ID   ACTH_MOUSE              Reviewed;         376 AA.
AC   P63268; P12718;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   04-NOV-2026, entry version 155.
DE   RecName: Full=Actin, gamma-enteric smooth muscle;
DE            EC=3.6.4.- {ECO:0000250|UniProtKB:P68137};
DE   AltName: Full=Alpha-actin-3;
DE   AltName: Full=Gamma-2-actin;
DE   AltName: Full=Smooth muscle gamma-actin;
DE   Contains:
DE     RecName: Full=Actin, gamma-enteric smooth muscle, intermediate form;
DE   Flags: Precursor;
GN   Name=Actg2; Synonyms=Acta3, Actsg;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2747639; DOI=10.1128/mcb.9.5.1875-1881.1989;
RA   Kim E., Waters S.H., Hake L.E., Hecht N.B.;
RT   "Identification and developmental expression of a smooth-muscle gamma-actin
RT   in postmeiotic male germ cells of mice.";
RL   Mol. Cell. Biol. 9:1875-1881(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   OXIDATION AT MET-45 AND MET-48, AND DEOXIDATION AT MET-45 AND MET-48.
RX   PubMed=23911929; DOI=10.1016/j.molcel.2013.06.019;
RA   Lee B.C., Peterfi Z., Hoffmann F.W., Moore R.E., Kaya A., Avanesov A.,
RA   Tarrago L., Zhou Y., Weerapana E., Fomenko D.E., Hoffmann P.R.,
RA   Gladyshev V.N.;
RT   "MsrB1 and MICALs regulate actin assembly and macrophage function via
RT   reversible stereoselective methionine oxidation.";
RL   Mol. Cell 51:397-404(2013).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=24337657; DOI=10.1007/s00439-013-1406-0;
RA   Thorson W., Diaz-Horta O., Foster J. II, Spiliopoulos M., Quintero R.,
RA   Farooq A., Blanton S., Tekin M.;
RT   "De novo ACTG2 mutations cause congenital distended bladder, microcolon,
RT   and intestinal hypoperistalsis.";
RL   Hum. Genet. 133:737-742(2014).
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.
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. Each
CC       actin can bind to 4 others.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC   -!- TISSUE SPECIFICITY: Expressed in tissues containing smooth muscle
CC       particularly the intestines and bladder. {ECO:0000269|PubMed:24337657}.
CC   -!- PTM: Oxidation of Met-45 and Met-48 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 promotes actin
CC       repolymerization. {ECO:0000269|PubMed:23911929}.
CC   -!- PTM: Monomethylation at Lys-85 (K85me1) 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:P68134}.
CC   -!- PTM: Methylated at His-74 by SETD3. {ECO:0000250|UniProtKB:P63267}.
CC   -!- PTM: [Actin, gamma-enteric smooth muscle, intermediate form]: N-
CC       terminal cleavage of acetylated cysteine of intermediate muscle actin
CC       by ACTMAP. {ECO:0000250|UniProtKB:P62737}.
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; M26689; AAA56841.1; -; mRNA.
DR   EMBL; BC002042; AAH02042.1; -; mRNA.
DR   CCDS; CCDS51822.1; -.
DR   PIR; A32788; A32788.
DR   RefSeq; NP_033740.2; NM_009610.2.
DR   AlphaFoldDB; P63268; -.
DR   SMR; P63268; -.
DR   BioGRID; 197947; 4.
DR   FunCoup; P63268; 150.
DR   IntAct; P63268; 1.
DR   STRING; 10090.ENSMUSP00000074658; -.
DR   GlyGen; P63268; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P63268; -.
DR   PhosphoSitePlus; P63268; -.
DR   SwissPalm; P63268; -.
DR   jPOST; P63268; -.
DR   PaxDb; 10090-ENSMUSP00000074658; -.
DR   PeptideAtlas; P63268; -.
DR   ProteomicsDB; 285855; -.
DR   Pumba; P63268; -.
DR   Antibodypedia; 3526; 349 antibodies from 36 providers.
DR   DNASU; 11468; -.
DR   Ensembl; ENSMPUT00000007827; ENSMPUP00000007704; ENSMPUG00000007760.
DR   Ensembl; ENSMUST00000075161.12; ENSMUSP00000074658.6; ENSMUSG00000059430.15.
DR   Ensembl; ENSMUST00000121731.8; ENSMUSP00000113552.2; ENSMUSG00000059430.15.
DR   GeneID; 11468; -.
DR   KEGG; mmu:11468; -.
DR   UCSC; uc009cnr.1; mouse.
DR   AGR; MGI:104589; -.
