PROF_PLAFX
ID PROF_PLAFX Reviewed; 171 AA.
AC P86294; A0A0L7KBZ5;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-MAY-2022, sequence version 2.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=Profilin {ECO:0000303|PubMed:19000816};
DE Short=PfPfn {ECO:0000303|PubMed:19000816};
GN ORFNames=PFHG_02206;
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 X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) IN COMPLEX WITH OCTAPROLINE PEPTIDE,
RP FUNCTION, ACTIN-BINDING, AND PHOSPHOLIPID-BINDING.
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.
CC {ECO:0000269|PubMed:19000816}.
CC -!- SUBUNIT: Binds actin. {ECO:0000269|PubMed:19000816}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P07274}.
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}.
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; CH671963; KOB60444.1; -; Genomic_DNA.
DR PDB; 2JKF; X-ray; 2.31 A; A=1-170.
DR PDB; 2JKG; X-ray; 1.89 A; A=1-170.
DR PDB; 4D60; X-ray; 3.30 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=1-170.
DR PDBsum; 2JKF; -.
DR PDBsum; 2JKG; -.
DR PDBsum; 4D60; -.
DR AlphaFoldDB; P86294; -.
DR SMR; P86294; -.
DR PRIDE; P86294; -.
DR EnsemblProtists; KOB60444; KOB60444; PFHG_02206.
DR VEuPathDB; PlasmoDB:PfHB3_090037100; -.
DR EvolutionaryTrace; P86294; -.
DR Proteomes; UP000054289; Unassembled WGS sequence.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; IPI:UniProtKB.
DR GO; GO:0003785; F:actin monomer binding; IMP:UniProtKB.
DR GO; GO:0005543; F:phospholipid binding; IMP:UniProtKB.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0060327; P:cytoplasmic actin-based contraction involved in cell motility; IMP: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 SMART; SM00392; PROF; 1.
DR SUPFAM; SSF55770; SSF55770; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Cytoplasm; Cytoskeleton; Lipid-binding;
KW Reference proteome.
FT CHAIN 1..171
FT /note="Profilin"
FT /id="PRO_0000377710"
FT REGION 5..10
FT /note="Pro-rich sequence-binding"
FT /evidence="ECO:0000269|PubMed:19000816"
FT REGION 100..112
FT /note="Actin-binding"
FT /evidence="ECO:0000255, ECO:0000303|PubMed:19000816"
FT REGION 152..156
FT /note="Actin-binding"
FT /evidence="ECO:0000255, ECO:0000303|PubMed:19000816"
FT MOTIF 48..54
FT /note="Plasmodium-specific profilin mini-domain"
FT /evidence="ECO:0000269|PubMed:19000816"
FT SITE 35
FT /note="Interaction with Pro-rich sequence"
FT SITE 89
FT /note="Interaction with actin"
FT /evidence="ECO:0000255"
FT HELIX 7..14
FT /evidence="ECO:0007829|PDB:2JKF"
FT HELIX 16..18
FT /evidence="ECO:0007829|PDB:2JKF"
FT STRAND 22..28
FT /evidence="ECO:0007829|PDB:2JKF"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:2JKF"
FT STRAND 34..40
FT /evidence="ECO:0007829|PDB:2JKF"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:2JKF"
FT HELIX 50..53
FT /evidence="ECO:0007829|PDB:2JKF"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:2JKF"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:2JKF"
FT HELIX 76..85
FT /evidence="ECO:0007829|PDB:2JKF"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:2JKF"
FT STRAND 98..111
FT /evidence="ECO:0007829|PDB:2JKF"
FT STRAND 114..123
FT /evidence="ECO:0007829|PDB:2JKF"
FT STRAND 126..133
FT /evidence="ECO:0007829|PDB:2JKF"
FT TURN 134..136
FT /evidence="ECO:0007829|PDB:2JKF"
FT STRAND 137..144
FT /evidence="ECO:0007829|PDB:2JKF"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:2JKF"
FT HELIX 151..168
FT /evidence="ECO:0007829|PDB:2JKF"
SQ SEQUENCE 171 AA; 19017 MW; 1FFBC426787A132C CRC64;
MAEEYSWDSY LNDRLLATNQ VSGAGLASEE DGVVYACVAQ GEESDPNFDK WSLFYKEDYD
IEVEDENGTK TTKTINEGQT ILVVFNEGYA PDGVWLGGTK YQFINIERDL EFEGYNFDVA
TCAKLKGGLH LVKVPGGNIL VVLYDEEKEQ DRGNSKIAAL TFAKELAESS Q
