ID   CADF1_PLAFX             Reviewed;         122 AA.
AC   P86292;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   25-MAY-2022, entry version 41.
DE   RecName: Full=Cofilin/actin-depolymerizing factor homolog 1 {ECO:0000303|PubMed:15975905};
DE            Short=PfADF1 {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   FUNCTION, INTERACTION WITH ACTIN, AND 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. {ECO:0000269|PubMed:15975905}.
CC   -!- SUBUNIT: Interacts with monomeric actin, does not bind to actin
CC       polymers. {ECO:0000269|PubMed:15975905}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q03048}.
CC       Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q03048}.
CC   -!- DEVELOPMENTAL STAGE: Expressed throughout the life cycle, in oocyst
CC       sporozoites that invade the mosquito salivary glands, salivary gland
CC       sporozoites infectious to the mammalian liver, and schizonts/merozoites
CC       that invade erythrocytes. {ECO:0000269|PubMed:15975905}.
CC   -!- SIMILARITY: Belongs to the actin-binding proteins ADF family.
CC       {ECO:0000255}.
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DR   EMBL; AANS01000859; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PDB; 3Q2B; X-ray; 1.60 A; A=1-122.
DR   PDBsum; 3Q2B; -.
DR   AlphaFoldDB; P86292; -.
DR   SMR; P86292; -.
DR   VEuPathDB; PlasmoDB:PfHB3_050008600; -.
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; IMP:UniProtKB.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IMP:UniProtKB.
DR   GO; GO:0030042; P:actin filament depolymerization; IEA:InterPro.
DR   GO; GO:0060327; P:cytoplasmic actin-based contraction involved in cell motility; IMP:UniProtKB.
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   1: Evidence at protein level;
KW   3D-structure; Actin-binding; Cytoplasm; Cytoskeleton; Reference proteome.
FT   CHAIN           1..122
FT                   /note="Cofilin/actin-depolymerizing factor homolog 1"
FT                   /id="PRO_0000377705"
FT   DOMAIN          4..122
FT                   /note="ADF-H"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00599"
FT   HELIX           9..21
FT                   /evidence="ECO:0007829|PDB:3Q2B"
FT   STRAND          23..32
FT                   /evidence="ECO:0007829|PDB:3Q2B"
FT   STRAND          35..43
FT                   /evidence="ECO:0007829|PDB:3Q2B"
FT   HELIX           47..56
FT                   /evidence="ECO:0007829|PDB:3Q2B"
FT   STRAND          61..68
FT                   /evidence="ECO:0007829|PDB:3Q2B"
FT   STRAND          73..79
FT                   /evidence="ECO:0007829|PDB:3Q2B"
FT   HELIX           85..99
FT                   /evidence="ECO:0007829|PDB:3Q2B"
FT   STRAND          105..107
FT                   /evidence="ECO:0007829|PDB:3Q2B"
FT   HELIX           115..118
FT                   /evidence="ECO:0007829|PDB:3Q2B"
SQ   SEQUENCE   122 AA;  13741 MW;  F746935229AFDD25 CRC64;
     MISGIRVNDN CVTEFNNMKI RKTCGWIIFV IQNCEIIIHS KGASTTLTEL VQSIDKNNEI
     QCAYVVFDAV SKIHFFMYAR ESSNSRDRMT YASSKQAILK KIEGVNVLTS VIESAQDVAD
     LK