DR   CTD; 72; -.
DR   MGI; MGI:104589; Actg2.
DR   VEuPathDB; HostDB:ENSMUSG00000059430; -.
DR   eggNOG; KOG0676; Eukaryota.
DR   GeneTree; ENSGT00940000154148; -.
DR   InParanoid; P63268; -.
DR   OMA; AACGSWI; -.
DR   OrthoDB; 9545632at2759; -.
DR   PhylomeDB; P63268; -.
DR   Reactome; R-MMU-445355; Smooth Muscle Contraction.
DR   Reactome; R-MMU-9764561; Regulation of CDH1 Function.
DR   Reactome; R-MMU-9913351; Formation of the dystrophin-glycoprotein complex (DGC).
DR   Reactome; R-MMU-9958825; Activation of STAT3 by cadherin engagement.
DR   BioGRID-ORCS; 11468; 6 hits in 78 CRISPR screens.
DR   CD-CODE; 8BEB9125; Cajal body.
DR   PRO; PR:P63268; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; P63268; protein.
DR   Bgee; ENSMUSG00000059430; Expressed in umbilical cord and 161 other cell types or tissues.
DR   ExpressionAtlas; P63268; baseline and differential.
DR   GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR   GO; GO:0044297; C:cell body; ISS:AgBase.
DR   GO; GO:0071944; C:cell periphery; IDA:MGI.
DR   GO; GO:0005737; C:cytoplasm; ISS:AgBase.
DR   GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR   GO; GO:0030175; C:filopodium; ISS:AgBase.
DR   GO; GO:0030027; C:lamellipodium; ISS:AgBase.
DR   GO; GO:0032982; C:myosin filament; ISS:AgBase.
DR   GO; GO:0016887; F:ATP hydrolysis activity; ISS:UniProtKB.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
DR   GO; GO:1905641; P:cellular response to acetaldehyde; IEA:Ensembl.
DR   GO; GO:0071354; P:cellular response to interleukin-6; IEA:Ensembl.
DR   GO; GO:0090131; P:mesenchyme migration; ISS:AgBase.
DR   GO; GO:0010628; P:positive regulation of gene expression; ISS:AgBase.
DR   GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR   CDD; cd10224; ASKHA_NBD_actin; 1.
DR   FunFam; 3.30.420.40:FF:000218; actin, alpha sarcomeric/skeletal-like; 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   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Cytoplasm; Cytoskeleton; Hydrolase; Methylation;
KW   Muscle protein; Nucleotide-binding; Oxidation; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..376
FT                   /note="Actin, gamma-enteric smooth muscle, intermediate
FT                   form"
FT                   /evidence="ECO:0000250|UniProtKB:P62737"
FT                   /id="PRO_0000442951"
FT   CHAIN           3..376
FT                   /note="Actin, gamma-enteric smooth muscle"
FT                   /evidence="ECO:0000250|UniProtKB:P63267"
FT                   /id="PRO_0000442952"
FT   MOD_RES         2
FT                   /note="N-acetylcysteine; in intermediate form"
FT                   /evidence="ECO:0000250|UniProtKB:P62737"
FT   MOD_RES         45
FT                   /note="Methionine (R)-sulfoxide"
FT                   /evidence="ECO:0000269|PubMed:23911929"
FT   MOD_RES         48
FT                   /note="Methionine (R)-sulfoxide"
FT                   /evidence="ECO:0000269|PubMed:23911929"
FT   MOD_RES         74
FT                   /note="Tele-methylhistidine"
FT                   /evidence="ECO:0000250|UniProtKB:P63267"
SQ   SEQUENCE   376 AA;  41877 MW;  6EC08CD5EEAD445E CRC64;
     MCEEETTALV CDNGSGLCKA GFAGDDAPRA VFPSIVGRPR HQGVMVGMGQ KDSYVGDEAQ
     SKRGILTLKY PIEHGIITNW DDMEKIWHHS FYNELRVAPE EHPTLLTEAP LNPKANREKM
     TQIMFETFNV PAMYVAIQAV LSLYASGRTT GIVLDSGDGV THNVPIYEGY ALPHAIMRLD
     LAGRDLTDYL MKILTERGYS FVTTAEREIV RDIKEKLCYV ALDFENEMAT AASSSSLEKS
     YELPDGQVIT IGNERFRCPE TLFQPSFIGM ESAGIHETTY NSIMKCDIDI RKDLYANNVL
     SGGTTMYPGI ADRMQKEITA LAPSTMKIKI IAPPERKYSV WIGGSILASL STFQQMWISK
     PEYDEAGPSI VHRKCF
//