ID   ACT1_PLAFO              Reviewed;         376 AA.
AC   P10988;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Actin-1;
DE   AltName: Full=Actin I;
DE            Short=pf-actin I;
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 [GENOMIC DNA / MRNA].
RX   PubMed=3278231; DOI=10.1016/0166-6851(88)90051-5;
RA   Wesseling J.G., de Ree J.M., Ponnudurai T., Smits M.A.,
RA   Schoenmakers J.G.G.;
RT   "Nucleotide sequence and deduced amino acid sequence of a Plasmodium
RT   falciparum actin gene.";
RL   Mol. Biochem. Parasitol. 27:313-320(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
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).
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:2459617}.
CC   -!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
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DR   EMBL; M19146; AAA29464.1; -; mRNA.
DR   EMBL; M22719; AAA29465.1; -; Genomic_DNA.
DR   PIR; A54496; A54496.
DR   AlphaFoldDB; P10988; -.
DR   SMR; P10988; -.
DR   PRIDE; P10988; -.
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-1"
FT                   /id="PRO_0000088994"
SQ   SEQUENCE   376 AA;  41843 MW;  265CC9D44EA4F57D CRC64;
     MGEEVVQALV VDNGSGNVKA GVAGDDAPRS VFPSIVGRPK NPGIMVGMEE KDAFVGDEAQ
     TKRGILTLKY PIEHGIVTNW DDMEKIWHHT FYNELRAAPE EHPVLLTEAP LNPKGNRERM
     TQIMFESFNV PAMYVAIQAV LSLYSSGRTT GIVLDSGDGV SHTVPIYEGY ALPHAIMRLD
     LAGRDLTEYL MKILHERGYG FSTSAEKEIV RDIKEKLCYI ALNFDEEMKT SEQSSDIEKS
     YELPDGNIIT VGNERFRCPE ALFQPSFLGK EAAGIHTTTF NSIKKCDVDI RKDLYGNIVL
     SGGTTMYEGT GERLTRDITT LAPSTMKIKV VAPPERKYSV WIGGSILSSL STFQQMWITK
     EEYDESGPSI VHRKCF