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 13-FEB-2019, entry version 103. DE RecName: Full=Actin, cytoplasmic 1; 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; 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 CC of cells. Actin exists in both monomeric (G-actin) and polymeric CC (F-actin) forms, both forms playing key functions, such as cell CC motility and contraction. In addition to their role in the CC cytoplasmic cytoskeleton, G- and F-actin also localize in the CC nucleus, and regulate gene transcription and motility and repair CC of damaged DNA. {ECO:0000250|UniProtKB:P60709}. CC -!- SUBUNIT: Polymerization of globular actin (G-actin) leads to a CC structural filament (F-actin) in the form of a two-stranded helix. CC Each actin can bind to 4 others. Identified in a IGF2BP1-dependent CC mRNP granule complex containing untranslated mRNAs. Component of CC the BAF complex, which includes at least actin (ACTB), ARID1A, CC ARID1B/BAF250, SMARCA2, SMARCA4/BRG1, ACTL6A/BAF53, ACTL6B/BAF53B, CC SMARCE1/BAF57 SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1, CC and one or more of SMARCD1/BAF60A, SMARCD2/BAF60B, or CC SMARCD3/BAF60C. In muscle cells, the BAF complex also contains CC DPF3. Found in a complex with XPO6, Ran, ACTB and PFN1. Interacts CC with XPO6 and EMD. Interacts with ERBB2. Interacts with GCSAM (By CC similarity). Interacts with TBC1D21. Interacts with CPNE1 (via CC VWFA domain) and CPNE4 (via VWFA domain) (By similarity). CC Interacts with DHX9 (via C-terminus); this interaction is direct CC and mediates the attachment to nuclear ribonucleoprotein CC complexes. Interacts with FAM107A (By similarity). CC {ECO:0000250|UniProtKB:P60709, ECO:0000250|UniProtKB:P60710}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton CC {ECO:0000250|UniProtKB:P60709}. Nucleus CC {ECO:0000250|UniProtKB:P60709}. Note=Localized in cytoplasmic mRNP CC granules containing untranslated mRNAs. 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. CC The (R)-S-oxide form is reverted by MSRB1 and MSRB2, which promote CC actin repolymerization. {ECO:0000250|UniProtKB:P60710}. CC -!- PTM: Monomethylation at Lys-84 (K84me1) regulates actin-myosin CC interaction and actomyosin-dependent processes. Demethylation by CC ALKBH4 is required for maintaining actomyosin dynamics supporting CC normal cleavage furrow ingression during cytokinesis and cell CC migration. {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 CC His-73 is required for smooth muscle contraction of the laboring CC uterus during delivery (By similarity). CC {ECO:0000250|UniProtKB:P60709, ECO:0000250|UniProtKB:P60710}. CC -!- MISCELLANEOUS: In vertebrates 3 main groups of actin isoforms, CC alpha, beta and gamma have been identified. The alpha actins are CC found in muscle tissues and are a major constituent of the CC contractile apparatus. The beta and gamma actins coexist in most CC cell types as components of the cytoskeleton and as mediators of CC internal cell 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 ProteinModelPortal; Q5R6G0; -. DR SMR; Q5R6G0; -. DR STRING; 9601.ENSPPYP00000019427; -. DR PRIDE; Q5R6G0; -. DR Ensembl; ENSPPYT00000020193; ENSPPYP00000019427; ENSPPYG00000017336. DR GeneID; 100173832; -. DR KEGG; pon:100173832; -. DR CTD; 60; -. DR eggNOG; KOG0676; Eukaryota. DR eggNOG; COG5277; LUCA. DR GeneTree; ENSGT00940000154122; -. DR HOVERGEN; HBG003771; -. DR InParanoid; Q5R6G0; -. DR KO; K05692; -. DR OMA; YKCDLDI; -. DR OrthoDB; 649708at2759; -. DR TreeFam; TF354237; -. DR Proteomes; UP000001595; Chromosome 7. DR GO; GO:0015629; C:actin cytoskeleton; ISS:UniProtKB. 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:0035267; C:NuA4 histone acetyltransferase complex; 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:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl. DR GO; GO:0005524; F:ATP binding; 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:0048870; P:cell motility; IEA:Ensembl. DR GO; GO:0072749; P:cellular response to cytochalasin B; IEA:Ensembl. DR GO; GO:0032091; P:negative regulation of protein binding; 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:0022898; P:regulation of transmembrane transporter activity; IEA:Ensembl. DR GO; GO:0048488; P:synaptic vesicle endocytosis; IEA:Ensembl. DR InterPro; IPR004000; Actin. DR InterPro; IPR020902; Actin/actin-like_CS. DR InterPro; IPR004001; Actin_CS. DR PANTHER; PTHR11937; PTHR11937; 1. DR Pfam; PF00022; Actin; 1. DR PRINTS; PR00190; ACTIN. DR SMART; SM00268; ACTIN; 1. 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; Complete proteome; Cytoplasm; Cytoskeleton; KW Methylation; Nucleotide-binding; Nucleus; Oxidation; KW Reference proteome; Ubl conjugation. FT CHAIN 1 375 Actin, cytoplasmic 1. FT /FTId=PRO_0000291871. FT INIT_MET 1 1 Removed; alternate. FT {ECO:0000250|UniProtKB:P60709}. FT CHAIN 2 375 Actin, cytoplasmic 1, N-terminally FT processed. FT /FTId=PRO_0000367079. FT MOD_RES 1 1 N-acetylmethionine. FT {ECO:0000250|UniProtKB:P60709}. FT MOD_RES 2 2 N-acetylaspartate; in Actin, cytoplasmic FT 1, N-terminally processed. FT {ECO:0000250|UniProtKB:P60709}. FT MOD_RES 44 44 Methionine (R)-sulfoxide. FT {ECO:0000250|UniProtKB:P60710}. FT MOD_RES 47 47 Methionine (R)-sulfoxide. FT {ECO:0000250|UniProtKB:P60710}. FT MOD_RES 73 73 Tele-methylhistidine. FT {ECO:0000250|UniProtKB:P60710}. FT MOD_RES 84 84 N6-methyllysine. FT {ECO:0000250|UniProtKB:P60709}. FT CONFLICT 288 288 D -> N (in Ref. 1; CAH93084). FT {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 //