ID   ACTC_HUMAN              Reviewed;         377 AA.
AC   P68032; P04270;
DT   20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-1987, sequence version 1.
DT   02-SEP-2026, entry version 188.
DE   RecName: Full=Actin, alpha cardiac muscle 1;
DE            EC=3.6.4.- {ECO:0000250|UniProtKB:P68137};
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   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6310553; DOI=10.1073/pnas.79.19.5901;
RA   Hamada H., Petrino M.G., Kakunaga T.;
RT   "Molecular structure and evolutionary origin of human cardiac muscle actin
RT   gene.";
RL   Proc. Natl. Acad. Sci. U.S.A. 79:5901-5905(1982).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Muscle;
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   CROSS-LINK BY V.CHOLERAE TOXIN RTXA (MICROBIAL INFECTION).
RX   PubMed=19015515; DOI=10.1073/pnas.0808082105;
RA   Kudryashov D.S., Durer Z.A., Ytterberg A.J., Sawaya M.R., Pashkov I.,
RA   Prochazkova K., Yeates T.O., Loo R.R., Loo J.A., Satchell K.J., Reisler E.;
RT   "Connecting actin monomers by iso-peptide bond is a toxicity mechanism of
RT   the Vibrio cholerae MARTX toxin.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:18537-18542(2008).
RN   [5]
RP   METHYLATION AT LYS-86, AND DEMETHYLATION BY ALKBH4.
RX   PubMed=23673617; DOI=10.1038/ncomms2863;
RA   Li M.M., Nilsen A., Shi Y., Fusser M., Ding Y.H., Fu Y., Liu B., Niu Y.,
RA   Wu Y.S., Huang C.M., Olofsson M., Jin K.X., Lv Y., Xu X.Z., He C.,
RA   Dong M.Q., Rendtlew Danielsen J.M., Klungland A., Yang Y.G.;
RT   "ALKBH4-dependent demethylation of actin regulates actomyosin dynamics.";
RL   Nat. Commun. 4:1832-1832(2013).
RN   [6]
RP   CROSS-LINK BY V.CHOLERAE TOXIN RTXA (MICROBIAL INFECTION).
RX   PubMed=26228148; DOI=10.1126/science.aab4090;
RA   Heisler D.B., Kudryashova E., Grinevich D.O., Suarez C., Winkelman J.D.,
RA   Birukov K.G., Kotha S.R., Parinandi N.L., Vavylonis D., Kovar D.R.,
RA   Kudryashov D.S.;
RT   "ACD toxin-produced actin oligomers poison formin-controlled actin
RT   polymerization.";
RL   Science 349:535-539(2015).
RN   [7]
RP   METHYLATION AT HIS-75.
RX   PubMed=30626964; DOI=10.1038/s41586-018-0821-8;
RA   Wilkinson A.W., Diep J., Dai S., Liu S., Ooi Y.S., Song D., Li T.M.,
RA   Horton J.R., Zhang X., Liu C., Trivedi D.V., Ruppel K.M.,
RA   Vilches-Moure J.G., Casey K.M., Mak J., Cowan T., Elias J.E.,
RA   Nagamine C.M., Spudich J.A., Cheng X., Carette J.E., Gozani O.;
RT   "SETD3 is an actin histidine methyltransferase that prevents primary
RT   dystocia.";
RL   Nature 565:372-376(2019).
RN   [8]
RP   VARIANTS CMD1R HIS-314 AND GLY-363.
RX   PubMed=9563954; DOI=10.1126/science.280.5364.750;
RA   Olson T.M., Michels V.V., Thibodeau S.N., Tai Y.-S., Keating M.T.;
RT   "Actin mutations in dilated cardiomyopathy, a heritable form of heart
RT   failure.";
RL   Science 280:750-752(1998).
RN   [9]
RP   VARIANT CMH11 SER-297.
