ACTB_CRIGR
ID ACTB_CRIGR Reviewed; 375 AA.
AC P48975;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 25-MAY-2022, entry version 107.
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 Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Staehlbom P.-A., Franzen S.A.;
RT "Isolation and characterization of the beta-actin gene from Chinese
RT hamster.";
RL Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases.
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-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. 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-84 (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-73 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 -!- 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 EMBL; U20114; AAA64871.1; -; Genomic_DNA.
DR RefSeq; NP_001231504.1; NM_001244575.1.
DR AlphaFoldDB; P48975; -.
DR SMR; P48975; -.
DR STRING; 10029.NP_001231504.1; -.
DR GeneID; 100689477; -.
DR KEGG; cge:100689477; -.
DR CTD; 60; -.
DR eggNOG; KOG0676; Eukaryota.
DR OrthoDB; 649708at2759; -.
DR GO; GO:0015629; C:actin cytoskeleton; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; ISS:AgBase.
DR GO; GO:0097433; C:dense body; ISS:AgBase.
DR GO; GO:0005925; C:focal adhesion; ISS:AgBase.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:AgBase.
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; IPR020902; Actin/actin-like_CS.
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.
DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE 3: Inferred from homology;
KW Acetylation; ATP-binding; Cytoplasm; Cytoskeleton; Methylation;
KW Nucleotide-binding; Nucleus; Oxidation; Ubl conjugation.
FT CHAIN 1..375
FT /note="Actin, cytoplasmic 1"
FT /id="PRO_0000000767"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000250|UniProtKB:P60709"
FT CHAIN 2..375
FT /note="Actin, cytoplasmic 1, N-terminally processed"
FT /id="PRO_0000367071"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P60709"
FT MOD_RES 2
FT /note="N-acetylaspartate; in Actin, cytoplasmic 1, N-
FT terminally processed"
FT /evidence="ECO:0000250|UniProtKB:P60709"
FT MOD_RES 44
FT /note="Methionine (R)-sulfoxide"
FT /evidence="ECO:0000250|UniProtKB:P60710"
FT MOD_RES 47
FT /note="Methionine (R)-sulfoxide"
FT /evidence="ECO:0000250|UniProtKB:P60710"
FT MOD_RES 73
FT /note="Tele-methylhistidine"
FT /evidence="ECO:0000250|UniProtKB:P60710"
FT MOD_RES 84
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:P60709"
SQ SEQUENCE 375 AA; 41738 MW; 6AFD05CA94F9BA22 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 TFQEMWISKQ
EYDESGPSIV HRKCF
