DCXH_PLAF7
ID DCXH_PLAF7 Reviewed; 238 AA.
AC C0H4E4;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Doublecortin domain-containing protein {ECO:0000250|UniProtKB:B6KAS6};
DE AltName: Full=PfApicortin {ECO:0000303|PubMed:32493727};
GN Name=DCX {ECO:0000250|UniProtKB:B6KAS6};
GN ORFNames=PF3D7_0517800 {ECO:0000312|EMBL:CAX63966.1};
OS Plasmodium falciparum (isolate 3D7).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=36329 {ECO:0000312|Proteomes:UP000001450};
RN [1] {ECO:0000312|Proteomes:UP000001450}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7 {ECO:0000312|Proteomes:UP000001450};
RX PubMed=12368864; DOI=10.1038/nature01097;
RA Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W.,
RA Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T., James K.D.,
RA Eisen J.A., Rutherford K.M., Salzberg S.L., Craig A., Kyes S., Chan M.-S.,
RA Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S., Pertea M.,
RA Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B., Martin D.M.A.,
RA Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A., McFadden G.I.,
RA Cummings L.M., Subramanian G.M., Mungall C., Venter J.C., Carucci D.J.,
RA Hoffman S.L., Newbold C., Davis R.W., Fraser C.M., Barrell B.G.;
RT "Genome sequence of the human malaria parasite Plasmodium falciparum.";
RL Nature 419:498-511(2002).
RN [2] {ECO:0000312|Proteomes:UP000001450}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7 {ECO:0000312|Proteomes:UP000001450};
RX PubMed=12368867; DOI=10.1038/nature01095;
RA Hall N., Pain A., Berriman M., Churcher C.M., Harris B., Harris D.,
RA Mungall K.L., Bowman S., Atkin R., Baker S., Barron A., Brooks K.,
RA Buckee C.O., Burrows C., Cherevach I., Chillingworth C., Chillingworth T.,
RA Christodoulou Z., Clark L., Clark R., Corton C., Cronin A., Davies R.M.,
RA Davis P., Dear P., Dearden F., Doggett J., Feltwell T., Goble A.,
RA Goodhead I., Gwilliam R., Hamlin N., Hance Z., Harper D., Hauser H.,
RA Hornsby T., Holroyd S., Horrocks P., Humphray S., Jagels K., James K.D.,
RA Johnson D., Kerhornou A., Knights A., Konfortov B., Kyes S., Larke N.,
RA Lawson D., Lennard N., Line A., Maddison M., Mclean J., Mooney P.,
RA Moule S., Murphy L., Oliver K., Ormond D., Price C., Quail M.A.,
RA Rabbinowitsch E., Rajandream M.A., Rutter S., Rutherford K.M., Sanders M.,
RA Simmonds M., Seeger K., Sharp S., Smith R., Squares R., Squares S.,
RA Stevens K., Taylor K., Tivey A., Unwin L., Whitehead S., Woodward J.R.,
RA Sulston J.E., Craig A., Newbold C., Barrell B.G.;
RT "Sequence of Plasmodium falciparum chromosomes 1, 3-9 and 13.";
RL Nature 419:527-531(2002).
RN [3] {ECO:0000305}
RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND BIOTECHNOLOGY.
RX PubMed=32493727; DOI=10.1242/dmm.042820;
RA Chakrabarti M., Garg S., Rajagopal A., Pati S., Singh S.;
RT "Targeted repression of Plasmodium apicortin by host microRNA impairs
RT malaria parasite growth and invasion.";
RL Dis. Model. Mech. 13:0-0(2020).
RN [4] {ECO:0000305}
RP FUNCTION, INTERACTION WITH ALPHA-TUBULIN 1 AND BETA-TUBULIN, SUBCELLULAR
RP LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=33633135; DOI=10.1038/s41598-021-83513-5;
RA Chakrabarti M., Joshi N., Kumari G., Singh P., Shoaib R., Munjal A.,
RA Kumar V., Behl A., Abid M., Garg S., Gupta S., Singh S.;
RT "Interaction of Plasmodium falciparum apicortin with alpha- and beta-
RT tubulin is critical for parasite growth and survival.";
RL Sci. Rep. 11:4688-4688(2021).