RX   PubMed=10330430; DOI=10.1172/jci6460;
RA   Mogensen J., Klausen I.C., Pedersen A.K., Egeblad H., Bross P., Kruse T.A.,
RA   Gregersen N., Hansen P.S., Baandrup U., Boerglum A.D.;
RT   "Alpha-cardiac actin is a novel disease gene in familial hypertrophic
RT   cardiomyopathy.";
RL   J. Clin. Invest. 103:R39-R43(1999).
RN   [10]
RP   VARIANTS CMH11 LYS-101; ALA-166 AND PRO-333.
RX   PubMed=10966831; DOI=10.1006/jmcc.2000.1204;
RA   Olson T.M., Doan T.P., Kishimoto N.Y., Whitby F.G., Ackerman M.J.,
RA   Fananapazir L.;
RT   "Inherited and de novo mutations in the cardiac actin gene cause
RT   hypertrophic cardiomyopathy.";
RL   J. Mol. Cell. Cardiol. 32:1687-1694(2000).
RN   [11]
RP   VARIANTS CMH11 CYS-168 AND LEU-307.
RX   PubMed=14729850; DOI=10.1136/jmg.2003.010447;
RA   Mogensen J., Perrot A., Andersen P.S., Havndrup O., Klausen I.C.,
RA   Christiansen M., Bross P., Egeblad H., Bundgaard H., Osterziel K.J.,
RA   Haltern G., Lapp H., Reinecke P., Gregersen N., Borglum A.D.;
RT   "Clinical and genetic characteristics of alpha cardiac actin gene mutations
RT   in hypertrophic cardiomyopathy.";
RL   J. Med. Genet. 41:E10-E10(2004).
RN   [12]
RP   VARIANT ASD5 VAL-125, AND CHARACTERIZATION OF VARIANT ASD5 VAL-125.
RX   PubMed=17947298; DOI=10.1093/hmg/ddm302;
RA   Matsson H., Eason J., Bookwalter C.S., Klar J., Gustavsson P.,
RA   Sunnegardh J., Enell H., Jonzon A., Vikkula M., Gutierrez I.,
RA   Granados-Riveron J., Pope M., Bu'Lock F., Cox J., Robinson T.E., Song F.,
RA   Brook D.J., Marston S., Trybus K.M., Dahl N.;
RT   "Alpha-cardiac actin mutations produce atrial septal defects.";
RL   Hum. Mol. Genet. 17:256-265(2008).
RN   [13]
RP   VARIANTS CMH11 TYR-90 AND CYS-97.
RX   PubMed=18403758; DOI=10.1056/nejmoa075463;
RA   Morita H., Rehm H.L., Menesses A., McDonough B., Roberts A.E.,
RA   Kucherlapati R., Towbin J.A., Seidman J.G., Seidman C.E.;
RT   "Shared genetic causes of cardiac hypertrophy in children and adults.";
RL   N. Engl. J. Med. 358:1899-1908(2008).
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   -!- INTERACTION:
CC       P68032; P23528: CFL1; NbExp=2; IntAct=EBI-352273, EBI-352733;
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:0000250|UniProtKB:P68033}.
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:0000269|PubMed:23673617}.
CC   -!- PTM: [Actin, alpha cardiac muscle 1, intermediate form]: N-terminal
CC       cleavage of acetylated cysteine of intermediate muscle actin by ACTMAP.
CC       {ECO:0000250|UniProtKB:P68033}.
CC   -!- PTM: Methylated at His-75 by SETD3. {ECO:0000269|PubMed:30626964}.
CC   -!- PTM: (Microbial infection) Monomeric actin is cross-linked by
CC       V.cholerae toxins RtxA and VgrG1 in case of infection: bacterial toxins
CC       mediate the cross-link between Lys-52 of one monomer and Glu-272 of
CC       another actin monomer, resulting in formation of highly toxic actin
CC       oligomers that cause cell rounding (PubMed:19015515). The toxin can be
CC       highly efficient at very low concentrations by acting on formin
CC       homology family proteins: toxic actin oligomers bind with high affinity
CC       to formins and adversely affect both nucleation and elongation
CC       abilities of formins, causing their potent inhibition in both profilin-
CC       dependent and independent manners (PubMed:26228148).
