ACT_ENTHI
ID ACT_ENTHI Reviewed; 376 AA.
AC P11426;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Actin;
OS Entamoeba histolytica.
OC Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC Entamoeba.
OX NCBI_TaxID=5759;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=ATCC 30459 / HM-1:IMSS;
RX PubMed=2883657; DOI=10.1073/pnas.84.9.3024;
RA Edman U., Meza I., Agabian N.;
RT "Genomic and cDNA actin sequences from a virulent strain of Entamoeba
RT histolytica.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:3024-3028(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2888016; DOI=10.1016/0166-6851(87)90154-x;
RA Huber M., Garfinkel L., Gitler C., Mirelman D., Revel M., Rozenblatt S.;
RT "Entamoeba histolytica: cloning and characterization of actin cDNA.";
RL Mol. Biochem. Parasitol. 24:227-235(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE OF 1-137.
RC STRAIN=ATCC 30459 / HM-1:IMSS;
RA Brachhaus I., Loippe M., Lioutas C., Tannich E.;
RL Submitted (JAN-1993) 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.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
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DR EMBL; M16339; AAA29082.1; -; Genomic_DNA.
DR EMBL; M16340; AAA29083.1; -; mRNA.
DR EMBL; M16341; AAA29084.1; -; mRNA.
DR EMBL; M19871; AAA29086.1; -; mRNA.
DR EMBL; X70852; CAA50205.1; -; Genomic_DNA.
DR PIR; A29877; ATAXE.
DR AlphaFoldDB; P11426; -.
DR SMR; P11426; -.
DR STRING; 5759.rna_EHI_107290-1; -.
DR VEuPathDB; AmoebaDB:EHI5A_072340; -.
DR VEuPathDB; AmoebaDB:EHI7A_173380; -.
DR VEuPathDB; AmoebaDB:EHI8A_198160; -.
DR VEuPathDB; AmoebaDB:EHI_107290; -.
DR VEuPathDB; AmoebaDB:KM1_268200; -.
DR eggNOG; KOG0676; Eukaryota.
DR OMA; FHTTAER; -.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:UniProt.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR GO; GO:0006909; P:phagocytosis; IEA:UniProt.
DR GO; GO:0042221; P:response to chemical; IEA:UniProt.
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"
FT /id="PRO_0000088938"
SQ SEQUENCE 376 AA; 42030 MW; CB123BCEF6AACCD3 CRC64;
MGDEEVQALV VDNGSGMCKA GFAGDDAPRA VFPSIVGRPR HVSVMAGMGQ KDAYVGDEAQ
SKRGILTLKY PIEHGIVNNW DDMEKIWHHT FYNELRVAPE EHPVLLTEAP MNPKANREKM
TQIMFETFNT PAMYVGIQAV LSLYASGRTT GIVMDSGDGV SHTVPIYEGF SLPHAILRLD
LAGRDLTDYL MKILTERGYA FTTTAEREIV RDIKEKLCYV AEDFNEEMQK AASSSELEKS
YELPDGQVIT VGNERFRCPE ALFQPSFLGM ECNGIHETTY NSIMKCDVDI RKDLYGNIVL
SGGTSMYPGI NTRLEKEMIQ LAPPTMKIKV IAPPERKYSV WIGGSILASL STFQNMWITK
EEYDESGPAI VHRKCF