ID ACT4_CAEEL Reviewed; 376 AA. AC P10986; Q7YSY2; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 2. DT 04-NOV-2026, entry version 180. DE RecName: Full=Actin-4; DE EC=3.6.4.- {ECO:0000250|UniProtKB:P68137}; DE Flags: Precursor; GN Name=act-4; ORFNames=M03F4.2; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; OC Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=2795655; DOI=10.1016/0022-2836(89)90503-2; RA Krause M., Wild M., Rosenzweig B., Hirsh D.; RT "Wild-type and mutant actin genes in Caenorhabditis elegans."; RL J. Mol. Biol. 208:381-392(1989). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2; RX PubMed=9851916; DOI=10.1126/science.282.5396.2012; RG The C. elegans sequencing consortium; RT "Genome sequence of the nematode C. elegans: a platform for investigating RT biology."; RL Science 282:2012-2018(1998). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-86. RX PubMed=6302275; DOI=10.1016/0022-2836(83)90056-6; RA Files J.G., Carr S., Hirsh D.; RT "Actin gene family of Caenorhabditis elegans."; RL J. Mol. Biol. 164:355-375(1983). 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. {ECO:0000269|PubMed:2795655}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O = ADP + phosphate + H(+); Xref=Rhea:RHEA:13065, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; CC Evidence={ECO:0000250|UniProtKB:P68137}; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton CC {ECO:0000269|PubMed:2795655}. CC -!- MISCELLANEOUS: In this organism there are four genes coding for actin. CC The sequences coded by genes 1 and 3 are identical. There are a few CC variations in the actins coded by genes 2 and 4. 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; X16799; CAA34720.1; -; Genomic_DNA. DR EMBL; X16800; CAA34720.1; JOINED; Genomic_DNA. DR EMBL; FO081654; CCD83476.1; -; Genomic_DNA. DR EMBL; J01046; AAA27890.1; -; Genomic_DNA. DR EMBL; J01045; AAA27890.1; JOINED; Genomic_DNA. DR PIR; S27135; S27135. DR RefSeq; NP_508841.1; NM_076440.8. DR AlphaFoldDB; P10986; -. DR SMR; P10986; -. DR BioGRID; 45702; 24. DR DIP; DIP-27204N; -. DR FunCoup; P10986; 1790. DR IntAct; P10986; 10. DR STRING; 6239.M03F4.2a.1; -. DR PaxDb; 6239-M03F4.2a.1; -. DR PeptideAtlas; P10986; -. DR EnsemblMetazoa; M03F4.2a.1; M03F4.2a.1; WBGene00000066. DR GeneID; 180767; -. DR KEGG; cel:CELE_M03F4.2; -. DR UCSC; M03F4.2a; c. elegans. DR AGR; WB:WBGene00000066; -. DR CTD; 180767; -. DR WormBase; M03F4.2a; CE12358; WBGene00000066; act-4. DR eggNOG; KOG0676; Eukaryota. DR InParanoid; P10986; -. DR OMA; AIMRVDM; -. DR OrthoDB; 9973372at2759; -. DR PhylomeDB; P10986; -. DR Reactome; R-CEL-114608; Platelet degranulation. DR Reactome; R-CEL-9035034; RHOF GTPase cycle. DR PRO; PR:P10986; -. DR Proteomes; UP000001940; Chromosome X. DR Bgee; WBGene00000066; Expressed in pharyngeal muscle cell (C elegans) and 4 other cell types or tissues. DR ExpressionAtlas; P10986; baseline and differential. DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central. DR GO; GO:0005856; C:cytoskeleton; ISS:WormBase. DR GO; GO:0045121; C:membrane raft; HDA:WormBase. DR GO; GO:0005865; C:striated muscle thin filament; IDA:WormBase. DR GO; GO:0016887; F:ATP hydrolysis activity; ISS:UniProtKB. DR GO; GO:0005200; F:structural constituent of cytoskeleton; ISS:WormBase. DR GO; GO:0030036; P:actin cytoskeleton organization; ISS:WormBase. DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IBA:GO_Central. DR GO; GO:0000281; P:mitotic cytokinesis; IBA:GO_Central. DR CDD; cd10224; ASKHA_NBD_actin; 1. DR FunFam; 3.30.420.40:FF:000218; actin, alpha sarcomeric/skeletal-like; 1. DR FunFam; 3.30.420.40:FF:000291; Actin, alpha skeletal muscle; 1. DR FunFam; 3.90.640.10:FF:000047; Actin, alpha skeletal muscle; 1. DR FunFam; 3.30.420.40:FF:000058; Putative actin-related protein 5; 1. DR Gene3D; 3.30.420.40; -; 2. DR Gene3D; 3.90.640.10; Actin, Chain A, domain 4; 1. DR InterPro; IPR004000; Actin. DR InterPro; IPR020902; Actin/actin-like_CS. DR InterPro; IPR004001; Actin_CS. DR InterPro; IPR043129; ATPase_NBD. DR PANTHER; PTHR11937; ACTIN; 1. DR Pfam; PF00022; Actin; 1. DR PRINTS; PR00190; ACTIN. DR SMART; SM00268; ACTIN; 1. DR SUPFAM; SSF53067; Actin-like ATPase domain; 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 Acetylation; ATP-binding; Cytoplasm; Cytoskeleton; Hydrolase; KW Nucleotide-binding; Reference proteome. FT PROPEP 1..2 FT /note="Removed in mature form" FT /evidence="ECO:0000250" FT /id="PRO_0000000654" FT CHAIN 3..376 FT /note="Actin-4" FT /id="PRO_0000000655" FT MOD_RES 3 FT /note="N-acetylaspartate" FT /evidence="ECO:0000250" FT CONFLICT 5 FT /note="E -> D (in Ref. 3; AAA27890)" FT /evidence="ECO:0000305" SQ SEQUENCE 376 AA; 41778 MW; 4DF86D2E14623560 CRC64; MCDDEVAALV VDNGSGMCKA GFAGDDAPRA VFPSIVGRPR HQGVMVGMGQ KDSYVGDEAQ SKRGILTLKY PIEHGIVTNW DDMEKIWHHT FYNELRVAPE EHPVLLTEAP LNPKANREKM TQIMFETFNT PAMYVAIQAV LSLYASGRTT GVVLDSGDGV THTVPIYEGY ALPHAILRLD LAGRDLTDYL MKILTERGYS FTTTAEREIV RDIKEKLCYV ALDFEQEMAT AASSSSLEKS YELPDGQVIT VGNERFRCPE ALFQPSFLGM ESAGIHETSY NSIMKCDIDI RKDLYANTVL SGGTTMYPGI ADRMQKEITA LAPSTMKIKI IAPPERKYSV WIGGSILASL STFQQMWISK QEYDESGPSI VHRKCF //