CC       {ECO:0000305|PubMed:19015515, ECO:0000305|PubMed:26228148}.
CC   -!- DISEASE: Cardiomyopathy, dilated, 1R (CMD1R) [MIM:613424]: A disorder
CC       characterized by ventricular dilation and impaired systolic function,
CC       resulting in congestive heart failure and arrhythmia. Patients are at
CC       risk of premature death. {ECO:0000269|PubMed:9563954}. Note=The disease
CC       is caused by variants affecting the gene represented in this entry.
CC   -!- DISEASE: Cardiomyopathy, familial hypertrophic, 11 (CMH11)
CC       [MIM:612098]: A hereditary heart disorder characterized by ventricular
CC       hypertrophy, which is usually asymmetric and often involves the
CC       interventricular septum. The symptoms include dyspnea, syncope,
CC       collapse, palpitations, and chest pain. They can be readily provoked by
CC       exercise. The disorder has inter- and intrafamilial variability ranging
CC       from benign to malignant forms with high risk of cardiac failure and
CC       sudden cardiac death. {ECO:0000269|PubMed:10330430,
CC       ECO:0000269|PubMed:10966831, ECO:0000269|PubMed:14729850,
CC       ECO:0000269|PubMed:18403758}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- DISEASE: Atrial septal defect 5 (ASD5) [MIM:612794]: A congenital heart
CC       malformation characterized by incomplete closure of the wall between
CC       the atria resulting in blood flow from the left to the right atria.
CC       {ECO:0000269|PubMed:17947298}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
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; J00073; AAB59619.1; -; Genomic_DNA.
DR   EMBL; J00070; AAB59619.1; JOINED; Genomic_DNA.
DR   EMBL; J00071; AAB59619.1; JOINED; Genomic_DNA.
DR   EMBL; J00072; AAB59619.1; JOINED; Genomic_DNA.
DR   EMBL; CR541795; CAG46594.1; -; mRNA.
DR   EMBL; BC009978; AAH09978.1; -; mRNA.
DR   CCDS; CCDS10041.1; -.
DR   PIR; A02998; ATHUC.
DR   RefSeq; NP_001393411.1; NM_001406482.1.
DR   RefSeq; NP_001393412.1; NM_001406483.1.
DR   RefSeq; NP_005150.1; NM_005159.5.
DR   RefSeq; XP_047288935.1; XM_047432979.1.
DR   PDB; 8GSU; X-ray; 1.50 A; A=3-377.
DR   PDB; 8GSW; X-ray; 1.40 A; A=3-377.
DR   PDB; 8GT1; X-ray; 1.35 A; A=3-377.
DR   PDB; 8GT2; X-ray; 1.50 A; A=3-377.
DR   PDB; 8GT3; X-ray; 1.50 A; A=3-377.
DR   PDB; 8GT4; X-ray; 1.55 A; A=3-377.
DR   PDB; 8GT5; X-ray; 1.40 A; A=3-377.
DR   PDB; 8ZB7; EM; 3.19 A; A/B/C/D/E/F=7-377.
DR   PDB; 8ZI9; EM; 3.08 A; F=7-377.
DR   PDB; 8ZJ1; EM; 4.25 A; A/C/D/E/F=7-377.
DR   PDB; 9B3Q; EM; 3.60 A; A/D/E=1-377.
DR   PDB; 9B3R; EM; 3.50 A; A/D/E=1-377.
DR   PDB; 9BPH; EM; 3.12 A; A/B/C/D=3-377.
DR   PDB; 9BPM; EM; 3.42 A; A/B/C/D=3-377.
DR   PDB; 9ZBL; EM; 2.79 A; A/B/C/D/E/F=1-377.
DR   PDB; 9ZBP; EM; 3.12 A; A/B/C/D/E/F=1-377.
