ACTA_MOUSE
ID ACTA_MOUSE Reviewed; 377 AA.
AC P62737; P03996; P04108;
DT 23-OCT-1986, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Actin, aortic smooth muscle;
DE AltName: Full=Alpha-actin-2;
DE Contains:
DE RecName: Full=Actin, aortic smooth muscle, intermediate form;
DE Flags: Precursor;
GN Name=Acta2; Synonyms=Actsa, Actvs;
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].
RC STRAIN=C3H/HeJ;
RX PubMed=3194212; DOI=10.1093/nar/16.21.10374;
RA Min B.H., Strauch A.R., Foster D.N.;
RT "Nucleotide sequence of a mouse vascular smooth muscle alpha-actin cDNA.";
RL Nucleic Acids Res. 16:10374-10374(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C3H/He; TISSUE=Osteoblast;
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 PROTEIN SEQUENCE OF 3-20, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT
RP CYS-2, AND ACETYLATION AT GLU-3.
RX PubMed=6725286; DOI=10.1016/s0021-9258(17)39861-7;
RA Strauch A.R., Rubenstein P.A.;
RT "A vascular smooth muscle alpha-isoactin biosynthetic intermediate in BC3H1
RT cells. Identification of acetylcysteine at the NH2 terminus.";
RL J. Biol. Chem. 259:7224-7229(1984).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-7.
RX PubMed=2398068; DOI=10.1016/s0021-9258(17)46273-9;
RA Min B.H., Foster D.N., Strauch A.R.;
RT "The 5'-flanking region of the mouse vascular smooth muscle alpha-actin
RT gene contains evolutionarily conserved sequence motifs within a functional
RT promoter.";
RL J. Biol. Chem. 265:16667-16675(1990).
RN [6]
RP PROTEIN SEQUENCE OF 21-41; 53-63; 71-86; 98-115; 186-193; 241-256 AND
RP 318-328, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
RA Lubec G., Kang S.U., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [7]
RP TISSUE SPECIFICITY, AND INDUCTION BY S.JAPONICUM INFECTION.
RX PubMed=21679490; DOI=10.1017/s0031182011000667;
RA Duan Y.N., Qian H.Y., Qin Y.W., Zhu D.D., He X.X., Zhou Q., Yang Y.N.,
RA Bao J., Feng J.R., Sun W., Chen J.L.;
RT "Dynamics of Sept4 expression in fibrotic livers of mice infected with
RT Schistosoma japonicum.";
RL Parasitology 138:1003-1010(2011).
RN [8]
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.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- TISSUE SPECIFICITY: Expressed in the liver (at protein level).
CC {ECO:0000269|PubMed:21679490}.
CC -!- INDUCTION: Induced by S.japonicum egg-mediated liver fibrosis at the
CC site of egg granulomas; expression peakes at 12 weeks post infection
CC with expression decreasing thereafter. {ECO:0000269|PubMed:21679490}.
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 (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Methylated at His-75 by SETD3. {ECO:0000250|UniProtKB:P62736}.
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; X13297; CAA31659.1; -; mRNA.
DR EMBL; AK017374; BAB30715.1; -; mRNA.
DR EMBL; BC064800; AAH64800.1; -; mRNA.
DR EMBL; M57409; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS29757.1; -.
DR PIR; S02135; A22224.
DR RefSeq; NP_031418.1; NM_007392.3.
DR AlphaFoldDB; P62737; -.
DR SMR; P62737; -.
DR BioGRID; 197952; 11.
DR IntAct; P62737; 5.
DR MINT; P62737; -.
DR STRING; 10090.ENSMUSP00000048218; -.
DR iPTMnet; P62737; -.
DR PhosphoSitePlus; P62737; -.
DR SwissPalm; P62737; -.
DR REPRODUCTION-2DPAGE; P62737; -.
DR UCD-2DPAGE; P62737; -.
DR CPTAC; non-CPTAC-3327; -.
DR CPTAC; non-CPTAC-3440; -.
DR jPOST; P62737; -.
DR MaxQB; P62737; -.
DR PaxDb; P62737; -.
DR PeptideAtlas; P62737; -.
DR PRIDE; P62737; -.
DR ProteomicsDB; 285544; -.
DR Antibodypedia; 30207; 1525 antibodies from 51 providers.
DR DNASU; 11475; -.
