ACTG_MOUSE
ID ACTG_MOUSE Reviewed; 375 AA.
AC P63260; P02571; P14104; P99022;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 164.
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 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 PROTEIN SEQUENCE OF 2-375, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT
RP GLU-2, AND METHYLATION AT HIS-73.
RX PubMed=213279; DOI=10.1111/j.1432-1033.1978.tb12624.x;
RA Vandekerckhove J., Weber K.;
RT "Actin amino-acid sequences. Comparison of actins from calf thymus, bovine
RT brain, and SV40-transformed mouse 3T3 cells with rabbit skeletal muscle
RT actin.";
RL Eur. J. Biochem. 90:451-462(1978).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3221869; DOI=10.1128/mcb.8.9.3929-3933.1988;
RA Tokunaga K., Takeda K., Kamiyama K., Kageyama H., Takenaga K., Sakiyama S.;
RT "Isolation of cDNA clones for mouse cytoskeletal gamma-actin and
RT differential expression of cytoskeletal actin mRNAs in mouse cells.";
RL Mol. Cell. Biol. 8:3929-3933(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N, and NMRI; TISSUE=Colon, and 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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 8-375.
RX PubMed=3210229; DOI=10.1016/0022-2836(88)90200-8;
RA Peter B., Man Y.M., Begg C.E., Gall I., Leader D.P.;
RT "Mouse cytoskeletal gamma-actin: analysis and implications of the structure
RT of cloned cDNA and processed pseudogenes.";
RL J. Mol. Biol. 203:665-675(1988).
RN [6]
RP PROTEIN SEQUENCE OF 29-39.
RC TISSUE=Brain;
RA Lubec G., Yang J.W., Zigmond M.;
RL Submitted (JUL-2007) to UniProtKB.
RN [7]
RP OXIDATION AT MET-44 AND MET-47, AND DEOXIDATION AT MET-44 AND MET-47.
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. {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 -!- INTERACTION:
CC P63260; Q08460: Kcnma1; NbExp=4; IntAct=EBI-351301, EBI-1633915;
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
CC (PubMed:23911929). The (R)-S-oxide form is reverted by MSRB1 and MSRB2,
CC which promote actin repolymerization (PubMed:23911929).
CC {ECO:0000269|PubMed:23911929}.
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; X13055; CAA31455.1; -; mRNA.
DR EMBL; AK076081; BAC36167.1; -; mRNA.
DR EMBL; AK087983; BAC40075.1; -; mRNA.
DR EMBL; BC003337; AAH03337.1; -; mRNA.
DR EMBL; BC021796; AAH21796.1; -; mRNA.
DR EMBL; BC023248; AAH23248.1; -; mRNA.
DR EMBL; M21495; AAA37168.1; -; mRNA.
DR CCDS; CCDS25730.1; -.
DR PIR; A30243; ATMSG.
DR RefSeq; NP_033739.1; NM_009609.3.
DR AlphaFoldDB; P63260; -.
DR SMR; P63260; -.
DR BioGRID; 197946; 71.
DR CORUM; P63260; -.
DR IntAct; P63260; 26.
DR MINT; P63260; -.
DR STRING; 10090.ENSMUSP00000071486; -.
DR CarbonylDB; P63260; -.
DR iPTMnet; P63260; -.
DR PhosphoSitePlus; P63260; -.
DR SwissPalm; P63260; -.
DR COMPLUYEAST-2DPAGE; P63260; -.
DR REPRODUCTION-2DPAGE; P63260; -.
DR UCD-2DPAGE; P63260; -.
DR EPD; P63260; -.
DR jPOST; P63260; -.
DR PaxDb; P63260; -.
DR PeptideAtlas; P63260; -.
DR PRIDE; P63260; -.
DR ProteomicsDB; 285853; -.
DR Antibodypedia; 32827; 383 antibodies from 34 providers.
DR DNASU; 11465; -.
DR Ensembl; ENSMUST00000071555; ENSMUSP00000071486; ENSMUSG00000062825.
DR Ensembl; ENSMUST00000106215; ENSMUSP00000101822; ENSMUSG00000062825.
DR GeneID; 11465; -.
DR KEGG; mmu:11465; -.
DR UCSC; uc007msi.1; mouse.
DR CTD; 71; -.
DR MGI; MGI:87906; Actg1.
DR VEuPathDB; HostDB:ENSMUSG00000062825; -.
DR eggNOG; KOG0676; Eukaryota.
DR GeneTree; ENSGT00950000182960; -.
DR HOGENOM; CLU_027965_0_2_1; -.
