ID ACTB_PONAB Reviewed; 375 AA. AC Q5R6G0; Q5R582; DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot. DT 21-DEC-2004, sequence version 1. DT 28-JUN-2023, entry version 121. DE RecName: Full=Actin, cytoplasmic 1; DE EC=3.6.4.- {ECO:0000250|UniProtKB:P68137}; DE AltName: Full=Beta-actin; DE Contains: DE RecName: Full=Actin, cytoplasmic 1, N-terminally processed; GN Name=ACTB; OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Pongo. OX NCBI_TaxID=9601; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain cortex; RG The German cDNA consortium; RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Actin is a highly conserved protein that polymerizes to CC produce filaments that form cross-linked networks in the cytoplasm of CC cells. Actin exists in both monomeric (G-actin) and polymeric (F-actin) CC forms, both forms playing key functions, such as cell motility and CC contraction. In addition to their role in the cytoplasmic cytoskeleton, CC G- and F-actin also localize in the nucleus, and regulate gene CC transcription and motility and repair of damaged DNA. Part of the CC ACTR1A/ACTB filament around which the dynactin complex is built. The CC dynactin multiprotein complex activates the molecular motor dynein for CC ultra-processive transport along microtubules (By similarity). CC {ECO:0000250|UniProtKB:P60709, ECO:0000250|UniProtKB:Q6QAQ1}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O = ADP + H(+) + phosphate; 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 -!- SUBUNIT: Polymerization of globular actin (G-actin) leads to a CC structural filament (F-actin) in the form of a two-stranded helix. Each CC actin can bind to 4 others. Identified in a IGF2BP1-dependent mRNP CC granule complex containing untranslated mRNAs. Component of the BAF CC complex, which includes at least actin (ACTB), ARID1A, ARID1B/BAF250, CC SMARCA2, SMARCA4/BRG1, ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57 CC SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1, and one or more of CC SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C. In muscle cells, the CC BAF complex also contains DPF3. Found in a complex with XPO6, Ran, ACTB CC and PFN1. Interacts with XPO6 and EMD. Interacts with ERBB2. Interacts CC with GCSAM (By similarity). Interacts with TBC1D21. Interacts with CC CPNE1 (via VWFA domain) and CPNE4 (via VWFA domain) (By similarity). CC Interacts with DHX9 (via C-terminus); this interaction is direct and CC mediates the attachment to nuclear ribonucleoprotein complexes. CC Interacts with FAM107A (By similarity). Part of the ACTR1A/ACTB CC filament around which the dynactin complex is built. The filament CC contains 8 copies of ACTR1A and 1 ACTB (By similarity). CC {ECO:0000250|UniProtKB:P60709, ECO:0000250|UniProtKB:P60710, CC ECO:0000250|UniProtKB:Q6QAQ1}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton CC {ECO:0000250|UniProtKB:P60709}. Nucleus {ECO:0000250|UniProtKB:P60709}. CC Note=Localized in cytoplasmic mRNP granules containing untranslated CC mRNAs. {ECO:0000250|UniProtKB:P60709}. CC -!- PTM: [Actin, cytoplasmic 1]: N-terminal cleavage of acetylated CC methionine of immature cytoplasmic actin by ACTMAP. CC {ECO:0000250|UniProtKB:P60709}. CC -!- PTM: ISGylated. {ECO:0000250|UniProtKB:P60709}. CC -!