CC -!- FUNCTION: Involved in the stabilization of microtubules
CC (PubMed:33633135). Probably by controlling microtubules stabilization,
CC plays a role in invasion, microneme secretion and parasite growth in
CC host erythrocytes (PubMed:32493727). {ECO:0000269|PubMed:32493727,
CC ECO:0000269|PubMed:33633135}.
CC -!- SUBUNIT: Interacts with alpha-tubulin 1 and beta-tubulin; the
CC interaction stabilizes microtubule assembly.
CC {ECO:0000269|PubMed:33633135}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:33633135}.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:33633135}. Note=Localizes
CC to the parasite surface in subpellicular regions in trophozoites and
CC schizonts (PubMed:33633135). In merozoites, localizes to the apical end
CC of the parasite (PubMed:33633135). {ECO:0000269|PubMed:33633135}.
CC -!- DEVELOPMENTAL STAGE: Expressed during the parasite blood stage,
CC including in rings, trophozoites, schizonts and free merozoites (at
CC protein level). {ECO:0000269|PubMed:32493727,
CC ECO:0000269|PubMed:33633135}.
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:0000250|UniProtKB:B6KAS6}.
CC -!- DOMAIN: The partial p25 alpha domain binds to microtubules.
CC {ECO:0000250|UniProtKB:B6KAS6}.
CC -!- BIOTECHNOLOGY: Human microRNA candidate miR-197 and to a lesser extent
CC miR150 causes the down-regulation of apicortin and thus may be a
CC possible candidate for nucleotide-based antimalarial treatment.
CC {ECO:0000269|PubMed:32493727}.
CC -!- MISCELLANEOUS: Tamoxifen used to treat breast cancer blocks the
CC interaction between DCX/apicortin and, alpha-tubulin 1 and beta-tubulin
CC resulting in microtubule destabilization.
CC {ECO:0000269|PubMed:33633135}.
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DR EMBL; AL844504; CAX63966.1; -; Genomic_DNA.
DR RefSeq; XP_002808695.1; XM_002808649.1.
DR AlphaFoldDB; C0H4E4; -.
DR SMR; C0H4E4; -.
DR EnsemblProtists; CAX63966; CAX63966; PF3D7_0517800.
DR GeneID; 812993; -.
DR KEGG; pfa:PF3D7_0517800; -.
DR VEuPathDB; PlasmoDB:PF3D7_0517800; -.
DR HOGENOM; CLU_1167860_0_0_1; -.
DR InParanoid; C0H4E4; -.
DR OMA; FRNGDEH; -.
DR PhylomeDB; C0H4E4; -.
DR Proteomes; UP000001450; Chromosome 5.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0032273; P:positive regulation of protein polymerization; IBA:GO_Central.
DR Gene3D; 3.10.20.230; -; 1.
DR InterPro; IPR003533; Doublecortin_dom.
DR InterPro; IPR036572; Doublecortin_dom_sf.
DR InterPro; IPR011057; Mss4-like_sf.
DR InterPro; IPR008907; P25-alpha.
DR PANTHER; PTHR12932; PTHR12932; 1.
DR SUPFAM; SSF51316; SSF51316; 1.
DR SUPFAM; SSF89837; SSF89837; 1.
DR PROSITE; PS50309; DC; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Cytoskeleton; Reference proteome.
FT CHAIN 1..238
FT /note="Doublecortin domain-containing protein"
FT /id="PRO_0000455113"
FT DOMAIN 151..232
FT /note="Doublecortin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00072"
FT REGION 82..112
FT /note="Partial p25alpha domain"
FT /evidence="ECO:0000250|UniProtKB:B6KAS6"
SQ SEQUENCE 238 AA; 27922 MW; 386BA7A6A365A058 CRC64;
MENFDEVIKE YQKYLEGKEK THKINSCKHP CCEEDNLKSV KNYFKVYHKK YIPSIIQKKK
KERNEHAPPL LKDIQDKRCT NVFERLNDKQ FYTGVQKTKF MELLKNNKNK SSYCYNNIKV
FSTMLKKPCN YVVTPGTLGI QKYGIQTGRP KTIFLFNNEK KYDKGVYFLV KSYIKNIKSL
CYEITKILQP SIGPTRKIYD QNFSLVRNVN DLINGGKYLC TSGDPPAPIR NLSLHFLT