DR   AlphaFoldDB; P68032; -.
DR   EMDB; EMD-39896; -.
DR   EMDB; EMD-44153; -.
DR   EMDB; EMD-44154; -.
DR   EMDB; EMD-44777; -.
DR   EMDB; EMD-44781; -.
DR   EMDB; EMD-60122; -.
DR   EMDB; EMD-60135; -.
DR   EMDB; EMD-73993; -.
DR   EMDB; EMD-73996; -.
DR   SMR; P68032; -.
DR   BioGRID; 106585; 700.
DR   FunCoup; P68032; 966.
DR   IntAct; P68032; 107.
DR   MINT; P68032; -.
DR   NDEx; IQUERY-CP-ACTC1; 4 NDEx IQuery Curated Pathways.
DR   STRING; 9606.ENSP00000290378; -.
DR   BindingDB; P68032; -.
DR   ChEMBL; CHEMBL6066852; -.
DR   GlyGen; P68032; 3 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (2 sites).
DR   iPTMnet; P68032; -.
DR   MetOSite; P68032; -.
DR   PhosphoSitePlus; P68032; -.
DR   SwissPalm; P68032; -.
DR   BioMuta; ACTC1; -.
DR   DMDM; 54036697; -.
DR   REPRODUCTION-2DPAGE; P68032; -.
DR   jPOST; P68032; -.
DR   MassIVE; P68032; -.
DR   PaxDb; 9606-ENSP00000290378; -.
DR   PeptideAtlas; P68032; -.
DR   PRIDE; P68032; -.
DR   ProteomicsDB; 57527; -.
DR   Pumba; P68032; -.
DR   TopDownProteomics; P68032; -.
DR   Antibodypedia; 9782; 347 antibodies from 38 providers.
DR   DNASU; 70; -.
DR   Ensembl; ENST00000290378.6; ENSP00000290378.4; ENSG00000159251.11.
DR   Ensembl; ENST00000713610.1; ENSP00000518905.1; ENSG00000159251.11.
DR   Ensembl; ENST00000713615.1; ENSP00000518911.1; ENSG00000159251.11.
DR   Ensembl; ENST00000868405.1; ENSP00000538464.1; ENSG00000159251.11.
DR   Ensembl; ENST00000953688.1; ENSP00000623747.1; ENSG00000159251.11.
DR   GeneID; 70; -.
DR   KEGG; hsa:70; -.
DR   MANE-Select; ENST00000290378.6; ENSP00000290378.4; NM_005159.5; NP_005150.1.
DR   UCSC; uc001ziu.2; human.
DR   AGR; HGNC:143; -.
DR   ClinPGx; PA162375571; -.
DR   CTD; 70; -.
DR   DisGeNET; 70; -.
DR   GeneCards; ACTC1; -.
DR   GeneReviews; ACTC1; -.
DR   HGNC; HGNC:143; ACTC1.
DR   HPA; ENSG00000159251; Tissue enriched (heart).
DR   MalaCards; ACTC1; -.
DR   MIM; 102540; gene.
DR   MIM; 612098; phenotype.
DR   MIM; 612794; phenotype.
DR   MIM; 613424; phenotype.
DR   OpenTargets; ENSG00000159251; -.
DR   Orphanet; 99103; Atrial septal defect, ostium secundum type.
DR   Orphanet; 154; Familial isolated dilated cardiomyopathy.
DR   Orphanet; 54260; Left ventricular noncompaction.
DR   VEuPathDB; HostDB:ENSG00000159251; -.
DR   eggNOG; KOG0676; Eukaryota.
DR   GeneTree; ENSGT00940000154710; -.
DR   HOGENOM; CLU_027965_0_2_1; -.
DR   InParanoid; P68032; -.
DR   OMA; FTTSAEF; -.
DR   OrthoDB; 9816491at2759; -.
DR   PAN-GO; P68032; 8 GO annotations based on evolutionary models.
DR   PhylomeDB; P68032; -.
