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Actin, alpha cardiac muscle 1 (Alpha-cardiac actin)

 ACTC_HUMAN              Reviewed;         377 AA.
P68032; P04270;
20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
20-MAR-1987, sequence version 1.
25-OCT-2017, entry version 138.
RecName: Full=Actin, alpha cardiac muscle 1;
AltName: Full=Alpha-cardiac actin;
Flags: Precursor;
Name=ACTC1; Synonyms=ACTC;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6310553; DOI=10.1073/pnas.79.19.5901;
Hamada H., Petrino M.G., Kakunaga T.;
"Molecular structure and evolutionary origin of human cardiac muscle
actin gene.";
Proc. Natl. Acad. Sci. U.S.A. 79:5901-5905(1982).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
CROSS-LINK BY V.CHOLERAE TOXIN RTXA (MICROBIAL INFECTION).
PubMed=19015515; DOI=10.1073/pnas.0808082105;
Kudryashov D.S., Durer Z.A., Ytterberg A.J., Sawaya M.R., Pashkov I.,
Prochazkova K., Yeates T.O., Loo R.R., Loo J.A., Satchell K.J.,
Reisler E.;
"Connecting actin monomers by iso-peptide bond is a toxicity mechanism
of the Vibrio cholerae MARTX toxin.";
Proc. Natl. Acad. Sci. U.S.A. 105:18537-18542(2008).
[5]
METHYLATION AT LYS-86, AND DEMETHYLATION BY ALKBH4.
PubMed=23673617; DOI=10.1038/ncomms2863;
Li M.M., Nilsen A., Shi Y., Fusser M., Ding Y.H., Fu Y., Liu B.,
Niu Y., Wu Y.S., Huang C.M., Olofsson M., Jin K.X., Lv Y., Xu X.Z.,
He C., Dong M.Q., Rendtlew Danielsen J.M., Klungland A., Yang Y.G.;
"ALKBH4-dependent demethylation of actin regulates actomyosin
dynamics.";
Nat. Commun. 4:1832-1832(2013).
[6]
CROSS-LINK BY V.CHOLERAE TOXIN RTXA (MICROBIAL INFECTION).
PubMed=26228148; DOI=10.1126/science.aab4090;
Heisler D.B., Kudryashova E., Grinevich D.O., Suarez C.,
Winkelman J.D., Birukov K.G., Kotha S.R., Parinandi N.L.,
Vavylonis D., Kovar D.R., Kudryashov D.S.;
"ACD toxin-produced actin oligomers poison formin-controlled actin
polymerization.";
Science 349:535-539(2015).
[7]
VARIANTS CMD1R HIS-314 AND GLY-363.
PubMed=9563954; DOI=10.1126/science.280.5364.750;
Olson T.M., Michels V.V., Thibodeau S.N., Tai Y.-S., Keating M.T.;
"Actin mutations in dilated cardiomyopathy, a heritable form of heart
failure.";
Science 280:750-752(1998).
[8]
VARIANT CMH11 SER-297.
PubMed=10330430; DOI=10.1172/JCI6460;
Mogensen J., Klausen I.C., Pedersen A.K., Egeblad H., Bross P.,
Kruse T.A., Gregersen N., Hansen P.S., Baandrup U., Boerglum A.D.;
"Alpha-cardiac actin is a novel disease gene in familial hypertrophic
cardiomyopathy.";
J. Clin. Invest. 103:R39-R43(1999).
[9]
VARIANTS CMH11 LYS-101; ALA-166 AND PRO-333.
PubMed=10966831; DOI=10.1006/jmcc.2000.1204;
Olson T.M., Doan T.P., Kishimoto N.Y., Whitby F.G., Ackerman M.J.,
Fananapazir L.;
"Inherited and de novo mutations in the cardiac actin gene cause
hypertrophic cardiomyopathy.";
J. Mol. Cell. Cardiol. 32:1687-1694(2000).
[10]
VARIANTS CMH11 CYS-168 AND LEU-307.
PubMed=14729850; DOI=10.1136/jmg.2003.010447;
Mogensen J., Perrot A., Andersen P.S., Havndrup O., Klausen I.C.,
Christiansen M., Bross P., Egeblad H., Bundgaard H., Osterziel K.J.,
Haltern G., Lapp H., Reinecke P., Gregersen N., Borglum A.D.;
"Clinical and genetic characteristics of alpha cardiac actin gene
mutations in hypertrophic cardiomyopathy.";
J. Med. Genet. 41:E10-E10(2004).
[11]
VARIANT ASD5 VAL-125, AND CHARACTERIZATION OF VARIANT ASD5 VAL-125.
PubMed=17947298; DOI=10.1093/hmg/ddm302;
Matsson H., Eason J., Bookwalter C.S., Klar J., Gustavsson P.,
Sunnegardh J., Enell H., Jonzon A., Vikkula M., Gutierrez I.,
Granados-Riveron J., Pope M., Bu'Lock F., Cox J., Robinson T.E.,
Song F., Brook D.J., Marston S., Trybus K.M., Dahl N.;
"Alpha-cardiac actin mutations produce atrial septal defects.";
Hum. Mol. Genet. 17:256-265(2008).