- PTM: Oxidation of Met-44 and Met-47 by MICALs (MICAL1, MICAL2 or CC MICAL3) to form methionine sulfoxide promotes actin filament CC depolymerization. MICAL1 and MICAL2 produce the (R)-S-oxide form. The CC (R)-S-oxide form is reverted by MSRB1 and MSRB2, which promote actin CC repolymerization. {ECO:0000250|UniProtKB:P60710}. CC -!- PTM: Monomethylation at Lys-84 (K84me1) regulates actin-myosin CC interaction and actomyosin-dependent processes. Demethylation by ALKBH4 CC is required for maintaining actomyosin dynamics supporting normal CC cleavage furrow ingression during cytokinesis and cell migration. CC {ECO:0000250|UniProtKB:P60709}. CC -!- PTM: [Actin, cytoplasmic 1, N-terminally processed]: N-terminal CC acetylation by NAA80 affects actin filament depolymerization and CC elongation, including elongation driven by formins. In contrast, CC filament nucleation by the Arp2/3 complex is not affected. CC {ECO:0000250|UniProtKB:P60709}. CC -!- PTM: Methylated at His-73 by SETD3 (By similarity). Methylation at His- CC 73 is required for smooth muscle contraction of the laboring uterus CC during delivery (By similarity). {ECO:0000250|UniProtKB:P60709, CC ECO:0000250|UniProtKB:P60710}. CC -!- MISCELLANEOUS: In vertebrates 3 main groups of actin isoforms, alpha, CC beta and gamma have been identified. The alpha actins are found in CC muscle tissues and are a major constituent of the contractile CC apparatus. The beta and gamma actins coexist in most cell types as CC components of the cytoskeleton and as mediators of internal cell CC motility. {ECO:0000250|UniProtKB:P60709}. 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; CR860530; CAH92656.1; -; mRNA. DR EMBL; CR860982; CAH93084.1; -; mRNA. DR RefSeq; NP_001126826.1; NM_001133354.1. DR AlphaFoldDB; Q5R6G0; -. DR SMR; Q5R6G0; -. DR STRING; 9601.ENSPPYP00000019427; -. DR Ensembl; ENSPPYT00000020193; ENSPPYP00000019427; ENSPPYG00000017336. DR GeneID; 100173832; -. DR KEGG; pon:100173832; -. DR CTD; 60; -. DR eggNOG; KOG0676; Eukaryota. DR GeneTree; ENSGT00950000182960; -. DR HOGENOM; CLU_027965_0_2_1; -. DR InParanoid; Q5R6G0; -. DR OMA; FHTTAER; -. DR OrthoDB; 10at2759; -. DR TreeFam; TF354237; -. DR Proteomes; UP000001595; Unplaced. DR GO; GO:0015629; C:actin cytoskeleton; ISS:UniProtKB. DR GO; GO:0005912; C:adherens junction; IEA:Ensembl. DR GO; GO:0043296; C:apical junction complex; IEA:Ensembl. DR GO; GO:0005903; C:brush border; IEA:Ensembl. DR GO; GO:0044305; C:calyx of Held; IEA:Ensembl. DR GO; GO:0030863; C:cortical cytoskeleton; IEA:Ensembl. DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IEA:Ensembl. DR GO; GO:0005856; C:cytoskeleton; ISS:AgBase. DR GO; GO:0005829; C:cytosol; IEA:Ensembl. DR GO; GO:0097433; C:dense body; ISS:AgBase. DR GO; GO:0005925; C:focal adhesion; ISS:AgBase. DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl. DR GO; GO:0030027; C:lamellipodium; IEA:Ensembl. DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IEA:Ensembl. DR GO; GO:0000786; C:nucleosome; IEA:Ensembl. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; ISS:AgBase. DR GO; GO:0098871; C:postsynaptic actin cytoskeleton; IEA:Ensembl. DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB. DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:Ensembl. DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl. DR GO; GO:0070160; C:tight junction; IEA:Ensembl. