ACTC_MOUSE
ID ACTC_MOUSE Reviewed; 377 AA.
AC P68033; P04270;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-1987, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Actin, alpha cardiac muscle 1;
DE AltName: Full=Alpha-cardiac actin;
DE Contains:
DE RecName: Full=Actin, alpha cardiac muscle 1, intermediate form;
DE Flags: Precursor;
GN Name=Actc1; Synonyms=Actc;
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Limb;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 3-377.
RX PubMed=3028523; DOI=10.1007/bf01116542;
RA Leader D.P., Gall I., Campbell P.C.;
RT "The structure of a cDNA clone corresponding to mouse cardiac muscle actin
RT mRNA.";
RL Biosci. Rep. 6:741-747(1986).
RN [4]
RP PROTEIN SEQUENCE OF 71-97 AND 241-256, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
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 -!- INTERACTION:
CC P68033; O70468: Mybpc3; NbExp=3; IntAct=EBI-352284, EBI-8347074;
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 (K86me1) 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:P68032}.
CC -!- PTM: Methylated at His-75 by SETD3. {ECO:0000250|UniProtKB:P68032}.
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; AK014303; BAB29258.1; -; mRNA.
DR EMBL; BC062138; AAH62138.1; -; mRNA.
DR EMBL; M15501; AAA37167.1; -; mRNA.
DR CCDS; CCDS16564.1; -.
DR PIR; A54728; A54728.
DR RefSeq; NP_033738.1; NM_009608.4.
DR AlphaFoldDB; P68033; -.
DR SMR; P68033; -.
DR BioGRID; 197945; 11.
DR IntAct; P68033; 7.
DR MINT; P68033; -.
DR STRING; 10090.ENSMUSP00000087736; -.
DR iPTMnet; P68033; -.
DR PhosphoSitePlus; P68033; -.
DR SwissPalm; P68033; -.
DR jPOST; P68033; -.
DR PaxDb; P68033; -.
DR PeptideAtlas; P68033; -.
DR PRIDE; P68033; -.
DR Antibodypedia; 9782; 324 antibodies from 35 providers.
DR DNASU; 11464; -.
DR Ensembl; ENSMUST00000090269; ENSMUSP00000087736; ENSMUSG00000068614.
DR GeneID; 11464; -.
DR KEGG; mmu:11464; -.
DR UCSC; uc008lpz.1; mouse.
DR CTD; 70; -.
DR MGI; MGI:87905; Actc1.
DR VEuPathDB; HostDB:ENSMUSG00000068614; -.
DR eggNOG; KOG0676; Eukaryota.
DR GeneTree; ENSGT00940000154710; -.
DR HOGENOM; CLU_027965_0_2_1; -.
DR InParanoid; P68033; -.
DR OMA; STFQQKE; -.
DR OrthoDB; 649708at2759; -.
DR PhylomeDB; P68033; -.
DR TreeFam; TF354237; -.
DR Reactome; R-MMU-390522; Striated Muscle Contraction.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013026; RHOB GTPase cycle.
DR BioGRID-ORCS; 11464; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Actc1; mouse.
DR PRO; PR:P68033; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P68033; protein.
DR Bgee; ENSMUSG00000068614; Expressed in atrioventricular valve and 260 other tissues.
DR ExpressionAtlas; P68033; baseline and differential.
DR Genevisible; P68033; MM.
DR GO; GO:0005884; C:actin filament; ISO:MGI.
DR GO; GO:0044297; C:cell body; ISS:AgBase.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005869; C:dynactin complex; IBA:GO_Central.
DR GO; GO:0030175; C:filopodium; ISS:AgBase.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0031674; C:I band; IDA:MGI.
DR GO; GO:0030027; C:lamellipodium; ISS:AgBase.
DR GO; GO:0030017; C:sarcomere; ISO:MGI.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0000146; F:microfilament motor activity; ISO:MGI.
DR GO; GO:0017022; F:myosin binding; ISO:MGI.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0030048; P:actin filament-based movement; ISO:MGI.
DR GO; GO:0070252; P:actin-mediated cell contraction; IMP:MGI.
DR GO; GO:0033275; P:actin-myosin filament sliding; ISO:MGI.
DR GO; GO:0031032; P:actomyosin structure organization; IMP:MGI.
DR GO; GO:0060048; P:cardiac muscle contraction; ISO:MGI.
DR GO; GO:0055008; P:cardiac muscle tissue morphogenesis; IMP:MGI.
DR GO; GO:0055003; P:cardiac myofibril assembly; IMP:MGI.
DR GO; GO:0060047; P:heart contraction; ISO:MGI.
DR GO; GO:0090131; P:mesenchyme migration; ISS:AgBase.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISS:AgBase.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0030240; P:skeletal muscle thin filament assembly; 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 CHAIN 2..377
FT /note="Actin, alpha cardiac muscle 1, intermediate form"
FT /evidence="ECO:0000250|UniProtKB:P62737"
FT /id="PRO_0000442999"
FT CHAIN 3..377
FT /note="Actin, alpha cardiac muscle 1"
FT /evidence="ECO:0000250|UniProtKB:P68135"
FT /id="PRO_0000000815"
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 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; 42019 MW; E5C10FA19730CAD2 CRC64;
MCDDEETTAL 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
LSGGTTMYPG IADRMQKEIT ALAPSTMKIK IIAPPERKYS VWIGGSILAS LSTFQQMWIS
KQEYDEAGPS IVHRKCF
