ACTB_CHLPG
ID ACTB_CHLPG Reviewed; 361 AA.
AC P84856;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 25-MAY-2022, entry version 64.
DE RecName: Full=Actin, cytoplasmic 1;
DE AltName: Full=Beta-actin;
GN Name=ACTB;
OS Chlorocebus pygerythrus (Vervet monkey) (Cercopithecus pygerythrus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Chlorocebus.
OX NCBI_TaxID=60710;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, AND MASS SPECTROMETRY.
RC TISSUE=Kidney epithelium {ECO:0000269|Ref.1};
RA Seema Z., Jain S.K.;
RT "Molecular biology of dengue; characterization of cellular receptors.";
RL Submitted (APR-2006) to UniProtKB.
CC -!- FUNCTION: Actin is a highly conserved protein that polymerizes to
CC produce filaments that form cross-linked networks in the cytoplasm of
CC cells. Actin exists in both monomeric (G-actin) and polymeric (F-actin)
CC forms, both forms playing key functions, such as cell motility and
CC contraction. In addition to their role in the cytoplasmic cytoskeleton,
CC G- and F-actin also localize in the nucleus, and regulate gene
CC transcription and motility and repair of damaged DNA.
CC {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. Each
CC actin can bind to 4 others. Identified in a IGF2BP1-dependent mRNP
CC granule complex containing untranslated mRNAs. Component of the BAF
CC complex, 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 of
CC SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C. In muscle cells, the
CC BAF complex also contains DPF3. Found in a complex with XPO6, Ran, ACTB
CC and PFN1. Interacts with XPO6 and EMD. Interacts with ERBB2. Interacts
CC with GCSAM (By similarity). Interacts with TBC1D21. Interacts with
CC CPNE1 (via VWFA domain) and CPNE4 (via VWFA domain) (By similarity).
CC Interacts with DHX9 (via C-terminus); this interaction is direct and
CC mediates the attachment to nuclear ribonucleoprotein complexes.
CC Interacts with FAM107A (By similarity). {ECO:0000250|UniProtKB:P60709,
CC ECO:0000250|UniProtKB:P60710}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P60709}. Nucleus {ECO:0000250|UniProtKB:P60709}.
CC Note=Localized in cytoplasmic mRNP granules containing untranslated
CC mRNAs. {ECO:0000250|UniProtKB:P60709}.
CC -!- PTM: ISGylated. {ECO:0000250|UniProtKB:P60709}.
CC -!- PTM: Oxidation of Met-29 and Met-32 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. The
CC (R)-S-oxide form is reverted by MSRB1 and MSRB2, which promote actin
CC repolymerization. {ECO:0000250|UniProtKB:P60710}.
CC -!- PTM: Monomethylation at Lys-69 (K84me1) regulates actin-myosin
CC interaction and actomyosin-dependent processes. Demethylation by ALKBH4
CC is required for maintaining actomyosin dynamics supporting normal
CC cleavage furrow ingression during cytokinesis and cell migration.
CC {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-58 by SETD3 (By similarity). Methylation at His-
CC 73 is required for smooth muscle contraction of the laboring uterus
CC during delivery (By similarity). {ECO:0000250|UniProtKB:P60709,
CC ECO:0000250|UniProtKB:P60710}.
CC -!- MASS SPECTROMETRY: Mass=40536; Mass_error=80; Method=MALDI;
CC Evidence={ECO:0000269|Ref.1};
CC -!- MISCELLANEOUS: In vertebrates 3 main groups of actin isoforms, alpha,
CC beta and gamma have been identified. The alpha actins are found in
CC muscle tissues and are a major constituent of the contractile
CC apparatus. The beta and gamma actins coexist in most cell types as
CC components of the cytoskeleton and as mediators of internal cell
CC motility. {ECO:0000250|UniProtKB:P60709}.
CC -!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
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DR AlphaFoldDB; P84856; -.
DR SMR; P84856; -.
DR PRIDE; P84856; -.
DR GO; GO:0015629; C:actin cytoskeleton; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR InterPro; IPR004000; Actin.
DR InterPro; IPR004001; Actin_CS.
DR InterPro; IPR043129; ATPase_NBD.
DR PANTHER; PTHR11937; PTHR11937; 1.
DR Pfam; PF00022; Actin; 1.
DR PRINTS; PR00190; ACTIN.
DR SMART; SM00268; ACTIN; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS00406; ACTINS_1; 1.
DR PROSITE; PS00432; ACTINS_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW Methylation; Nucleotide-binding; Nucleus; Oxidation; Ubl conjugation.
FT CHAIN 1..361
FT /note="Actin, cytoplasmic 1"
FT /id="PRO_0000238617"
FT MOD_RES 29
FT /note="Methionine (R)-sulfoxide"
FT /evidence="ECO:0000250|UniProtKB:P60710"
FT MOD_RES 32
FT /note="Methionine (R)-sulfoxide"
FT /evidence="ECO:0000250|UniProtKB:P60710"
FT MOD_RES 58
FT /note="Tele-methylhistidine"
FT /evidence="ECO:0000250|UniProtKB:P60710"
FT MOD_RES 69
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:P60709"
SQ SEQUENCE 361 AA; 40445 MW; D77D52C9413DB744 CRC64;
MCKAGFAGDD APRAVFPSIV GRPRHQGVMV GMGQKDSYVG DEAQSKRGIL TLKYPIEHGI
VYNWDDMEKI WHHTFYNELR VAPEEHPVLL TEAPLNPKAN LEKMTQIMFE TFNTPAMYVA
IQAVLSLYAS GRTTGIVMDS GDGVTHTVPI YEGYALPHAI LRLDLAGRDL TDYLMKILTE
RYGYSFTTTA EREIVRDIKE KLCYVALDFE QEMATAASSS SLEKSYELPD GQVITIGNER
FRCPEALFQP SFLGMESCGI HETTFNSIMK CDVDIRKDLY ANTVLSGGTT MYPGIADRMQ
KEITALAPST MKIKIIAPPE RKYSVWIGGS ILASLSTFQQ MWISKQEYDE SGPSIVHRKC
F
