ID   ACTB_CTEID              Reviewed;         375 AA.
AC   P83751; O73815; P12714;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-FEB-2004, sequence version 1.
DT   25-MAY-2022, entry version 67.
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   Ctenopharyngodon idella (Grass carp) (Leuciscus idella).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Xenocyprididae; Xenocypridinae; Ctenopharyngodon.
OX   NCBI_TaxID=7959;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2762162; DOI=10.1093/nar/17.14.5850;
RA   Liu Z.J., Zhu Z.Y., Roberg K., Faras A.F., Guise K.S., Kapuscinski A.R.,
RA   Hackett P.B.;
RT   "The beta-actin gene of carp (Ctenopharyngodon idella).";
RL   Nucleic Acids Res. 17:5850-5850(1989).
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 (By
CC       similarity). Each actin can bind to 4 others (By similarity).
CC       {ECO:0000250|UniProtKB:P60709, ECO:0000250|UniProtKB:P60710}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:P60710}. Nucleus {ECO:0000250|UniProtKB:O93400}.
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: Methylation at His-73 by SETD3. Methylation stabilizes actin
CC       filaments. {ECO:0000250|UniProtKB:P60706}.
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:O93400}.
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; M25013; AAA49197.1; -; Genomic_DNA.
DR   PIR; S05430; S05430.
DR   AlphaFoldDB; P83751; -.
DR   SMR; P83751; -.
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: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.
FT   CHAIN           1..375
FT                   /note="Actin, cytoplasmic 1"
FT                   /id="PRO_0000367089"
FT   INIT_MET        1
FT                   /note="Removed; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P60706"
FT   CHAIN           2..375
FT                   /note="Actin, cytoplasmic 1, N-terminally processed"
FT                   /id="PRO_0000000799"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine; in Actin, cytoplasmic 1;
FT                   alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P60706"
FT   MOD_RES         2
FT                   /note="N-acetylaspartate; in Actin, cytoplasmic 1, N-
FT                   terminally processed"
FT                   /evidence="ECO:0000250|UniProtKB:P60706"
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"
SQ   SEQUENCE   375 AA;  41753 MW;  6DE990BC0FBD0D19 CRC64;
     MDDEIAALVV DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS
     KRGILTLKYP IEHGIVTNWD DMEKIWHHTF YNELRVAPEE HPVLLTEAPL NPKANREKMT
     QIMFETFNTP AMYVAIQAVL SLYASGRTTG IVMDSGDGVT HTVPIYEGYA LPHAILRLDL
     AGRDLTDYLM KILTERGYSF TTTAEREIVR DIKEKLCYVA LDFEQEMGTA ASSSSLEKSY
     ELPDGQVITI GNERFRCPEA LFQPSFLGME SCGIHETTFN SIMKCDVDIR KDLYANTVLS
     GGTTMYPGIA DRMQKEITSL APSTMKIKII APPERKYSVW IGGSILASLS TFQQMWISKQ
     EYDESGPSIV HRKCF