ACTS_MOUSE
ID ACTS_MOUSE Reviewed; 377 AA.
AC P68134; P02568; P99020;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Actin, alpha skeletal muscle;
DE AltName: Full=Alpha-actin-1;
DE Contains:
DE RecName: Full=Actin, alpha skeletal muscle, intermediate form;
DE Flags: Precursor;
GN Name=Acta1; Synonyms=Acta;
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=3013550; DOI=10.1089/dna.1986.5.235;
RA Leader D.P., Gall I., Campbell P.C., Frischauf A.-M.;
RT "Isolation and characterization of cDNA clones from mouse skeletal muscle
RT actin mRNA.";
RL DNA 5:235-238(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3023820; DOI=10.1128/mcb.6.1.15-25.1986;
RA Hu M.C.-T., Sharp S.B., Davidson N.;
RT "The complete sequence of the mouse skeletal alpha-actin gene reveals
RT several conserved and inverted repeat sequences outside of the protein-
RT coding region.";
RL Mol. Cell. Biol. 6:15-25(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC 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 [4]
RP OXIDATION AT MET-46 AND MET-49, AND DEOXIDATION AT MET-46 AND MET-49.
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).
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 -!- 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 (By similarity). Interacts with alpha-
CC actinin. Identified in a complex composed of ACTA1, COBL, GSN AND
CC TMSB4X (By similarity). Interacts with TTID. Interacts (via its C-
CC terminus) with USP25 (By similarity). {ECO:0000250|UniProtKB:P68133,
CC ECO:0000250|UniProtKB:P68135}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- PTM: Oxidation of Met-46 and Met-49 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-86 (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:P68133}.
CC -!- PTM: Methylated at His-75 by SETD3. {ECO:0000250|UniProtKB:P68133}.
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; M12866; AAA37164.1; -; mRNA.
DR EMBL; M12347; AAA37141.1; -; Genomic_DNA.
DR EMBL; BC014877; AAH14877.1; -; mRNA.
DR CCDS; CCDS22764.1; -.
DR PIR; A24904; A24904.
DR RefSeq; NP_001258970.1; NM_001272041.1.
DR RefSeq; NP_033736.1; NM_009606.3.
DR PDB; 4B1U; X-ray; 2.00 A; B=2-377.
DR PDB; 6KLL; EM; 3.00 A; A/B/C/D=3-377.
DR PDB; 6KLN; EM; 3.40 A; A/B/C/D=3-377.
DR PDB; 7AQK; EM; 9.00 A; h/i/j/k/l/m/n/o/p/q/r=1-377.
DR PDB; 7NEP; EM; 10.20 A; A/B/C/D/E/F/G/H/I/J/K=4-377.
DR PDB; 7QIN; EM; 6.60 A; A/B/C/D/E=7-377.
DR PDBsum; 4B1U; -.
DR PDBsum; 6KLL; -.
DR PDBsum; 6KLN; -.
DR PDBsum; 7AQK; -.
DR PDBsum; 7NEP; -.
DR PDBsum; 7QIN; -.
DR AlphaFoldDB; P68134; -.
DR SMR; P68134; -.
DR BioGRID; 197943; 49.
DR IntAct; P68134; 26.
DR MINT; P68134; -.
DR STRING; 10090.ENSMUSP00000034453; -.
DR iPTMnet; P68134; -.
DR PhosphoSitePlus; P68134; -.
DR SwissPalm; P68134; -.
DR EPD; P68134; -.
DR jPOST; P68134; -.
DR MaxQB; P68134; -.
DR PaxDb; P68134; -.
DR PeptideAtlas; P68134; -.
DR PRIDE; P68134; -.
DR ProteomicsDB; 285545; -.
DR Antibodypedia; 3508; 1341 antibodies from 45 providers.
DR DNASU; 11459; -.
DR Ensembl; ENSMUST00000034453; ENSMUSP00000034453; ENSMUSG00000031972.
