ID   ACTB_OREMO              Reviewed;         375 AA.
AC   P68143; P53484;
DT   25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 63.
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   Oreochromis mossambicus (Mozambique tilapia) (Tilapia mossambica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX   NCBI_TaxID=8127;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Gill;
RA   Takeuchi K.;
RT   "Cloning of Tilapia actin cDNAs.";
RL   Submitted (JAN-2000) 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 (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}.
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DR   EMBL; AB037865; BAA90688.1; -; mRNA.
DR   AlphaFoldDB; P68143; -.
DR   SMR; P68143; -.
DR   PRIDE; P68143; -.
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   2: Evidence at transcript level;
KW   Acetylation; ATP-binding; Cytoplasm; Cytoskeleton; Methylation;
KW   Nucleotide-binding; Nucleus; Oxidation.
FT   CHAIN           1..375
FT                   /note="Actin, cytoplasmic 1"
FT                   /id="PRO_0000367091"
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_0000000803"
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-acetylglutamate; 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;  41767 MW;  9C505616D33E9495 CRC64;
     MEDEIAALVV 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 SCGIHETTYN SIMKCDVDIR KDLYANTVLS
     GGTTMYPGIA DRMQKEITAL APSTMKIKII APPERKYSVW IGGSILASLS TFQQMWISKQ
     EYDESGPSIV HRKCF