ID   ACT18_DICDI             Reviewed;         380 AA.
AC   P07828; Q54HE5;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 3.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Actin-18;
DE   AltName: Full=Actin-3-sub 2;
GN   Name=act18; Synonyms=act3-2; ORFNames=DDB_G0289489;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3003365; DOI=10.1016/0022-2836(85)90108-1;
RA   Romans P., Firtel R.A.;
RT   "Organization of the actin multigene family of Dictyostelium discoideum and
RT   analysis of variability in the protein coding regions.";
RL   J. Mol. Biol. 186:321-335(1985).
RN   [2]
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; X03284; CAA27034.1; -; Genomic_DNA.
DR   EMBL; AAFI02000141; EAL62676.1; -; Genomic_DNA.
DR   PIR; D23412; D23412.
DR   RefSeq; XP_636193.1; XM_631101.1.
DR   AlphaFoldDB; P07828; -.
DR   SMR; P07828; -.
DR   STRING; 44689.DDB0220459; -.
DR   PaxDb; P07828; -.
DR   PRIDE; P07828; -.
DR   EnsemblProtists; EAL62676; EAL62676; DDB_G0289489.
DR   GeneID; 8627180; -.
DR   KEGG; ddi:DDB_G0289489; -.
DR   dictyBase; DDB_G0289489; act18.
DR   eggNOG; KOG0676; Eukaryota.
DR   HOGENOM; CLU_027965_0_2_1; -.
DR   InParanoid; P07828; -.
DR   OMA; SNMKIKI; -.
DR   PhylomeDB; P07828; -.
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:P07828; -.
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:0031012; C:extracellular matrix; 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   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Cytoskeleton; Nucleotide-binding;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..380
FT                   /note="Actin-18"
FT                   /id="PRO_0000088925"
FT   CONFLICT        56
FT                   /note="G -> V (in Ref. 1; CAA27034)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   380 AA;  42532 MW;  6C3FA2D27E23F286 CRC64;
     MEREEVQAIV IDNGSDMCKA GFAGDDAPRA VFQSIVGRPR YTGVMDVMGQ KDSYIGDEAH
     SRKGFLTLKY PIERGIVTNW DDMEEIWHHT FYNELGVAPE EHPVLLTEQP LNPKKNREKM
     TQIMFETFNT PAMYVAIQAV LSLYSSGRTT GIVMDSGDGV SHAVSIYEGH ALPHAILRLD
     LAGRDLSDYM MKILTKRGYS FTTTAEKEII KDIKEKLSYV ALDFDAEMLT AASSTTLEKS
     YELPDGKVIT IGNERFRCPE ALFQPSLLAM ESAGIHETIY NSIMKCDVDI RRYLFGNVIL
     SGGSTMFPGI ADRMNKELTA LAPSTMKIKI IAPPERKYSV WVGGSILASL SSFQEMWISK
     EEYNESGPSI VHRKCSNYLK