ACT2_PLAF7
ID ACT2_PLAF7 Reviewed; 376 AA.
AC Q8ILW9;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Actin-2;
DE AltName: Full=Actin II;
GN ORFNames=PF14_0124;
OS Plasmodium falciparum (isolate 3D7).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=36329;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7;
RX PubMed=12368864; DOI=10.1038/nature01097;
RA Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W.,
RA Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T., James K.D.,
RA Eisen J.A., Rutherford K.M., Salzberg S.L., Craig A., Kyes S., Chan M.-S.,
RA Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S., Pertea M.,
RA Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B., Martin D.M.A.,
RA Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A., McFadden G.I.,
RA Cummings L.M., Subramanian G.M., Mungall C., Venter J.C., Carucci D.J.,
RA Hoffman S.L., Newbold C., Davis R.W., Fraser C.M., Barrell B.G.;
RT "Genome sequence of the human malaria parasite Plasmodium falciparum.";
RL Nature 419:498-511(2002).
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 -!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
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DR EMBL; AE014187; AAN36736.1; -; Genomic_DNA.
DR RefSeq; XP_001348297.1; XM_001348261.1.
DR AlphaFoldDB; Q8ILW9; -.
DR SMR; Q8ILW9; -.
DR BioGRID; 1207072; 1.
DR IntAct; Q8ILW9; 1.
DR STRING; 5833.PF14_0124; -.
DR PRIDE; Q8ILW9; -.
DR EnsemblProtists; CZT99835; CZT99835; PF3D7_1412500.
DR GeneID; 811705; -.
DR KEGG; pfa:PF3D7_1412500; -.
DR VEuPathDB; PlasmoDB:PF3D7_1412500; -.
DR HOGENOM; CLU_027965_0_2_1; -.
DR InParanoid; Q8ILW9; -.
DR OMA; PNIMVGM; -.
DR PhylomeDB; Q8ILW9; -.
DR Reactome; R-PFA-114608; Platelet degranulation.
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:0000146; F:microfilament motor activity; TAS:GeneDB.
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 GO; GO:0007010; P:cytoskeleton organization; TAS:GeneDB.
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.
FT CHAIN 1..376
FT /note="Actin-2"
FT /id="PRO_0000233392"
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