[12]
VARIANTS CMH11 TYR-90 AND CYS-97.
PubMed=18403758; DOI=10.1056/NEJMoa075463;
Morita H., Rehm H.L., Menesses A., McDonough B., Roberts A.E.,
Kucherlapati R., Towbin J.A., Seidman J.G., Seidman C.E.;
"Shared genetic causes of cardiac hypertrophy in children and
adults.";
N. Engl. J. Med. 358:1899-1908(2008).
-!- FUNCTION: Actins are highly conserved proteins that are involved
in various types of cell motility and are ubiquitously expressed
in all eukaryotic cells.
-!- SUBUNIT: Polymerization of globular actin (G-actin) leads to a
structural filament (F-actin) in the form of a two-stranded helix.
Each actin can bind to 4 others.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
-!- PTM: Oxidation of Met-46 and Met-49 by MICALs (MICAL1, MICAL2 or
MICAL3) to form methionine sulfoxide promotes actin filament
depolymerization. MICAL1 and MICAL2 produce the (R)-S-oxide form.
The (R)-S-oxide form is reverted by MSRB1 and MSRB2, which promote
actin repolymerization (By similarity). {ECO:0000250}.
-!- PTM: Monomethylation at Lys-86 (K84me1) regulates actin-myosin
interaction and actomyosin-dependent processes. Demethylation by
ALKBH4 is required for maintaining actomyosin dynamics supporting
normal cleavage furrow ingression during cytokinesis and cell
migration. {ECO:0000269|PubMed:23673617}.
-!- PTM: (Microbial infection) Monomeric actin is cross-linked by
V.cholerae toxins RtxA and VgrG1 in case of infection: bacterial
toxins mediate the cross-link between Lys-52 of one monomer and
Glu-272 of another actin monomer, resulting in formation of highly
toxic actin oligomers that cause cell rounding (PubMed:19015515).
The toxin can be highly efficient at very low concentrations by
acting on formin homology family proteins: toxic actin oligomers
bind with high affinity to formins and adversely affect both
nucleation and elongation abilities of formins, causing their
potent inhibition in both profilin-dependent and independent
manners (PubMed:26228148). {ECO:0000305|PubMed:19015515,
ECO:0000305|PubMed:26228148}.
-!- DISEASE: Cardiomyopathy, dilated 1R (CMD1R) [MIM:613424]: A
disorder characterized by ventricular dilation and impaired
systolic function, resulting in congestive heart failure and
arrhythmia. Patients are at risk of premature death.
{ECO:0000269|PubMed:9563954}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Cardiomyopathy, familial hypertrophic 11 (CMH11)
[MIM:612098]: A hereditary heart disorder characterized by
ventricular hypertrophy, which is usually asymmetric and often
involves the interventricular septum. The symptoms include
dyspnea, syncope, collapse, palpitations, and chest pain. They can
be readily provoked by exercise. The disorder has inter- and
intrafamilial variability ranging from benign to malignant forms
with high risk of cardiac failure and sudden cardiac death.
{ECO:0000269|PubMed:10330430, ECO:0000269|PubMed:10966831,
ECO:0000269|PubMed:14729850, ECO:0000269|PubMed:18403758}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Atrial septal defect 5 (ASD5) [MIM:612794]: A congenital
heart malformation characterized by incomplete closure of the wall
between the atria resulting in blood flow from the left to the
right atria. {ECO:0000269|PubMed:17947298}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: In vertebrates 3 main groups of actin isoforms,
alpha, beta and gamma have been identified. The alpha actins are
found in muscle tissues and are a major constituent of the
contractile apparatus. The beta and gamma actins coexist in most
cell types as components of the cytoskeleton and as mediators of
internal cell motility.
-!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; J00073; AAB59619.1; -; Genomic_DNA.
EMBL; J00070; AAB59619.1; JOINED; Genomic_DNA.
EMBL; J00071; AAB59619.1; JOINED; Genomic_DNA.
EMBL; J00072; AAB59619.1; JOINED; Genomic_DNA.
EMBL; CR541795; CAG46594.1; -; mRNA.
EMBL; BC009978; AAH09978.1; -; mRNA.
CCDS; CCDS10041.1; -.
PIR; A02998; ATHUC.
RefSeq; NP_005150.1; NM_005159.4.
UniGene; Hs.118127; -.
ProteinModelPortal; P68032; -.
SMR; P68032; -.
BioGrid; 106585; 45.
IntAct; P68032; 35.
MINT; MINT-1425728; -.
STRING; 9606.ENSP00000290378; -.
iPTMnet; P68032; -.
PhosphoSitePlus; P68032; -.
SwissPalm; P68032; -.
BioMuta; ACTC1; -.
DMDM; 54036697; -.
REPRODUCTION-2DPAGE; P68032; -.
EPD; P68032; -.
MaxQB; P68032; -.
PaxDb; P68032; -.
PeptideAtlas; P68032; -.
PRIDE; P68032; -.
TopDownProteomics; P68032; -.