DR   PathwayCommons; P68032; -.
DR   Reactome; R-HSA-390522; Striated Muscle Contraction.
DR   Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR   Reactome; R-HSA-9013026; RHOB GTPase cycle.
DR   Reactome; R-HSA-9764561; Regulation of CDH1 Function.
DR   Reactome; R-HSA-9913351; Formation of the dystrophin-glycoprotein complex (DGC).
DR   Reactome; R-HSA-9958825; Activation of STAT3 by cadherin engagement.
DR   SignaLink; P68032; -.
DR   SIGNOR; P68032; -.
DR   Agora; ENSG00000159251; -.
DR   BioGRID-ORCS; 70; 7 hits in 1146 CRISPR screens.
DR   CD-CODE; DEE660B4; Stress granule.
DR   ChiTaRS; ACTC1; human.
DR   GeneWiki; ACTC1; -.
DR   GenomeRNAi; 70; -.
DR   Pharos; P68032; Tbio.
DR   PRO; PR:P68032; -.
DR   Proteomes; UP000005640; Chromosome 15.
DR   RNAct; P68032; protein.
DR   Bgee; ENSG00000159251; Expressed in left ventricle myocardium and 156 other cell types or tissues.
DR   GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR   GO; GO:0005884; C:actin filament; IDA:UniProtKB.
DR   GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR   GO; GO:0044297; C:cell body; ISS:AgBase.
DR   GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; HDA:UniProtKB.
DR   GO; GO:0030175; C:filopodium; ISS:AgBase.
DR   GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR   GO; GO:0031674; C:I band; ISS:UniProtKB.
DR   GO; GO:0030027; C:lamellipodium; ISS:AgBase.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0030017; C:sarcomere; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR   GO; GO:0016887; F:ATP hydrolysis activity; ISS:UniProtKB.
DR   GO; GO:0000146; F:microfilament motor activity; IDA:UniProtKB.
DR   GO; GO:0017022; F:myosin binding; IDA:BHF-UCL.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
DR   GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR   GO; GO:0030048; P:actin filament-based movement; IDA:UniProtKB.
DR   GO; GO:0033275; P:actin-myosin filament sliding; IMP:BHF-UCL.
DR   GO; GO:0031032; P:actomyosin structure organization; ISS:UniProtKB.
DR   GO; GO:0055008; P:cardiac muscle tissue morphogenesis; ISS:UniProtKB.
DR   GO; GO:0055003; P:cardiac myofibril assembly; ISS:UniProtKB.
DR   GO; GO:0060047; P:heart contraction; IMP:UniProtKB.
DR   GO; GO:0090131; P:mesenchyme migration; ISS:AgBase.
DR   GO; GO:0010628; P:positive regulation of gene expression; ISS:AgBase.
DR   GO; GO:0030240; P:skeletal muscle thin filament assembly; ISS:UniProtKB.
DR   CDD; cd10224; ASKHA_NBD_actin; 1.
DR   FunFam; 3.30.420.40:FF:000131; Actin, alpha skeletal muscle; 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.
DR   PDBsum; 8GSU; -.
DR   PDBsum; 8GSW; -.
DR   PDBsum; 8GT1; -.
DR   PDBsum; 8GT2; -.
DR   PDBsum; 8GT3; -.
DR   PDBsum; 8GT4; -.
DR   PDBsum; 8GT5; -.
DR   PDBsum; 8ZB7; -.
DR   PDBsum; 8ZI9; -.
DR   PDBsum; 8ZJ1; -.
DR   PDBsum; 9B3Q; -.
DR   PDBsum; 9B3R; -.
DR   PDBsum; 9BPH; -.
DR   PDBsum; 9BPM; -.
DR   PDBsum; 9ZBL; -.
