ID   ACTB_SIGHI              Reviewed;         375 AA.
AC   Q91ZK5;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 92.
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   Sigmodon hispidus (Hispid cotton rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Sigmodontinae; Sigmodon.
OX   NCBI_TaxID=42415;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Pletneva L.M., Harrast T.D., Langley R.J., Blanco J.C., Prince G.A.;
RT   "Sigmodon hispidus beta actin mRNA.";
RL   Submitted (SEP-2001) 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}.
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; AF421789; AAL16942.1; -; mRNA.
DR   AlphaFoldDB; Q91ZK5; -.
DR   SMR; Q91ZK5; -.
DR   PRIDE; Q91ZK5; -.
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   2: Evidence at transcript level;
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_0000000785"
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_0000367083"
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;  41719 MW;  DEF814DE94E36624 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
     GGTTIYPGIA DRMQKEITAL APSTMKIKII APPERKYSVW IGGSILASLS TFQQMWISKQ
     EYDESGPSIV HRKCF