ACTA_PHYPO
ID ACTA_PHYPO Reviewed; 376 AA.
AC P02576;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Actin, plasmodial isoform;
GN Name=ARDA;
GN and
GN Name=ARDB;
GN and
GN Name=ARDC;
OS Physarum polycephalum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Myxogastria;
OC Myxogastromycetidae; Physariida; Physaraceae; Physarum.
OX NCBI_TaxID=5791;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2951301; DOI=10.1016/0378-1119(86)90359-8;
RA Nader W.F., Isenberg G., Sauer H.W.;
RT "Structure of Physarum actin gene locus ardA: a nonpalindromic sequence
RT causes inviability of phage lambda and recA-independent deletions.";
RL Gene 48:133-144(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=M3CVIII;
RX PubMed=3172209; DOI=10.1016/0022-2836(88)90528-1;
RA Gonzales-Y-Merchand J.A., Cox R.A.;
RT "Structure and expression of an actin gene of Physarum polycephalum.";
RL J. Mol. Biol. 202:161-168(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3402310; DOI=10.1089/dna.1.1988.7.317;
RA Hamelin M., Adam L., Lemieux G., Pallotta D.;
RT "Expression of the three unlinked isocoding actin genes of Physarum
RT polycephalum.";
RL DNA 7:317-328(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ARDB).
RC STRAIN=LU648 X LU688;
RX PubMed=1525865; DOI=10.1007/bf00351700;
RA Burland T., Bailey J., Adam L., Mukhopadhyay M.J., Dove W.F., Pallotta D.;
RT "Transient expression in Physarum of a chloramphenicol acetyltransferase
RT gene under the control of actin gene promoters.";
RL Curr. Genet. 21:393-398(1992).
RN [5]
RP PROTEIN SEQUENCE OF 2-376, METHYLATION AT HIS-74, AND ABSENCE OF
RP METHYLATION AT LYS-85.
RX PubMed=732876; DOI=10.1038/276720a0;
RA Vandekerckhove J., Weber K.;
RT "The amino acid sequence of Physarum actin.";
RL Nature 276:720-721(1978).
RN [6]
RP PHOSPHORYLATION AT THR-203 AND THR-204 BY AFK.
RX PubMed=1324166; DOI=10.1002/j.1460-2075.1992.tb05395.x;
RA Gettemans J., de Ville Y., Vandekerckhove J., Waelkens E.;
RT "Physarum actin is phosphorylated as the actin-fragmin complex at residues
RT Thr203 and Thr202 by a specific 80 kDa kinase.";
RL EMBO J. 11:3185-3191(1992).
RN [7]
RP PHOSPHORYLATION AT THR-202 BY AFK.
RX PubMed=1315751; DOI=10.1016/s0021-9258(19)50427-6;
RA Furuhashi K., Hatano S., Ando S., Nishizawa K., Inagaki M.;
RT "Phosphorylation by actin kinase of the pointed end domain on the actin
RT molecule.";
RL J. Biol. Chem. 267:9326-9330(1992).
RN [8]
RP PHOSPHORYLATION AT THR-203 AND THR-204 BY AFK.
RX PubMed=8896448; DOI=10.1002/j.1460-2075.1996.tb00939.x;
RA Eichinger L., Bomblies L., Vandekerckhove J., Schleicher M., Gettemans J.;
RT "A novel type of protein kinase phosphorylates actin in the actin-fragmin
RT complex.";
RL EMBO J. 15:5547-5556(1996).
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 -!- PTM: Phosphorylated by actin-fragmin kinase (AFK).
CC {ECO:0000269|PubMed:1315751, ECO:0000269|PubMed:1324166,
CC ECO:0000269|PubMed:8896448}.
CC -!- MISCELLANEOUS: This protein is the only actin found in the cytoplasm of
CC the plasmodium of Physarum polycephalum.
CC -!- MISCELLANEOUS: There are three different genes which code for this
CC actin.
CC -!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
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DR EMBL; M15272; AAA29971.1; -; Genomic_DNA.
DR EMBL; X07792; CAA30629.1; -; Genomic_DNA.
DR EMBL; M21501; AAA29970.1; -; mRNA.
DR EMBL; M21500; AAA29969.1; -; mRNA.
DR EMBL; X60788; CAA43201.1; -; Genomic_DNA.
DR PIR; A29044; ATFY.
DR AlphaFoldDB; P02576; -.
DR SMR; P02576; -.
DR iPTMnet; P02576; -.
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 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW Methylation; Nucleotide-binding; Phosphoprotein.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:732876"
FT CHAIN 2..376
FT /note="Actin, plasmodial isoform"
FT /id="PRO_0000088988"
FT SITE 85
FT /note="Not N6-methylated"
FT /evidence="ECO:0000269|PubMed:732876"
FT MOD_RES 2
FT /note="Blocked amino end (Glu)"
FT MOD_RES 74
FT /note="Tele-methylhistidine"
FT /evidence="ECO:0000269|PubMed:732876"
FT MOD_RES 202
FT /note="Phosphothreonine; by AFK"
FT /evidence="ECO:0000269|PubMed:1315751"
FT MOD_RES 203
FT /note="Phosphothreonine; by AFK"
FT /evidence="ECO:0000269|PubMed:1324166,
FT ECO:0000269|PubMed:8896448"
FT MOD_RES 204
FT /note="Phosphothreonine; by AFK"
FT /evidence="ECO:0000269|PubMed:1324166,
FT ECO:0000269|PubMed:8896448"
SQ SEQUENCE 376 AA; 41800 MW; 3E22438B2A08E216 CRC64;
MEGEDVQALV IDNGSGMCKA GFAGDDAPRA VFPSIVGRPR HTGVMVGMGQ KDSYVGDEAQ
SKRGILTLKY PIEHGIVTNW DDMEKIWHHT FYNELRVAPE EHPVLLTEAP LNPKANREKM
TQIMFETFNT PAMYVAIQAV LSLYASGRTT GIVMDSGDGV SHTVPIYEGY ALPHAILRLD
LAGRDLTDYL MKILTERGYS FTTTAEREIV RDIKEKLAYV ALDFEQEMQT AASSSALEKS
YELPDGQVIT IGNERFRCPE ALFQPSFLGM ESAGIHETTY NSIMKCDVDI RKDLYGNVVL
SGGTTMFPGI ADRMQKELTA LAPSTMKIKI IAPPERKYSV WIGGSILASL STFQQMWISK
EEYDESGPSI VHRKCF