DR InParanoid; P63260; -.
DR OMA; WICKSEY; -.
DR OrthoDB; 649708at2759; -.
DR PhylomeDB; P63260; -.
DR TreeFam; TF354237; -.
DR Reactome; R-MMU-114608; Platelet degranulation.
DR Reactome; R-MMU-190873; Gap junction degradation.
DR Reactome; R-MMU-196025; Formation of annular gap junctions.
DR Reactome; R-MMU-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-MMU-3928662; EPHB-mediated forward signaling.
DR Reactome; R-MMU-418990; Adherens junctions interactions.
DR Reactome; R-MMU-437239; Recycling pathway of L1.
DR Reactome; R-MMU-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-MMU-445095; Interaction between L1 and Ankyrins.
DR Reactome; R-MMU-446353; Cell-extracellular matrix interactions.
DR Reactome; R-MMU-5626467; RHO GTPases activate IQGAPs.
DR Reactome; R-MMU-5663213; RHO GTPases Activate WASPs and WAVEs.
DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR Reactome; R-MMU-5674135; MAP2K and MAPK activation.
DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-MMU-9013418; RHOBTB2 GTPase cycle.
DR BioGRID-ORCS; 11465; 11 hits in 73 CRISPR screens.
DR ChiTaRS; Actg1; mouse.
DR PRO; PR:P63260; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P63260; protein.
DR Bgee; ENSMUSG00000062825; Expressed in ectoplacental cone and 72 other tissues.
DR ExpressionAtlas; P63260; baseline and differential.
DR Genevisible; P63260; MM.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:MGI.
DR GO; GO:0005884; C:actin filament; ISO:MGI.
DR GO; GO:0043296; C:apical junction complex; ISO:MGI.
DR GO; GO:0045177; C:apical part of cell; IDA:MGI.
DR GO; GO:0120220; C:basal body patch; IDA:MGI.
DR GO; GO:0044305; C:calyx of Held; IDA:SynGO.
DR GO; GO:0005911; C:cell-cell junction; ISO:MGI.
DR GO; GO:0043034; C:costamere; TAS:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0097433; C:dense body; ISS:AgBase.
DR GO; GO:0070062; C:extracellular exosome; ISO:MGI.
DR GO; GO:0031941; C:filamentous actin; IDA:MGI.
DR GO; GO:0005925; C:focal adhesion; ISS:AgBase.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0030016; C:myofibril; IDA:MGI.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:AgBase.
DR GO; GO:0098871; C:postsynaptic actin cytoskeleton; ISO:MGI.
DR GO; GO:0099143; C:presynaptic actin cytoskeleton; ISO:MGI.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0005522; F:profilin binding; ISO:MGI.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IDA:MGI.
DR GO; GO:0098973; F:structural constituent of postsynaptic actin cytoskeleton; ISO:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0001525; P:angiogenesis; ISO:MGI.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IDA:MGI.
DR GO; GO:0001738; P:morphogenesis of a polarized epithelium; ISO:MGI.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0090303; P:positive regulation of wound healing; ISO:MGI.
DR GO; GO:1902396; P:protein localization to bicellular tight junction; ISO:MGI.
DR GO; GO:0051893; P:regulation of focal adhesion assembly; ISO:MGI.
DR GO; GO:0051492; P:regulation of stress fiber assembly; ISO:MGI.
DR GO; GO:0150111; P:regulation of transepithelial transport; ISO:MGI.
DR GO; GO:0051592; P:response to calcium ion; IEA:Ensembl.
DR GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl.
DR GO; GO:0045214; P:sarcomere organization; IDA:MGI.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IDA:SynGO.
DR GO; GO:0120192; P:tight junction assembly; ISO:MGI.
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 Acetylation; ATP-binding; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Methylation; Nucleotide-binding; Oxidation;
KW Reference proteome.
FT CHAIN 1..375
FT /note="Actin, cytoplasmic 2"
FT /id="PRO_0000367101"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000269|PubMed:213279"
FT CHAIN 2..375
FT /note="Actin, cytoplasmic 2, N-terminally processed"
FT /id="PRO_0000000833"
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:0000269|PubMed:213279"
FT MOD_RES 44
FT /note="Methionine (R)-sulfoxide"
FT /evidence="ECO:0000269|PubMed:23911929"
FT MOD_RES 47
FT /note="Methionine (R)-sulfoxide"
FT /evidence="ECO:0000269|PubMed:23911929"
FT MOD_RES 73
FT /note="Tele-methylhistidine"
FT /evidence="ECO:0000269|PubMed:213279"
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
