ID   ACTG_TRIVU              Reviewed;         375 AA.
AC   P63257; P02571; P14104; P99022;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Actin, cytoplasmic 2;
DE   AltName: Full=Gamma-actin;
DE   Contains:
DE     RecName: Full=Actin, cytoplasmic 2, N-terminally processed;
GN   Name=ACTG1; Synonyms=ACTG;
OS   Trichosurus vulpecula (Brush-tailed possum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Diprotodontia; Phalangeridae; Trichosurus.
OX   NCBI_TaxID=9337;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Wedlock D.N., Hickson R., Buddle B.M.;
RT   "Isolation of the complete gamma-actin cDNA from the common brushtail
RT   possum.";
RL   Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Actins are highly conserved proteins that are involved in
CC       various types of cell motility and are ubiquitously expressed in all
CC       eukaryotic cells. {ECO:0000250|UniProtKB:P63261}.
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. Interacts with TWF1, CAPZB, cofilin and
CC       profilin. {ECO:0000250|UniProtKB:P63261}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:P63261}.
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:P63260}.
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:P63261}.
CC   -!- PTM: [Actin, cytoplasmic 2, 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:P63261}.
CC   -!- PTM: Methylated at His-73 by SETD3. {ECO:0000250|UniProtKB:P63261}.
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.
CC   -!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
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DR   EMBL; AF076191; AAC26520.1; -; mRNA.
DR   AlphaFoldDB; P63257; -.
DR   SMR; P63257; -.
DR   PRIDE; P63257; -.
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: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; Oxidation.
FT   CHAIN           1..375
FT                   /note="Actin, cytoplasmic 2"
FT                   /id="PRO_0000000837"
FT   INIT_MET        1
FT                   /note="Removed; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P63261"
FT   CHAIN           2..375
FT                   /note="Actin, cytoplasmic 2, N-terminally processed"
FT                   /id="PRO_0000367103"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:P63261"
FT   MOD_RES         2
FT                   /note="N-acetylglutamate; in Actin, cytoplasmic 2, N-
FT                   terminally processed"
FT                   /evidence="ECO:0000250|UniProtKB:P63261"
FT   MOD_RES         44
FT                   /note="Methionine (R)-sulfoxide"
FT                   /evidence="ECO:0000250|UniProtKB:P63260"
FT   MOD_RES         47
FT                   /note="Methionine (R)-sulfoxide"
FT                   /evidence="ECO:0000250|UniProtKB:P63260"
FT   MOD_RES         73
FT                   /note="Tele-methylhistidine"
FT                   /evidence="ECO:0000250|UniProtKB:P63258"
FT   MOD_RES         84
FT                   /note="N6-methyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P63261"
SQ   SEQUENCE   375 AA;  41793 MW;  54D08F986964EFD5 CRC64;
     MEEEIAALVI 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 TFQQMWISKQ
     EYDESGPSIV HRKCF