DR   PDBsum; 9ZBP; -.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; ATP-binding; Atrial septal defect;
KW   Cardiomyopathy; Cytoplasm; Cytoskeleton; Disease variant; Hydrolase;
KW   Isopeptide bond; 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_0000442998"
FT   CHAIN           3..377
FT                   /note="Actin, alpha cardiac muscle 1"
FT                   /evidence="ECO:0000250|UniProtKB:P68135"
FT                   /id="PRO_0000000813"
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:0000250|UniProtKB:P68033"
FT   MOD_RES         49
FT                   /note="Methionine (R)-sulfoxide"
FT                   /evidence="ECO:0000250|UniProtKB:P68033"
FT   MOD_RES         75
FT                   /note="Tele-methylhistidine"
FT                   /evidence="ECO:0000269|PubMed:30626964"
FT   MOD_RES         86
FT                   /note="N6-methyllysine"
FT                   /evidence="ECO:0000269|PubMed:23673617"
FT   CROSSLNK        52
FT                   /note="Isoglutamyl lysine isopeptide (Lys-Glu) (interchain
FT                   with E-272); by Vibrio toxins RtxA and VgrG1"
FT                   /evidence="ECO:0000250|UniProtKB:P60709"
FT   CROSSLNK        272
FT                   /note="Isoglutamyl lysine isopeptide (Glu-Lys) (interchain
FT                   with K-52); by Vibrio toxins RtxA and VgrG1"
FT                   /evidence="ECO:0000250|UniProtKB:P60709"
FT   VARIANT         90
FT                   /note="H -> Y (in CMH11; dbSNP:rs121912676)"
FT                   /evidence="ECO:0000269|PubMed:18403758"
FT                   /id="VAR_045924"
FT   VARIANT         97
FT                   /note="R -> C (in CMH11; dbSNP:rs759495229)"
FT                   /evidence="ECO:0000269|PubMed:18403758"
FT                   /id="VAR_045925"
FT   VARIANT         101
FT                   /note="E -> K (in CMH11; dbSNP:rs193922680)"
FT                   /evidence="ECO:0000269|PubMed:10966831"
FT                   /id="VAR_012857"
FT   VARIANT         125
FT                   /note="M -> V (in ASD5; reduced affinity for myosin; normal
FT                   actin filament polymerization ability; normal actomyosin
FT                   motor function; dbSNP:rs121912677)"
FT                   /evidence="ECO:0000269|PubMed:17947298"
FT                   /id="VAR_046502"
FT   VARIANT         166
FT                   /note="P -> A (in CMH11; dbSNP:rs267606628)"
FT                   /evidence="ECO:0000269|PubMed:10966831"
FT                   /id="VAR_012858"
FT   VARIANT         168
FT                   /note="Y -> C (in CMH11; dbSNP:rs2140430974)"
FT                   /evidence="ECO:0000269|PubMed:14729850"
FT                   /id="VAR_046503"
FT   VARIANT         297
FT                   /note="A -> S (in CMH11; dbSNP:rs121912675)"
FT                   /evidence="ECO:0000269|PubMed:10330430"
FT                   /id="VAR_012859"
FT   VARIANT         307
FT                   /note="M -> L (in CMH11; dbSNP:rs2140429593)"
FT                   /evidence="ECO:0000269|PubMed:14729850"
FT                   /id="VAR_046504"
FT   VARIANT         314
FT                   /note="R -> H (in CMD1R; dbSNP:rs121912673)"
FT                   /evidence="ECO:0000269|PubMed:9563954"
FT                   /id="VAR_012860"
FT   VARIANT         333
FT                   /note="A -> P (in CMH11; dbSNP:rs267606629)"
FT                   /evidence="ECO:0000269|PubMed:10966831"
FT                   /id="VAR_012861"
FT   VARIANT         363
FT                   /note="E -> G (in CMD1R; dbSNP:rs121912674)"
FT                   /evidence="ECO:0000269|PubMed:9563954"
