ID   ACT2_PLAFO              Reviewed;         376 AA.
AC   P14883;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Actin-2;
DE   AltName: Full=Actin II;
DE            Short=pf-actin II;
OS   Plasmodium falciparum (isolate NF54).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX   NCBI_TaxID=5843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2459617; DOI=10.1016/0166-6851(88)90107-7;
RA   Wesseling J.G., Smits M.A., Schoenmakers J.G.G.;
RT   "Extremely diverged actin proteins in Plasmodium falciparum.";
RL   Mol. Biochem. Parasitol. 30:143-153(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DEVELOPMENTAL STAGE.
RX   PubMed=2671721; DOI=10.1016/0166-6851(89)90119-9;
RA   Wesseling J.G., Snijders P.J.F., van Someren P., Jansen J., Smits M.A.,
RA   Schoenmakers J.G.G.;
RT   "Stage-specific expression and genomic organization of the actin genes of
RT   the malaria parasite Plasmodium falciparum.";
RL   Mol. Biochem. Parasitol. 35:167-176(1989).
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.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC   -!- DEVELOPMENTAL STAGE: Actin-1 is formed in all parasitic stages; asexual
CC       blood stages and in the sexual stages. Actin-2 is stage-specific,
CC       formed only in the sexual stages of the parasite's life cycle.
CC       {ECO:0000269|PubMed:2671721}.
CC   -!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
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DR   EMBL; M18817; AAA29466.1; -; mRNA.
DR   EMBL; M22718; AAA29467.1; -; Genomic_DNA.
DR   PIR; A45525; A54509.
DR   AlphaFoldDB; P14883; -.
DR   SMR; P14883; -.
DR   PRIDE; P14883; -.
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   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; Cytoskeleton; Nucleotide-binding.
FT   CHAIN           1..376
FT                   /note="Actin-2"
FT                   /id="PRO_0000088995"
SQ   SEQUENCE   376 AA;  42679 MW;  87238490FCC9294C CRC64;
     MSEEAVALVV DNGSGMVKSG LAGDDAPKCV FPSIVGRPKM PNIMIGMEQK ECYVGDEAQN
     KRGILTLKYP IEHGIVTNWD DMEKIWHHTF YNELRVSPEE HPVLLTEAPL NPKTNREKMT
     QIMFETFDVP AMYVSIQAIL SLYASGRTTG IVLDSGDGVS HTVPIYEGYV LPHAINRIDM
     AGRDLTYHMM KWFTERGHTF TTTAEREIVR DIKEKLCYIA MDYDEELKRS EEHSDEIEEI
     YELPDGNLIT VGSERFRCPE ALFNPTLIGR ECPGLHITAY QSIMKCDIDI RKELYNNIVL
     SGGTTMYNNI GERLTKEMTN LAPSSMKIKV IAPPERKYSV WIGGSILSSL STFQQMWITK
     EEYEDSGPSI VHRKCF