ID   ACT2_PLAFX              Reviewed;         376 AA.
AC   P86288;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   03-AUG-2022, entry version 33.
DE   RecName: Full=Actin-2 {ECO:0000250|UniProtKB:P60010};
DE   AltName: Full=Actin II {ECO:0000250|UniProtKB:P60010};
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.
CC   -!- FUNCTION: Actins are highly conserved proteins that are involved in
CC       various types of cell motility and are ubiquitously expressed in all
CC       eukaryotic cells. Actin assembles into short polymer microfilaments,
CC       these are thought to contribute to parasite gliding motility (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the actin family. {ECO:0000255}.
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DR   EMBL; AANS01001772; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; P86288; -.
DR   SMR; P86288; -.
DR   PRIDE; P86288; -.
DR   VEuPathDB; PlasmoDB:PfHB3_140018400; -.
DR   Proteomes; UP000054289; Unassembled WGS sequence.
DR   GO; GO:0005884; C:actin filament; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; ISS:UniProtKB.
DR   GO; GO:0070360; P:actin polymerization-dependent cell migration in host; ISS:UniProtKB.
DR   InterPro; IPR004000; Actin.
DR   InterPro; IPR020902; Actin/actin-like_CS.
DR   InterPro; IPR004001; Actin_CS.
DR   InterPro; IPR043129; ATPase_NBD.
DR   PANTHER; PTHR11937; PTHR11937; 1.
DR   Pfam; PF00022; Actin; 1.
DR   PRINTS; PR00190; ACTIN.
DR   SMART; SM00268; ACTIN; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
DR   PROSITE; PS00406; ACTINS_1; 1.
DR   PROSITE; PS00432; ACTINS_2; 1.
DR   PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Cytoskeleton; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..376
FT                   /note="Actin-2"
FT                   /id="PRO_0000376864"
SQ   SEQUENCE   376 AA;  42606 MW;  88688BD4A3822957 CRC64;
     MSEEAVALVV DNGSGMVKSG LAGDDAPKCV FPSIVGRPKM PNIMIGMEQK ECYVGDEAQN
     KRGILTLKYP IEHGIVTNWD DMEKIWHHTF YNELRVSPEE HPVLLTEAPL NPKTNREKMT
     QIMFETFDVP AMYVSIQAIL SLYASGRTTG IVLDSGDGVS HTVPIYEGYV LPHAINRIDM
     AGRDLTYHMM KLFTERGHTF TTTAEREIVR DIKEKLCYIA MDYDEELKRS EEHSDEIEEI
     YELPDGNLIT VGSERFRCPE ALFNPTLIGR ECPGLHITAY QSIMKCDIDI RKELYNNIVL
     SGGTTMYNNI GERLTKEMTN LAPSSMKIKV IAPPERKYSV WIGGSILSSL STFQQMWITK
     EEYEDSGPSI VHRKCF