FT                   /id="VAR_012862"
FT   STRAND          10..14
FT                   /evidence="ECO:0007829|PDB:8GT1"
FT   STRAND          16..23
FT                   /evidence="ECO:0007829|PDB:8GT1"
FT   STRAND          26..28
FT                   /evidence="ECO:0007829|PDB:8GT1"
FT   STRAND          30..34
FT                   /evidence="ECO:0007829|PDB:8GT1"
FT   STRAND          37..41
FT                   /evidence="ECO:0007829|PDB:8GT1"
FT   STRAND          47..49
FT                   /evidence="ECO:0007829|PDB:8ZI9"
FT   HELIX           58..62
FT                   /evidence="ECO:0007829|PDB:8GT1"
FT   TURN            63..65
FT                   /evidence="ECO:0007829|PDB:8GT1"
FT   STRAND          66..70
FT                   /evidence="ECO:0007829|PDB:8GT1"
FT   STRAND          72..74
FT                   /evidence="ECO:0007829|PDB:8GT1"
FT   HELIX           81..89
FT                   /evidence="ECO:0007829|PDB:8GT1"
FT   HELIX           90..96
FT                   /evidence="ECO:0007829|PDB:8GT1"
FT   HELIX           100..102
FT                   /evidence="ECO:0007829|PDB:8GT1"
FT   STRAND          105..109
FT                   /evidence="ECO:0007829|PDB:8GT1"
FT   HELIX           115..127
FT                   /evidence="ECO:0007829|PDB:8GT1"
FT   STRAND          132..138
FT                   /evidence="ECO:0007829|PDB:8GT1"
FT   HELIX           139..146
FT                   /evidence="ECO:0007829|PDB:8GT1"
FT   STRAND          150..157
FT                   /evidence="ECO:0007829|PDB:8GT1"
FT   STRAND          162..168
FT                   /evidence="ECO:0007829|PDB:8GT1"
FT   HELIX           174..176
FT                   /evidence="ECO:0007829|PDB:8GT1"
FT   STRAND          178..181
FT                   /evidence="ECO:0007829|PDB:8GT1"
FT   HELIX           184..195
FT                   /evidence="ECO:0007829|PDB:8GT1"
FT   HELIX           196..198
FT                   /evidence="ECO:0007829|PDB:8GT1"
FT   HELIX           205..218
FT                   /evidence="ECO:0007829|PDB:8GT1"
FT   HELIX           225..234
FT                   /evidence="ECO:0007829|PDB:8GT1"
FT   STRAND          240..243
FT                   /evidence="ECO:0007829|PDB:8GT1"
FT   STRAND          249..253
FT                   /evidence="ECO:0007829|PDB:8GT1"
FT   HELIX           255..264
FT                   /evidence="ECO:0007829|PDB:8GT1"
FT   HELIX           266..269
FT                   /evidence="ECO:0007829|PDB:8GT1"
FT   HELIX           273..275
FT                   /evidence="ECO:0007829|PDB:8GT1"
FT   HELIX           276..285
FT                   /evidence="ECO:0007829|PDB:8GT1"
FT   HELIX           289..296
FT                   /evidence="ECO:0007829|PDB:8GT1"
FT   STRAND          299..303
FT                   /evidence="ECO:0007829|PDB:8GT1"
FT   HELIX           304..307
FT                   /evidence="ECO:0007829|PDB:8GT1"
FT   HELIX           311..322
FT                   /evidence="ECO:0007829|PDB:8GT1"
FT   HELIX           337..339
FT                   /evidence="ECO:0007829|PDB:8GT1"
FT   HELIX           340..348
FT                   /evidence="ECO:0007829|PDB:8GT1"
FT   HELIX           352..356
FT                   /evidence="ECO:0007829|PDB:8GT1"
FT   STRAND          358..360
FT                   /evidence="ECO:0007829|PDB:8GT1"
FT   HELIX           361..367
FT                   /evidence="ECO:0007829|PDB:8GT1"
FT   HELIX           369..371
FT                   /evidence="ECO:0007829|PDB:8GT1"
FT   HELIX           372..375
FT                   /evidence="ECO:0007829|PDB:8GT1"
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
//