ACT1_PLAFX
ID ACT1_PLAFX Reviewed; 376 AA.
AC P86287;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=Actin-1 {ECO:0000250|UniProtKB:P60010};
DE AltName: Full=Actin I {ECO:0000250|UniProtKB:P60010};
DE Short=PfACT1 {ECO:0000303|PubMed:15670824};
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 FUNCTION, AND SUBUNIT.
RX PubMed=15670824; DOI=10.1016/j.febslet.2004.12.037;
RA Schueler H., Mueller A.-K., Matuschewski K.;
RT "Unusual properties of Plasmodium falciparum actin: new insights into
RT microfilament dynamics of apicomplexan parasites.";
RL FEBS Lett. 579:655-660(2005).
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 {ECO:0000269|PubMed:15670824}.
CC -!- SUBUNIT: Polymerization of actin is slow and requires the presence of
CC gelsolin and phalloidin (in vitro). Interacts with DNase I with low
CC affinity (in vitro). {ECO:0000269|PubMed:15670824}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the actin family. {ECO:0000255}.
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DR EMBL; AANS01001675; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PDB; 4CBU; X-ray; 1.30 A; A=1-376.
DR PDB; 5OGW; EM; 3.80 A; A/B/C/D/E=1-376.
DR PDBsum; 4CBU; -.
DR PDBsum; 5OGW; -.
DR AlphaFoldDB; P86287; -.
DR SMR; P86287; -.
DR DrugBank; DB11638; Artenimol.
DR VEuPathDB; PlasmoDB:PfHB3_120051000; -.
DR Proteomes; UP000054289; Unassembled WGS sequence.
DR GO; GO:0005884; C:actin filament; IDA: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; IDA:UniProtKB.
DR GO; GO:0070360; P:actin polymerization-dependent cell migration in host; IMP: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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Cytoskeleton; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..376
FT /note="Actin-1"
FT /id="PRO_0000376863"
FT STRAND 9..13
FT /evidence="ECO:0007829|PDB:4CBU"
FT STRAND 15..22
FT /evidence="ECO:0007829|PDB:4CBU"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:4CBU"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:4CBU"
FT HELIX 57..61
FT /evidence="ECO:0007829|PDB:4CBU"
FT TURN 62..65
FT /evidence="ECO:0007829|PDB:4CBU"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:4CBU"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:4CBU"
FT HELIX 80..92
FT /evidence="ECO:0007829|PDB:4CBU"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:4CBU"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:4CBU"
FT HELIX 114..126
FT /evidence="ECO:0007829|PDB:4CBU"
FT STRAND 131..137
FT /evidence="ECO:0007829|PDB:4CBU"
FT HELIX 138..145
FT /evidence="ECO:0007829|PDB:4CBU"
FT STRAND 149..156
FT /evidence="ECO:0007829|PDB:4CBU"
FT STRAND 161..167
FT /evidence="ECO:0007829|PDB:4CBU"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:4CBU"
FT STRAND 177..180
FT /evidence="ECO:0007829|PDB:4CBU"
FT HELIX 183..193
FT /evidence="ECO:0007829|PDB:4CBU"
FT HELIX 194..197
FT /evidence="ECO:0007829|PDB:4CBU"
FT HELIX 204..217
FT /evidence="ECO:0007829|PDB:4CBU"
FT HELIX 224..231
FT /evidence="ECO:0007829|PDB:4CBU"
FT STRAND 239..242
FT /evidence="ECO:0007829|PDB:4CBU"
FT STRAND 248..251
FT /evidence="ECO:0007829|PDB:4CBU"
FT HELIX 254..260
FT /evidence="ECO:0007829|PDB:4CBU"
FT TURN 261..263
FT /evidence="ECO:0007829|PDB:4CBU"
FT HELIX 265..268
FT /evidence="ECO:0007829|PDB:4CBU"
FT HELIX 275..284
FT /evidence="ECO:0007829|PDB:4CBU"
FT HELIX 288..290
FT /evidence="ECO:0007829|PDB:4CBU"
FT HELIX 291..295
FT /evidence="ECO:0007829|PDB:4CBU"
FT STRAND 298..302
FT /evidence="ECO:0007829|PDB:4CBU"
FT HELIX 303..305
FT /evidence="ECO:0007829|PDB:4CBU"
FT HELIX 310..321
FT /evidence="ECO:0007829|PDB:4CBU"
FT HELIX 336..338
FT /evidence="ECO:0007829|PDB:4CBU"
FT HELIX 339..349
FT /evidence="ECO:0007829|PDB:4CBU"
FT HELIX 353..355
FT /evidence="ECO:0007829|PDB:4CBU"
FT STRAND 357..359
FT /evidence="ECO:0007829|PDB:4CBU"
FT HELIX 360..365
FT /evidence="ECO:0007829|PDB:4CBU"
SQ SEQUENCE 376 AA; 41871 MW; EC526236FB47148A CRC64;
MGEEDVQALV 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
SGGTTMYEGI GERLTRDITT LAPSTMKIKV VAPPERKYSV WIGGSILSSL STFQQMWITK
EEYDESGPSI VHRKCF
