave
CC       stripe pattern (PubMed:27932494). Cortical microtubules, the mitotic
CC       spindle, spindle pole, and centrioles are normal (PubMed:27932494).
CC       {ECO:0000269|PubMed:27932494}.
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DR   EMBL; LN714497; CEL74611.1; -; Genomic_DNA.
DR   EMBL; AAYL02000031; ESS35450.1; -; Genomic_DNA.
DR   PDB; 6B4A; X-ray; 2.00 A; A/B=148-243.
DR   PDBsum; 6B4A; -.
DR   SMR; B6KAS6; -.
DR   EnsemblProtists; ESS35450; ESS35450; TGVEG_256030.
DR   VEuPathDB; ToxoDB:TGVEG_256030; -.
DR   eggNOG; ENOG502S25E; Eukaryota.
DR   InParanoid; B6KAS6; -.
DR   OMA; FRNGDEH; -.
DR   Proteomes; UP000002226; Partially assembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   Gene3D; 3.10.20.230; -; 1.
DR   InterPro; IPR003533; Doublecortin_dom.
DR   InterPro; IPR036572; Doublecortin_dom_sf.
DR   InterPro; IPR008907; P25-alpha.
DR   Pfam; PF03607; DCX; 1.
DR   Pfam; PF05517; p25-alpha; 1.
DR   SMART; SM00537; DCX; 1.
DR   SUPFAM; SSF89837; SSF89837; 1.
DR   PROSITE; PS50309; DC; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Cytoskeleton; Reference proteome.
FT   CHAIN           1..256
FT                   /note="Doublecortin domain-containing protein"
FT                   /id="PRO_0000455112"
FT   DOMAIN          152..226
FT                   /note="Doublecortin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00072"
FT   REGION          71..103
FT                   /note="Partial p25alpha domain"
FT                   /evidence="ECO:0000269|PubMed:32111164"
FT   STRAND          152..158
FT                   /evidence="ECO:0007829|PDB:6B4A"
FT   STRAND          167..171
FT                   /evidence="ECO:0007829|PDB:6B4A"
FT   HELIX           178..189
FT                   /evidence="ECO:0007829|PDB:6B4A"
FT   STRAND          198..200
FT                   /evidence="ECO:0007829|PDB:6B4A"
FT   HELIX           210..212
FT                   /evidence="ECO:0007829|PDB:6B4A"
FT   STRAND          217..225
FT                   /evidence="ECO:0007829|PDB:6B4A"
FT   HELIX           230..232
FT                   /evidence="ECO:0007829|PDB:6B4A"
FT   HELIX           234..237
FT                   /evidence="ECO:0007829|PDB:6B4A"
SQ   SEQUENCE   256 AA;  29222 MW;  0B23EFD0D82115C7 CRC64;
     MACGIPWKLA RRDELMATRQ AERPGEYFPP PYPPCPPTVV TPLRTSAYDF PEATFVTRPC
     LPAKKATGHK NVFERLTDTA YYTGSHRERF DEFGNGRGIA GREYLYAYDG LTESPSRCHE
     VYSSVIKRPR KPVVTPGTLG IQRFGVQIPA PRLMWLYRNG DKHDDGTPFF VRPYIKSMES
     LYQQITKEIT PIAGPVRRIF DQNFRVITDL DDIVDGAKYL CTSGEPPAAY DRLEKFLSEW
     VIQKSQTKVP SQFFVV
 
 
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