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl. DR GO; GO:0019894; F:kinesin binding; IEA:Ensembl. DR GO; GO:0050998; F:nitric-oxide synthase binding; IEA:Ensembl. DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl. DR GO; GO:0098973; F:structural constituent of postsynaptic actin cytoskeleton; IEA:Ensembl. DR GO; GO:0030957; F:Tat protein binding; IEA:Ensembl. DR GO; GO:0034333; P:adherens junction assembly; IEA:Ensembl. DR GO; GO:0045176; P:apical protein localization; IEA:Ensembl. DR GO; GO:0048870; P:cell motility; IEA:Ensembl. DR GO; GO:0072749; P:cellular response to cytochalasin B; IEA:Ensembl. DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IEA:Ensembl. DR GO; GO:0043968; P:histone H2A acetylation; IEA:Ensembl. DR GO; GO:0043967; P:histone H4 acetylation; IEA:Ensembl. DR GO; GO:0001738; P:morphogenesis of a polarized epithelium; IEA:Ensembl. DR GO; GO:0032091; P:negative regulation of protein binding; IEA:Ensembl. DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; IEA:Ensembl. DR GO; GO:0071896; P:protein localization to adherens junction; IEA:Ensembl. DR GO; GO:0051726; P:regulation of cell cycle; IEA:Ensembl. DR GO; GO:0051621; P:regulation of norepinephrine uptake; IEA:Ensembl. DR GO; GO:1903076; P:regulation of protein localization to plasma membrane; IEA:Ensembl. DR GO; GO:1900242; P:regulation of synaptic vesicle endocytosis; IEA:Ensembl. DR GO; GO:0150111; P:regulation of transepithelial transport; IEA:Ensembl. DR GO; GO:0022898; P:regulation of transmembrane transporter activity; IEA:Ensembl. DR CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1. DR Gene3D; 3.30.420.40; -; 2. 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 PANTHER; PTHR11937:SF192; ACTIN, CYTOPLASMIC 2; 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 2: Evidence at transcript level; KW Acetylation; ATP-binding; Cytoplasm; Cytoskeleton; Hydrolase; Methylation; KW Nucleotide-binding; Nucleus; Oxidation; Reference proteome; KW Ubl conjugation. FT CHAIN 1..375 FT /note="Actin, cytoplasmic 1" FT /id="PRO_0000291871" FT INIT_MET 1 FT /note="Removed; alternate" FT /evidence="ECO:0000250|UniProtKB:P60709" FT CHAIN 2..375 FT /note="Actin, cytoplasmic 1, N-terminally processed" FT /id="PRO_0000367079" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000250|UniProtKB:P60709" FT MOD_RES 2 FT /note="N-acetylaspartate; in Actin, cytoplasmic 1, N- FT terminally processed" FT /evidence="ECO:0000250|UniProtKB:P60709" FT MOD_RES 44 FT /note="Methionine (R)-sulfoxide" FT /evidence="ECO:0000250|UniProtKB:P60710" FT MOD_RES 47 FT /note="Methionine (R)-sulfoxide" FT /evidence="ECO:0000250|UniProtKB:P60710" FT MOD_RES 73 FT /note="Tele-methylhistidine" FT /evidence="ECO:0000250|UniProtKB:P60710" FT MOD_RES 84 FT /note="N6-methyllysine" FT /evidence="ECO:0000250|UniProtKB:P60709" FT CONFLICT 288 FT /note="D -> N (in Ref. 1; CAH93084)" FT /evidence="ECO:0000305" SQ SEQUENCE 375 AA; 41737 MW; 6AFD05CA94E360E2 CRC64; MDDDIAALVV DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS KRGILTLKYP IEHGIVTNWD DMEKIWHHTF YNELRVAPEE HPVLLTEAPL NPKANREKMT QIMFETFNTP AMYVAIQAVL SLYASGRTTG IVMDSGDGVT HTVPIYEGYA LPHAILRLDL AGRDLTDYLM KILTERGYSF TTTAEREIVR DIKEKLCYVA LDFEQEMATA ASSSSLEKSY ELPDGQVITI GNERFRCPEA LFQPSFLGME SCGIHETTFN SIMKCDVDIR KDLYANTVLS GGTTMYPGIA DRMQKEITAL APSTMKIKII APPERKYSVW IGGSILASLS TFQQMWISKQ EYDESGPSIV HRKCF //