ID   PROF_PLABE              Reviewed;         174 AA.
AC   B8QYR5;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 31.
DE   RecName: Full=Profilin {ECO:0000312|EMBL:ACI15365.1};
OS   Plasmodium berghei.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Vinckeia).
OX   NCBI_TaxID=5821;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:ACI15365.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DEVELOPMENTAL STAGE.
RC   STRAIN=ANKA {ECO:0000312|EMBL:ACI15365.1};
RX   PubMed=19000816; DOI=10.1016/j.str.2008.09.008;
RA   Kursula I., Kursula P., Ganter M., Panjikar S., Matuschewski K.,
RA   Schueler H.;
RT   "Structural basis for parasite-specific functions of the divergent profilin
RT   of Plasmodium falciparum.";
RL   Structure 16:1638-1648(2008).
CC   -!- FUNCTION: Essential for the invasive blood stages of the parasite.
CC       Binds to proline rich sequences in various regulatory formin-like
CC       proteins and also to membrane phospholipids. Binds to actin and affects
CC       the structure of the cytoskeleton. Weakly sequesters actin monomers (By
CC       similarity). {ECO:0000250|UniProtKB:P86294}.
CC   -!- SUBUNIT: Binds actin. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:P07274}.
CC   -!- DEVELOPMENTAL STAGE: Expressed throughout the life cycle: 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:19000816}.
CC   -!- DOMAIN: The actin binding residues are poorly conserved between
CC       Plasmodium and other organisms. The Plasmodium-specific profilin mini-
CC       domain may have a role in binding to membrane phospholipids.
CC   -!- SIMILARITY: Belongs to the profilin family. {ECO:0000255}.
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DR   EMBL; EU735101; ACI15365.1; -; Genomic_DNA.
DR   AlphaFoldDB; B8QYR5; -.
DR   SMR; B8QYR5; -.
DR   VEuPathDB; PlasmoDB:PBANKA_0833000; -.
DR   OMA; DITMCAR; -.
DR   GO; GO:0015629; C:actin cytoskeleton; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0003785; F:actin monomer binding; ISS:UniProtKB.
DR   GO; GO:0005543; F:phospholipid binding; ISS:UniProtKB.
DR   GO; GO:0030036; P:actin cytoskeleton organization; ISS:UniProtKB.
DR   GO; GO:0060327; P:cytoplasmic actin-based contraction involved in cell motility; ISS:UniProtKB.
DR   InterPro; IPR005455; PFN.
DR   InterPro; IPR036140; PFN_sf.
DR   InterPro; IPR016814; Profilin_apicomplexa.
DR   PANTHER; PTHR11604; PTHR11604; 1.
DR   Pfam; PF00235; Profilin; 1.
DR   PIRSF; PIRSF022993; Profilin_apicomplexa; 1.
DR   SUPFAM; SSF55770; SSF55770; 1.
PE   2: Evidence at transcript level;
KW   Actin-binding; Cytoplasm; Cytoskeleton; Lipid-binding.
FT   CHAIN           1..174
FT                   /note="Profilin"
FT                   /id="PRO_0000377709"
FT   REGION          4..9
FT                   /note="Pro-rich sequence-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P86294"
FT   REGION          99..111
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P86294, ECO:0000255"
FT   REGION          151..155
FT                   /note="Actin-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P86294, ECO:0000255"
FT   MOTIF           47..53
FT                   /note="Plasmodium-specific profilin mini-domain"
FT                   /evidence="ECO:0000250|UniProtKB:P86294"
FT   SITE            34
FT                   /note="Interaction with Pro-rich sequence"
FT                   /evidence="ECO:0000250"
FT   SITE            88
FT                   /note="Interaction with actin"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   174 AA;  19266 MW;  38D8D92145DE683C CRC64;
     MEEYSWENFL NDKLLATNQV SAAGLASEED GVVYECVATP DENNPDFDKW SLFYKEDYDI
     EIEDENGSKT TKTITEGQSI LTMFNEGYAS DGIWLGGTKY QFINMDKGLE YEGHSFDVAT
     CAKSKGGMHI IKVGGGHILI VLYDEEKEQD RGNSKNAALA FSKELIESTD TGAA