ID   CADF2_PLAFX             Reviewed;         143 AA.
AC   P86293;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   25-MAY-2022, entry version 35.
DE   RecName: Full=Cofilin/actin-depolymerizing factor homolog 2 {ECO:0000303|PubMed:15975905};
DE            Short=PfADF2 {ECO:0000303|PubMed:15975905};
OS   Plasmodium falciparum (isolate HB3).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX   NCBI_TaxID=137071;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   The Broad Institute Genome Sequencing Platform;
RA   Birren B., Lander E., Galagan J., Nusbaum C., Devon K., Henn M., Jaffe D.,
RA   Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M., Mauceli E.,
RA   Brockman W., MacCallum I.A., Rounsley S., Young S., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Kodira C., Zeng Q., Oleary S., Yandava C., Alvarado L., Wirth D.,
RA   Volkman S., Hartl D.;
RT   "The genome sequence of the Plasmodium falciparum HB3.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000305}
RP   DEVELOPMENTAL STAGE.
RX   PubMed=15975905; DOI=10.1091/mbc.e05-02-0086;
RA   Schueler H., Mueller A.-K., Matuschewski K.;
RT   "A Plasmodium actin-depolymerizing factor that binds exclusively to actin
RT   monomers.";
RL   Mol. Biol. Cell 16:4013-4023(2005).
CC   -!- FUNCTION: Not involved in actin polymerisation, instead functions to
CC       stimulate nucleotide exchange on monomeric actin and influence turnover
CC       of the small amount of cytosolic actin microfilaments. Essential for
CC       erythrocytic schizogony (By similarity).
CC       {ECO:0000250|UniProtKB:P86292}.
CC   -!- SUBUNIT: Interacts with monomeric actin, does not bind to actin
CC       polymers. {ECO:0000250|UniProtKB:P86292}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q03048}.
CC       Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q03048}.
CC   -!- DEVELOPMENTAL STAGE: Expressed at very low levels throughout the life
CC       cycle. {ECO:0000269|PubMed:15975905}.
CC   -!- SIMILARITY: Belongs to the actin-binding proteins ADF family.
CC       {ECO:0000255}.
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DR   EMBL; AANS01001005; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; P86293; -.
DR   SMR; P86293; -.
DR   VEuPathDB; PlasmoDB:PfHB3_130067800; -.
DR   Proteomes; UP000054289; Unassembled WGS sequence.
DR   GO; GO:0015629; C:actin cytoskeleton; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003785; F:actin monomer binding; ISS:UniProtKB.
DR   GO; GO:0030036; P:actin cytoskeleton organization; ISS:UniProtKB.
DR   GO; GO:0030042; P:actin filament depolymerization; IEA:InterPro.
DR   GO; GO:0060327; P:cytoplasmic actin-based contraction involved in cell motility; ISS:UniProtKB.
DR   CDD; cd11286; ADF_cofilin_like; 1.
DR   Gene3D; 3.40.20.10; -; 1.
DR   InterPro; IPR002108; ADF-H.
DR   InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR   InterPro; IPR017904; ADF/Cofilin.
DR   PANTHER; PTHR11913; PTHR11913; 1.
DR   Pfam; PF00241; Cofilin_ADF; 1.
DR   SMART; SM00102; ADF; 1.
DR   PROSITE; PS51263; ADF_H; 1.
PE   2: Evidence at transcript level;
KW   Actin-binding; Cytoplasm; Cytoskeleton; Reference proteome.
FT   CHAIN           1..143
FT                   /note="Cofilin/actin-depolymerizing factor homolog 2"
FT                   /id="PRO_0000377707"
FT   DOMAIN          4..141
FT                   /note="ADF-H"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00599"
SQ   SEQUENCE   143 AA;  16998 MW;  E969FB02D105201C CRC64;
     MVSGVKVSDE CVYEFNKLKI KHIHKYIIYR IENYEEVIVD FLEQDNSLKS YKDIIIDIRN
     NLKTTECRYI IADMPIPTPE GVLRNRIYFI FWSPDLAKSK EKMLYASSKE YLVRKINGIF
     KSLEITCDLE DFEDELRTII LNT