ID   ACTB_RABIT              Reviewed;         375 AA.
AC   P29751;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   02-SEP-2026, entry version 154.
DE   RecName: Full=Actin, cytoplasmic 1;
DE   AltName: Full=Beta-actin;
DE            EC=3.6.4.- {ECO:0000250|UniProtKB:P68137};
DE   Contains:
DE     RecName: Full=Actin, cytoplasmic 1, N-terminally processed;
GN   Name=ACTB;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=New Zealand white; TISSUE=Uterus;
RX   PubMed=1555776; DOI=10.1016/0378-1119(92)90388-6;
RA   Harris D.E., Warshaw D.M., Periasamy M.;
RT   "Nucleotide sequences of the rabbit alpha-smooth-muscle and beta-non-muscle
RT   actin mRNAs.";
RL   Gene 112:265-266(1992).
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 (By similarity). Actin exists in both monomeric (G-actin) and
CC       polymeric (F-actin) forms, both forms playing key functions, such as
CC       cell motility and contraction (By similarity). In addition to their
CC       role in the cytoplasmic cytoskeleton, G- and F-actin also localize in
CC       the nucleus, and regulate gene transcription and motility and repair of
CC       damaged DNA (By similarity). Plays a role in the assembly of the gamma-
CC       tubulin ring complex (gTuRC), which regulates the minus-end nucleation
CC       of alpha-beta tubulin heterodimers that grow into microtubule
CC       protafilaments (By similarity). Part of the ACTR1A/ACTB filament around
CC       which the dynactin complex is built (By similarity). The dynactin
CC       multiprotein complex activates the molecular motor dynein for ultra-
CC       processive transport along microtubules (By similarity).
CC       {ECO:0000250|UniProtKB:P60709, ECO:0000250|UniProtKB:Q6QAQ1}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + phosphate + H(+); Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000250|UniProtKB:P68137};
CC   -!- SUBUNIT: Polymerization of globular actin (G-actin) leads to a
CC       structural filament (F-actin) in the form of a two-stranded helix (By
CC       similarity). Each actin can bind to 4 others (By similarity).
CC       Identified in a IGF2BP1-dependent mRNP granule complex containing
CC       untranslated mRNAs (By similarity). Component of the BAF complex, which
CC       includes at least actin (ACTB), ARID1A, ARID1B/BAF250, SMARCA2,
CC       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 (By similarity). In
CC       muscle cells, the BAF complex also contains DPF3 (By similarity). Found
CC       in a complex with XPO6, Ran, ACTB and PFN1 (By similarity). Interacts
CC       with PFN1 (By similarity). Interacts with XPO6 and EMD (By similarity).
CC       Interacts with ERBB2 (By similarity). Interacts with GCSAM (By
CC       similarity). Interacts with TBC1D21 (By similarity). 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 (By
CC       similarity). Interacts with FAM107A (By similarity). Associates with
CC       the gamma-tubulin ring complex (gTuRC) consisting of TUBGCP2, TUBGCP3,
CC       TUBGCP4, TUBGCP5 and TUBGCP6 and gamma-tubulin TUBG1 or TUBG2; within
CC       the complex, interacts with TUBGCP3 and TUBGCP6 to form a luminal
CC       bridge with MZT1 that stabilizes the initial structure during complex
CC       assembly (By similarity). Part of the ACTR1A/ACTB filament around which
CC       the dynactin complex is built (By similarity). The filament contains 8
CC       copies of ACTR1A and 1 ACTB (By similarity). Interacts with TPRN which
CC       forms ring-like structures in the stereocilium taper region; the
CC       interaction may stabilize stereocilia in inner ear hair cells (By
CC       similarity). Interacts with AMOTL2 (via N-terminus), the interaction
CC       facilitates binding of cell junction complexes to actin fibers in
CC       endothelial cells (By similarity). {ECO:0000250|UniProtKB:O18840,
CC       ECO:0000250|UniProtKB:P60709, ECO:0000250|UniProtKB:P60710,
CC       ECO:0000250|UniProtKB:Q6QAQ1}.
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: [Actin, cytoplasmic 1]: N-terminal cleavage of acetylated
CC       methionine of immature cytoplasmic actin by ACTMAP.
CC       {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; X60733; CAA43140.1; -; mRNA.
DR   PIR; JH0637; ATRBB.
DR   RefSeq; NP_001095153.1; NM_001101683.1.
DR   AlphaFoldDB; P29751; -.
DR   SMR; P29751; -.
DR   BioGRID; 1172293; 4.
DR   DIP; DIP-2197N; -.
DR   FunCoup; P29751; 946.
DR   IntAct; P29751; 5.
DR   MINT; P29751; -.
DR   GeneID; 100009272; -.
DR   KEGG; ocu:100009272; -.
DR   CTD; 60; -.
DR   InParanoid; P29751; -.
DR   OrthoDB; 9546537at2759; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0015629; C:actin cytoskeleton; ISS:UniProtKB.
DR   GO; GO:0005856; C:cytoskeleton; ISS:AgBase.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
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:0016887; F:ATP hydrolysis activity; ISS:UniProtKB.
DR   CDD; cd10224; ASKHA_NBD_actin; 1.
DR   FunFam; 3.30.420.40:FF:000131; Actin, alpha skeletal muscle; 1.
DR   FunFam; 3.30.420.40:FF:000291; Actin, alpha skeletal muscle; 1.
DR   FunFam; 3.90.640.10:FF:000047; Actin, alpha skeletal muscle; 1.
DR   FunFam; 3.30.420.40:FF:000058; Putative actin-related protein 5; 1.
DR   Gene3D; 3.30.420.40; -; 2.
DR   Gene3D; 3.90.640.10; Actin, Chain A, domain 4; 1.
DR   InterPro; IPR004000; Actin.
DR   InterPro; IPR020902; Actin/actin-like_CS.
DR   InterPro; IPR004001; Actin_CS.
DR   InterPro; IPR043129; ATPase_NBD.
DR   PANTHER; PTHR11937; ACTIN; 1.
DR   Pfam; PF00022; Actin; 1.
DR   PRINTS; PR00190; ACTIN.
DR   SMART; SM00268; ACTIN; 1.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 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; Hydrolase; Methylation;
KW   Nucleotide-binding; Nucleus; Oxidation; Reference proteome;
KW   Ubl conjugation.
FT   CHAIN           1..375
FT                   /note="Actin, cytoplasmic 1"
FT                   /id="PRO_0000000779"
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_0000367080"
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;  41756 MW;  CB1D01AFBF036B99 CRC64;
     MDDDIAALVV DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS
     KRGILTLKYP IEHGIVTNWD DMEKIWHHTF YNELRVAPEE RPVLLTEAPL 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
//