ID   ACTG_XENLA              Reviewed;         375 AA.
AC   A2BDB0;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 54.
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;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (DEC-2002) 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.
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: 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; BC130155; AAI30156.1; -; mRNA.
DR   RefSeq; NP_001091279.1; NM_001097810.1.
DR   AlphaFoldDB; A2BDB0; -.
DR   SMR; A2BDB0; -.
DR   PRIDE; A2BDB0; -.
DR   Proteomes; UP000186698; Genome assembly.
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; Reference proteome.
FT   CHAIN           1..375
FT                   /note="Actin, cytoplasmic 2"
FT                   /id="PRO_0000367108"
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_0000280383"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine; in Actin, cytoplasmic 2;
FT                   alternate"
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:P63260"
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