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 26-JUN-2013, entry version 62. 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 (By similarity). 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 mRNP granule CC complex, at least composed of ACTB, ACTN4, DHX9, ERG, HNRNPA1, CC HNRNPA2B1, HNRNPAB, HNRNPD, HNRNPL, HNRNPR, HNRNPU, HSPA1, HSPA8, CC IGF2BP1, ILF2, ILF3, NCBP1, NCL, PABPC1, PABPC4, PABPN1, RPLP0, CC RPS3, RPS3A, RPS4X, RPS8, RPS9, SYNCRIP, TROVE2, YBX1 and CC untranslated mRNAs. Component of the BAF complex, which includes CC at least actin (ACTB), ARID1A, ARID1B/BAF250, SMARCA2, CC SMARCA4/BRG1, ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57, CC SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1, and one or more CC of SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C. In muscle CC cells, the BAF complex also contains DPF3. Found in a complex with CC XPO6, Ran, ACTB and PFN1. Component of the MLL5-L complex, at CC least composed of MLL5, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB CC and OGT. Interacts with XPO6 and EMD. Interacts with ERBB2 (By CC similarity). Interacts with GCSAM (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Note=Localized in CC cytoplasmic mRNP granules containing untranslated mRNAs (By CC similarity). CC -!- PTM: ISGylated (By similarity). CC -!- PTM: Oxidation of Met-44 by MICALs (MICAL1, MICAL2 or MICAL3) to CC form methionine sulfoxide promotes actin filament CC depolymerization. Methionine sulfoxide is produced CC stereospecifically, but it is not known whether the (S)-S-oxide or CC the (R)-S-oxide is produced (By similarity). 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). CC -!- SIMILARITY: Belongs to the actin family. 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 PRIDE; Q5R6G0; -. DR Ensembl; ENSPPYT00000020193; ENSPPYP00000019427; ENSPPYG00000017336. DR GeneID; 100173832; -. DR KEGG; pon:100173832; -. DR CTD; 60; -. DR GeneTree; ENSGT00690000101979; -. DR HOVERGEN; HBG003771; -. DR InParanoid; Q5R6G0; -. DR KO; K05692; -. DR OMA; IKNLMER; -. DR GO; GO:0030863; C:cortical cytoskeleton; IEA:Compara. DR GO; GO:0005829; C:cytosol; IEA:Compara. DR GO; GO:0070062; C:extracellular vesicular exosome; IEA:Compara. DR GO; GO:0070688; C:MLL5-L complex; IEA:Compara. DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IEA:Compara. DR GO; GO:0030529; C:ribonucleoprotein complex; IEA:Compara. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR InterPro; IPR004000; Actin-related. 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 (By similarity). FT CHAIN 2 375 Actin, cytoplasmic 1, N-terminally FT processed. FT /FTId=PRO_0000291871. FT MOD_RES 1 1 N-acetylmethionine (By similarity). FT MOD_RES 2 2 N-acetylaspartate; in Actin, cytoplasmic FT 1, N-terminally processed (By FT similarity). FT MOD_RES 44 44 Methionine sulfoxide (By similarity). FT MOD_RES 73 73 Tele-methylhistidine (By similarity). FT CONFLICT 288 288 D -> N (in Ref. 1; CAH93084). 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 //