DR GeneID; 11459; -.
DR KEGG; mmu:11459; -.
DR UCSC; uc009nwr.2; mouse.
DR CTD; 58; -.
DR MGI; MGI:87902; Acta1.
DR VEuPathDB; HostDB:ENSMUSG00000031972; -.
DR eggNOG; KOG0676; Eukaryota.
DR GeneTree; ENSGT00940000156048; -.
DR HOGENOM; CLU_027965_0_2_1; -.
DR InParanoid; P68134; -.
DR OMA; DESHACE; -.
DR OrthoDB; 649708at2759; -.
DR PhylomeDB; P68134; -.
DR TreeFam; TF354237; -.
DR Reactome; R-MMU-390522; Striated Muscle Contraction.
DR BioGRID-ORCS; 11459; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Acta1; mouse.
DR PRO; PR:P68134; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; P68134; protein.
DR Bgee; ENSMUSG00000031972; Expressed in tarsal region and 197 other tissues.
DR ExpressionAtlas; P68134; baseline and differential.
DR Genevisible; P68134; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0005884; C:actin filament; ISS:UniProtKB.
DR GO; GO:0044297; C:cell body; ISS:AgBase.
DR GO; GO:0005737; C:cytoplasm; ISS:AgBase.
DR GO; GO:0005869; C:dynactin complex; IBA:GO_Central.
DR GO; GO:0030175; C:filopodium; ISS:AgBase.
DR GO; GO:0030027; C:lamellipodium; ISS:AgBase.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0030017; C:sarcomere; ISO:MGI.
DR GO; GO:0001725; C:stress fiber; ISS:UniProtKB.
DR GO; GO:0005865; C:striated muscle thin filament; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0071417; P:cellular response to organonitrogen compound; 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:0009991; P:response to extracellular stimulus; IEA:Ensembl.
DR GO; GO:0010226; P:response to lithium ion; IEA:Ensembl.
DR GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl.
DR GO; GO:0048545; P:response to steroid hormone; IEA:Ensembl.
DR GO; GO:0043503; P:skeletal muscle fiber adaptation; IEA:Ensembl.
DR GO; GO:0048741; P:skeletal muscle fiber development; IDA:UniProtKB.
DR GO; GO:0030240; P:skeletal muscle thin filament assembly; ISS:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Cytoplasm; Cytoskeleton;
KW Methylation; Muscle protein; Nucleotide-binding; Oxidation;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..377
FT /note="Actin, alpha skeletal muscle, intermediate form"
FT /evidence="ECO:0000250|UniProtKB:P62737"
FT /id="PRO_0000442805"
FT CHAIN 3..377
FT /note="Actin, alpha skeletal muscle"
FT /evidence="ECO:0000250|UniProtKB:P62737"
FT /id="PRO_0000442806"
FT REGION 112..125
FT /note="Interaction with alpha-actinin"
FT /evidence="ECO:0000250|UniProtKB:P68135"
FT REGION 360..372
FT /note="Interaction with alpha-actinin"
FT /evidence="ECO:0000250|UniProtKB:P68135"
FT MOD_RES 2
FT /note="N-acetylcysteine; in intermediate form"
FT /evidence="ECO:0000250|UniProtKB:P62737"
FT MOD_RES 46
FT /note="Methionine (R)-sulfoxide"
FT /evidence="ECO:0000269|PubMed:23911929"
FT MOD_RES 49
FT /note="Methionine (R)-sulfoxide"
FT /evidence="ECO:0000269|PubMed:23911929"
FT MOD_RES 63
FT /note="N6-malonyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 75
