ACT24_DICDI
ID ACT24_DICDI Reviewed; 377 AA.
AC Q54HF1;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Putative actin-24;
GN Name=act24; ORFNames=DDB_G0289505;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAFI02000141; EAL62684.1; -; Genomic_DNA.
DR RefSeq; XP_636187.1; XM_631095.1.
DR AlphaFoldDB; Q54HF1; -.
DR SMR; Q54HF1; -.
DR STRING; 44689.DDB0220462; -.
DR PaxDb; Q54HF1; -.
DR EnsemblProtists; EAL62684; EAL62684; DDB_G0289505.
DR GeneID; 8627174; -.
DR KEGG; ddi:DDB_G0289505; -.
DR dictyBase; DDB_G0289505; act24.
DR eggNOG; KOG0676; Eukaryota.
DR HOGENOM; CLU_027965_0_2_1; -.
DR InParanoid; Q54HF1; -.
DR PhylomeDB; Q54HF1; -.
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:Q54HF1; -.
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..377
FT /note="Putative actin-24"
FT /id="PRO_0000312674"
SQ SEQUENCE 377 AA; 42138 MW; 67AC474048E0ED59 CRC64;
MECKEDLTIV IDNGSGMCKA GFAGYDAPHA VFPSIVGRPR HTGVMVGMGQ KDSYIGDEAQ
SKRDILNLKF PVERGIITNW NDMEEIWHHT FYNELRVAPE EHPVLLTEPP LNSKANREKM
PQIMFETFNT PAMYVAIQAV LSLYASGRAT GVILDSGDGV SYTVPVYEGN TFPLSITRLH
LAGGDLTDYM SRLLYTDCGY YFSTKAEKEI VKDIKEKLAY VALDFEAEMQ TAASSPSLEK
SYKLPDGRMI TIGNERFRCP EALFQPSLLA MDYDGIHETT YNSIMKCDVD FHKDLYGNVL
LSGGSTMFPG IADRMNKELT ALAPSTMKIK IIAPPERKYS AWIGGSILAS LSSFQPRWIS
KEEYDESGPS IVHRKCW