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-JUL-2009, entry version 30. 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). 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. Component of the BAF complex, CC 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 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 (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (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; -. DR UniGene; Pab.18012; -. DR SMR; Q5R6G0; 4-371. DR PRIDE; Q5R6G0; -. DR GeneID; 100173832; -. DR HOVERGEN; Q5R6G0; -. DR OMA; Q5R6G0; ADSEDIQ. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005515; F:protein binding; IEA:InterPro. DR InterPro; IPR004000; Actin-like. DR InterPro; IPR004001; Actin_CS. DR PANTHER; PTHR11937; Actin_like; 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; Cytoplasm; Cytoskeleton; Methylation; KW Nucleotide-binding; Phosphoprotein. 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; in Actin, cytoplasmic FT 1; alternate (By similarity). FT MOD_RES 2 2 N-acetylaspartate; in Actin, cytoplasmic FT 1, N-terminally processed (By FT similarity). FT MOD_RES 53 53 Phosphotyrosine (By similarity). FT MOD_RES 73 73 Tele-methylhistidine (By similarity). FT MOD_RES 91 91 Phosphotyrosine (By similarity). FT MOD_RES 166 166 Phosphotyrosine (By similarity). FT MOD_RES 198 198 Phosphotyrosine (By similarity). FT MOD_RES 218 218 Phosphotyrosine (By similarity). FT MOD_RES 294 294 Phosphotyrosine (By similarity). FT MOD_RES 318 318 Phosphothreonine (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 //