FT /note="Tele-methylhistidine"
FT /evidence="ECO:0000250|UniProtKB:P68138"
FT MOD_RES 86
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:P68133"
FT STRAND 10..14
FT /evidence="ECO:0007829|PDB:4B1U"
FT STRAND 16..23
FT /evidence="ECO:0007829|PDB:4B1U"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:4B1U"
FT STRAND 30..34
FT /evidence="ECO:0007829|PDB:4B1U"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:6KLL"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:6KLL"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:6KLL"
FT HELIX 57..62
FT /evidence="ECO:0007829|PDB:4B1U"
FT TURN 63..66
FT /evidence="ECO:0007829|PDB:4B1U"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:6KLL"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:4B1U"
FT HELIX 81..93
FT /evidence="ECO:0007829|PDB:4B1U"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:4B1U"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:4B1U"
FT HELIX 115..127
FT /evidence="ECO:0007829|PDB:4B1U"
FT STRAND 132..138
FT /evidence="ECO:0007829|PDB:4B1U"
FT HELIX 139..146
FT /evidence="ECO:0007829|PDB:4B1U"
FT STRAND 150..157
FT /evidence="ECO:0007829|PDB:4B1U"
FT STRAND 162..168
FT /evidence="ECO:0007829|PDB:4B1U"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:4B1U"
FT STRAND 178..181
FT /evidence="ECO:0007829|PDB:4B1U"
FT HELIX 184..197
FT /evidence="ECO:0007829|PDB:4B1U"
FT HELIX 205..218
FT /evidence="ECO:0007829|PDB:4B1U"
FT HELIX 225..229
FT /evidence="ECO:0007829|PDB:4B1U"
FT STRAND 240..243
FT /evidence="ECO:0007829|PDB:4B1U"
FT STRAND 249..253
FT /evidence="ECO:0007829|PDB:4B1U"
FT HELIX 255..264
FT /evidence="ECO:0007829|PDB:4B1U"
FT HELIX 266..269
FT /evidence="ECO:0007829|PDB:4B1U"
FT HELIX 276..285
FT /evidence="ECO:0007829|PDB:4B1U"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:4B1U"
FT HELIX 292..296
FT /evidence="ECO:0007829|PDB:4B1U"
FT STRAND 299..303
FT /evidence="ECO:0007829|PDB:4B1U"
FT HELIX 304..306
FT /evidence="ECO:0007829|PDB:4B1U"
FT HELIX 311..322
FT /evidence="ECO:0007829|PDB:4B1U"
FT HELIX 337..339
FT /evidence="ECO:0007829|PDB:4B1U"
FT HELIX 340..350
FT /evidence="ECO:0007829|PDB:4B1U"
FT HELIX 352..354
FT /evidence="ECO:0007829|PDB:4B1U"
FT TURN 355..357
FT /evidence="ECO:0007829|PDB:4B1U"
FT STRAND 358..360
FT /evidence="ECO:0007829|PDB:4B1U"
FT HELIX 361..367
FT /evidence="ECO:0007829|PDB:4B1U"
FT HELIX 368..370
FT /evidence="ECO:0007829|PDB:4B1U"
FT HELIX 371..375
FT /evidence="ECO:0007829|PDB:4B1U"
SQ SEQUENCE 377 AA; 42051 MW; DF2A3A046346A179 CRC64;
MCDEDETTAL VCDNGSGLVK AGFAGDDAPR AVFPSIVGRP RHQGVMVGMG QKDSYVGDEA
QSKRGILTLK YPIEHGIITN WDDMEKIWHH TFYNELRVAP EEHPTLLTEA PLNPKANREK
MTQIMFETFN VPAMYVAIQA VLSLYASGRT TGIVLDSGDG VTHNVPIYEG YALPHAIMRL
DLAGRDLTDY LMKILTERGY SFVTTAEREI VRDIKEKLCY VALDFENEMA TAASSSSLEK
SYELPDGQVI TIGNERFRCP ETLFQPSFIG MESAGIHETT YNSIMKCDID IRKDLYANNV
MSGGTTMYPG IADRMQKEIT ALAPSTMKIK IIAPPERKYS VWIGGSILAS LSTFQQMWIT
KQEYDEAGPS IVHRKCF
