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}.
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; 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