DR Ensembl; ENSMUST00000039631; ENSMUSP00000048218; ENSMUSG00000035783.
DR GeneID; 11475; -.
DR KEGG; mmu:11475; -.
DR UCSC; uc008hgg.2; mouse.
DR CTD; 59; -.
DR MGI; MGI:87909; Acta2.
DR VEuPathDB; HostDB:ENSMUSG00000035783; -.
DR eggNOG; KOG0676; Eukaryota.
DR GeneTree; ENSGT00940000154148; -.
DR HOGENOM; CLU_027965_0_2_1; -.
DR InParanoid; P62737; -.
DR OMA; PNIMVGM; -.
DR OrthoDB; 649708at2759; -.
DR PhylomeDB; P62737; -.
DR TreeFam; TF354237; -.
DR Reactome; R-MMU-445355; Smooth Muscle Contraction.
DR BioGRID-ORCS; 11475; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Acta2; mouse.
DR PRO; PR:P62737; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; P62737; protein.
DR Bgee; ENSMUSG00000035783; Expressed in ascending aorta and 263 other tissues.
DR ExpressionAtlas; P62737; baseline and differential.
DR Genevisible; P62737; MM.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:MGI.
DR GO; GO:0044297; C:cell body; ISS:AgBase.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005856; C:cytoskeleton; IDA:MGI.
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:0030485; C:smooth muscle contractile fiber; IDA:MGI.
DR GO; GO:0001725; C:stress fiber; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019901; F:protein kinase binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0072144; P:glomerular mesangial cell development; IEA:Ensembl.
DR GO; GO:0090131; P:mesenchyme migration; ISS:AgBase.
DR GO; GO:0006936; P:muscle contraction; ISO:MGI.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISS:AgBase.
DR GO; GO:2000491; P:positive regulation of hepatic stellate cell activation; ISO:MGI.
DR GO; GO:0061874; P:positive regulation of hepatic stellate cell contraction; ISO:MGI.
DR GO; GO:0061870; P:positive regulation of hepatic stellate cell migration; ISO:MGI.
DR GO; GO:0008217; P:regulation of blood pressure; IMP:MGI.
DR GO; GO:0061041; P:regulation of wound healing; ISO:MGI.
DR GO; GO:0009615; P:response to virus; IEA:Ensembl.
DR GO; GO:0014829; P:vascular associated smooth muscle contraction; IMP: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; Muscle protein; Nucleotide-binding;
KW Oxidation; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:6725286"
FT CHAIN 2..377
FT /note="Actin, aortic smooth muscle, intermediate form"
FT /evidence="ECO:0000269|PubMed:6725286"
FT /id="PRO_0000442605"
FT CHAIN 3..377
FT /note="Actin, aortic smooth muscle"
FT /evidence="ECO:0000269|PubMed:6725286"
FT /id="PRO_0000442606"
FT MOD_RES 2
FT /note="N-acetylcysteine; in intermediate form"
FT /evidence="ECO:0000269|PubMed:6725286"
FT MOD_RES 3
FT /note="N-acetylglutamate; in Actin, aortic smooth muscle"
FT /evidence="ECO:0000269|PubMed:6725286"
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 75
FT /note="Tele-methylhistidine"
FT /evidence="ECO:0000250|UniProtKB:P62739"
FT MOD_RES 86
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:P68032"
SQ SEQUENCE 377 AA; 42009 MW; 2D0543262DB35CA5 CRC64;
MCEEEDSTAL VCDNGSGLCK AGFAGDDAPR AVFPSIVGRP RHQGVMVGMG QKDSYVGDEA
QSKRGILTLK YPIEHGIITN WDDMEKIWHH SFYNELRVAP EEHPTLLTEA PLNPKANREK
MTQIMFETFN VPAMYVAIQA VLSLYASGRT TGIVLDSGDG VTHNVPIYEG YALPHAIMRL
DLAGRDLTDY LMKILTERGY SFVTTAEREI VRDIKEKLCY VALDFENEMA TAASSSSLEK
SYELPDGQVI TIGNERFRCP ETLFQPSFIG MESAGIHETT YNSIMKCDID IRKDLYANNV
LSGGTTMYPG IADRMQKEIT ALAPSTMKIK IIAPPERKYS VWIGGSILAS LSTFQQMWIS
KQEYDEAGPS IVHRKCF
