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 22-JUL-2008, entry version 22. DE RecName: Full=Actin, cytoplasmic 1; DE AltName: Full=Beta-actin; 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. Found in a complex with XPO6, CC Ran, ACTB and PFN1. Component of a complex composed at least of CC ACTB, AP2M1, AP2A1, AP2A2, MEGF10 and VIM. Interacts with XPO6 (By CC 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 SMR; Q5R6G0; 4-371. DR HOVERGEN; Q5R6G0; -. DR InterPro; IPR004001; Actin_CS. DR InterPro; IPR004000; Actin_like. 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; Structural protein. FT PROPEP 1 1 Removed in mature form (By similarity). FT /FTId=PRO_0000291870. FT CHAIN 2 375 Actin, cytoplasmic 1. FT /FTId=PRO_0000291871. FT MOD_RES 1 1 N-acetylmethionine (By similarity). FT MOD_RES 2 2 N-acetylaspartate (By similarity). FT MOD_RES 73 73 Tele-methylhistidine (By similarity). FT MOD_RES 166 166 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 //