ID   ACT25_DICDI             Reviewed;         385 AA.
AC   Q54HF0;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Putative actin-25;
GN   Name=act25; ORFNames=DDB_G0289507;
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; EAL62685.1; -; Genomic_DNA.
DR   RefSeq; XP_636188.1; XM_631096.1.
DR   AlphaFoldDB; Q54HF0; -.
DR   SMR; Q54HF0; -.
DR   STRING; 44689.DDB0220463; -.
DR   PaxDb; Q54HF0; -.
DR   EnsemblProtists; EAL62685; EAL62685; DDB_G0289507.
DR   GeneID; 8627175; -.
DR   KEGG; ddi:DDB_G0289507; -.
DR   dictyBase; DDB_G0289507; act25.
DR   eggNOG; KOG0676; Eukaryota.
DR   HOGENOM; CLU_027965_0_2_1; -.
DR   InParanoid; Q54HF0; -.
DR   PhylomeDB; Q54HF0; -.
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:Q54HF0; -.
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:0005200; F:structural constituent of cytoskeleton; ISS:dictyBase.
DR   GO; GO:0006909; P:phagocytosis; ISS:dictyBase.
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   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Cytoskeleton; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..385
FT                   /note="Putative actin-25"
FT                   /id="PRO_0000312675"
SQ   SEQUENCE   385 AA;  43215 MW;  0A229EF7C73925E1 CRC64;
     MECEEVQAIV IDNGSSVCKA GFGGDDAPRT AFPSIVGRPR CTGFIVDMDK KDSYFCKKNS
     CFMGQKDLYI GDEAQSKRGI LNVKYPIERG IITNWNDMEE IWYHTFYNEL HVAPEEHPVL
     LTEPPLNPKA NREKMTQIMF ETFKTPAIYV ANQGVLSLYS TGLTTGIVMN SGDGVSHTVP
     VYEGYILRQA ILSLDLAGRD LTDYMNELLT DRGYYFTTKG EKEIVRGIKE KLSYVALDFE
     AEMQIASASP ALEKSYELPD GQVITIGNER FRCPEALFRP YTGIHETIYN SIMKCDDDIR
     KDLFGSVVLS GGSTMFPGIV DRMNKELTAL APSTMKIKII APPERKYSVW IGGSILASLS
     SFQPRWISKE EYDESGPSIV HRKCF