ID   ACT28_DICDI             Reviewed;         353 AA.
AC   Q54HE7;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Putative actin-28;
GN   Name=act28; ORFNames=DDB_G0289511;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(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. Multiple isoforms are involved in various cellular
CC       functions such as cytoskeleton structure, cell mobility, chromosome
CC       movement and muscle contraction (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
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DR   EMBL; AAFI02000141; EAL62687.1; -; Genomic_DNA.
DR   RefSeq; XP_636191.1; XM_631099.1.
DR   AlphaFoldDB; Q54HE7; -.
DR   SMR; Q54HE7; -.
DR   STRING; 44689.DDB0229354; -.
DR   PaxDb; Q54HE7; -.
DR   PRIDE; Q54HE7; -.
DR   EnsemblProtists; EAL62687; EAL62687; DDB_G0289511.
DR   GeneID; 8627178; -.
DR   KEGG; ddi:DDB_G0289511; -.
DR   dictyBase; DDB_G0289511; act28.
DR   eggNOG; KOG0676; Eukaryota.
DR   HOGENOM; CLU_027965_0_2_1; -.
DR   InParanoid; Q54HE7; -.
DR   PhylomeDB; Q54HE7; -.
DR   Reactome; R-DDI-114608; Platelet degranulation.
DR   Reactome; R-DDI-196025; Formation of annular gap junctions.
DR   Reactome; R-DDI-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR   Reactome; R-DDI-5626467; RHO GTPases activate IQGAPs.
DR   Reactome; R-DDI-5663213; RHO GTPases Activate WASPs and WAVEs.
DR   Reactome; R-DDI-8856828; Clathrin-mediated endocytosis.
DR   Reactome; R-DDI-9013418; RHOBTB2 GTPase cycle.
DR   PRO; PR:Q54HE7; -.
DR   Proteomes; UP000002195; Chromosome 5.
DR   GO; GO:0015629; C:actin cytoskeleton; ISS:dictyBase.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0017022; F:myosin binding; ISS:dictyBase.
DR   GO; GO:0008976; F:polyphosphate kinase activity; IDA:dictyBase.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; ISS:dictyBase.
DR   GO; GO:0006909; P:phagocytosis; ISS:dictyBase.
DR   InterPro; IPR004000; Actin.
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.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Cytoskeleton; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..353
FT                   /note="Putative actin-28"
FT                   /id="PRO_0000312678"
SQ   SEQUENCE   353 AA;  39323 MW;  964890F1634BFA59 CRC64;
     MEINVQAIVI DNGSDTCKAG FVGEEAPRSE FPSIVGIDQN DKDSYVGNEA QSKRGILTLK
     YPIERGIITN WDDMEKIWHH AFYNELGVAP EENIVVLSES PLNPEENREK MAQIMFETFK
     TPAIYVENQA VFSIYNSGRM TGIVLDSGDS ASHVVPVYEG LALPLATSSL GFAGCDLTDQ
     MSLLLNDLGY NLEREIVRDI KEKLSYVSSD FLWEIDDPSL EKSYELPDGQ VITIGKELLA
     CSEGLFLPYV FFGTNLDGID KAIYNSIMKC DVDIHNDLYG NVVLSGGSTM FPGIEYRMYK
     ELTQLAPSTT EIVINAPPER KNSVWIGGSI LGLVPNFPEL CFDKEDYDEY GRL