ID   ACT23_DICDI             Reviewed;         358 AA.
AC   Q55EU6;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Putative actin-23;
GN   Name=act23; ORFNames=DDB_G0268744;
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).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=AX2;
RX   PubMed=16926386; DOI=10.1074/mcp.m600113-mcp200;
RA   Gotthardt D., Blancheteau V., Bosserhoff A., Ruppert T., Delorenzi M.,
RA   Soldati T.;
RT   "Proteomics fingerprinting of phagosome maturation and evidence for the
RT   role of a Galpha during uptake.";
RL   Mol. Cell. Proteomics 5:2228-2243(2006).
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; AAFI02000004; EAL72961.1; -; Genomic_DNA.
DR   RefSeq; XP_646924.1; XM_641832.1.
DR   AlphaFoldDB; Q55EU6; -.
DR   SMR; Q55EU6; -.
DR   STRING; 44689.DDB0220461; -.
DR   PaxDb; Q55EU6; -.
DR   EnsemblProtists; EAL72961; EAL72961; DDB_G0268744.
DR   GeneID; 8616612; -.
DR   KEGG; ddi:DDB_G0268744; -.
DR   dictyBase; DDB_G0268744; act23.
DR   eggNOG; KOG0676; Eukaryota.
DR   HOGENOM; CLU_027965_0_2_1; -.
DR   InParanoid; Q55EU6; -.
DR   OMA; THKEEYI; -.
DR   PhylomeDB; Q55EU6; -.
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:Q55EU6; -.
DR   Proteomes; UP000002195; Chromosome 1.
DR   GO; GO:0015629; C:actin cytoskeleton; ISS:dictyBase.
DR   GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
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; 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; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..358
FT                   /note="Putative actin-23"
FT                   /id="PRO_0000312673"
SQ   SEQUENCE   358 AA;  39964 MW;  E3ADB69D28AA6821 CRC64;
     MCKAGFAGDD APCTVFPSIV GRPRHTGVMV GMCQKGSYVG DEAQSKRGIL TLKYPIEHGI
     VTNWDDMEKI WHHTFYNELR VAPEEHPVLL TEAPLNPKAN REKMTQIMFE TFNTPAMYVA
     IQAVLSLYAS GRTTGIVMDS GDGVSHTVPI YEGYALPHAI LRLDLAGRDL TDYLMKILTE
     RGYSFTTTAE REIVRDIKEK LAYVALDFEA EMQTATSSAL EKSYELPDGQ VITIGNERFR
     CPEALFQPSF LGMESAGIHE TTYNSIMKCD VDIRKDLYGN VVLSGGTTMF PGIADRMNKE
     LTALAPSTMK IKIIAPPERK YSVWIGSILA SLSTFQQMWI SKEEYDESGP SIVHRKCF