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 07-SEP-2016, entry version 82. 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: Actins are highly conserved proteins that are involved CC in various types of cell motility and are ubiquitously expressed CC in all eukaryotic cells. {ECO:0000250}. 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. Component CC of the MLL5-L complex, at least composed of KMT2E/MLL5, STK38, CC PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT. Interacts with XPO6 CC and EMD. Interacts with ERBB2. Interacts with GCSAM. Interacts CC with CPNE1 (via VWFA domain) and CPNE4 (via VWFA domain) (By CC similarity). Interacts with TBC1D21. {ECO:0000250, CC ECO:0000250|UniProtKB:P60710}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Note=Localized in CC cytoplasmic mRNP granules containing untranslated mRNAs. CC {ECO:0000250}. CC -!- PTM: ISGylated. {ECO:0000250}. 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 (By similarity). {ECO:0000250}. 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 (By similarity). {ECO:0000250}. 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 (By similarity). {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; CR860530; CAH92656.1; -; mRNA. DR EMBL; CR860982; CAH93084.1; -; mRNA. DR RefSeq; NP_001126826.1; NM_001133354.1. DR ProteinModelPortal; Q5R6G0; -. DR SMR; Q5R6G0; 6-375. 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; ENSGT00760000118957; -. DR HOVERGEN; HBG003771; -. DR InParanoid; Q5R6G0; -. DR KO; K05692; -. DR OMA; PFHTTAE; -. DR OrthoDB; EOG091G08LD; -. DR TreeFam; TF354237; -. DR Proteomes; UP000001595; Chromosome 7. DR GO; GO:0072562; C:blood microparticle; 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:0070062; C:extracellular exosome; IEA:Ensembl. DR GO; GO:0005925; C:focal adhesion; ISS:AgBase. DR GO; GO:0070688; C:MLL5-L complex; IEA:Ensembl. DR GO; GO:0043209; C:myelin sheath; IEA:Ensembl. DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IEA:Ensembl. DR GO; GO:0000790; C:nuclear chromatin; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; ISS:AgBase. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IEA:Ensembl. DR GO; GO:0000980; F:RNA polymerase II distal enhancer sequence-specific DNA binding; IEA:Ensembl. DR GO; GO:0043044; P:ATP-dependent chromatin remodeling; IEA:Ensembl. DR GO; GO:0070527; P:platelet aggregation; IEA:Ensembl. DR GO; GO:0001895; P:retina homeostasis; IEA:Ensembl. DR GO; GO:0021762; P:substantia nigra development; 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; Oxidation; Reference proteome; KW Ubl conjugation. FT CHAIN 1 375 Actin, cytoplasmic 1. FT /FTId=PRO_0000367079. 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_0000291871. 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. {ECO:0000250}. FT MOD_RES 47 47 Methionine (R)-sulfoxide. {ECO:0000250}. 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 //