DNASU; 70; -.
Ensembl; ENST00000290378; ENSP00000290378; ENSG00000159251.
GeneID; 70; -.
KEGG; hsa:70; -.
UCSC; uc001ziu.2; human.
CTD; 70; -.
DisGeNET; 70; -.
EuPathDB; HostDB:ENSG00000159251.6; -.
GeneCards; ACTC1; -.
GeneReviews; ACTC1; -.
HGNC; HGNC:143; ACTC1.
HPA; CAB003761; -.
HPA; CAB037330; -.
HPA; HPA041264; -.
HPA; HPA041271; -.
MalaCards; ACTC1; -.
MIM; 102540; gene.
MIM; 612098; phenotype.
MIM; 612794; phenotype.
MIM; 613424; phenotype.
neXtProt; NX_P68032; -.
OpenTargets; ENSG00000159251; -.
Orphanet; 99103; Atrial septal defect, ostium secundum type.
Orphanet; 154; Familial isolated dilated cardiomyopathy.
Orphanet; 155; Familial isolated hypertrophic cardiomyopathy.
Orphanet; 54260; Left ventricular noncompaction.
PharmGKB; PA162375571; -.
eggNOG; KOG0676; Eukaryota.
eggNOG; COG5277; LUCA.
GeneTree; ENSGT00760000118957; -.
HOGENOM; HOG000233340; -.
HOVERGEN; HBG003771; -.
InParanoid; P68032; -.
KO; K12314; -.
OMA; INRIDMA; -.
OrthoDB; EOG091G08LD; -.
PhylomeDB; P68032; -.
TreeFam; TF354237; -.
Reactome; R-HSA-390522; Striated Muscle Contraction.
SignaLink; P68032; -.
GeneWiki; ACTC1; -.
GenomeRNAi; 70; -.
PRO; PR:P68032; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000159251; -.
CleanEx; HS_ACTC1; -.
Genevisible; P68032; HS.
GO; GO:0005884; C:actin filament; IDA:UniProtKB.
GO; GO:0042643; C:actomyosin, actin portion; IDA:UniProtKB.
GO; GO:0072562; C:blood microparticle; IDA:UniProtKB.
GO; GO:0044297; C:cell body; ISS:AgBase.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0030175; C:filopodium; ISS:AgBase.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0031674; C:I band; ISS:UniProtKB.
GO; GO:0030027; C:lamellipodium; ISS:AgBase.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0030017; C:sarcomere; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
GO; GO:0016887; F:ATPase activity; IDA:UniProtKB.
GO; GO:0017022; F:myosin binding; IDA:BHF-UCL.
GO; GO:0030048; P:actin filament-based movement; IDA:UniProtKB.
GO; GO:0033275; P:actin-myosin filament sliding; IMP:BHF-UCL.
GO; GO:0031032; P:actomyosin structure organization; ISS:UniProtKB.
GO; GO:0006915; P:apoptotic process; ISS:UniProtKB.
GO; GO:0060048; P:cardiac muscle contraction; IEA:Ensembl.
GO; GO:0055008; P:cardiac muscle tissue morphogenesis; ISS:UniProtKB.
GO; GO:0055003; P:cardiac myofibril assembly; ISS:UniProtKB.
GO; GO:0060047; P:heart contraction; IMP:UniProtKB.
GO; GO:0090131; P:mesenchyme migration; ISS:AgBase.
GO; GO:0030049; P:muscle filament sliding; TAS:Reactome.
GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
GO; GO:0010628; P:positive regulation of gene expression; ISS:AgBase.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
GO; GO:0030240; P:skeletal muscle thin filament assembly; ISS:UniProtKB.
InterPro; IPR004000; Actin.
InterPro; IPR020902; Actin/actin-like_CS.
InterPro; IPR004001; Actin_CS.
PANTHER; PTHR11937; PTHR11937; 1.
Pfam; PF00022; Actin; 1.
PRINTS; PR00190; ACTIN.
SMART; SM00268; ACTIN; 1.
PROSITE; PS00406; ACTINS_1; 1.
PROSITE; PS00432; ACTINS_2; 1.
PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
1: Evidence at protein level;
ATP-binding; Atrial septal defect; Cardiomyopathy; Complete proteome;
Cytoplasm; Cytoskeleton; Disease mutation; Isopeptide bond;
Methylation; Muscle protein; Nucleotide-binding; Oxidation;
Reference proteome.
PROPEP 1 2 Removed in mature form. {ECO:0000250}.
/FTId=PRO_0000000812.
CHAIN 3 377 Actin, alpha cardiac muscle 1.
/FTId=PRO_0000000813.
MOD_RES 46 46 Methionine (R)-sulfoxide. {ECO:0000250}.
MOD_RES 49 49 Methionine (R)-sulfoxide. {ECO:0000250}.
MOD_RES 75 75 Tele-methylhistidine.
{ECO:0000250|UniProtKB:P62739}.
MOD_RES 86 86 N6-methyllysine.
{ECO:0000269|PubMed:23673617}.
CROSSLNK 52 52 Isoglutamyl lysine isopeptide (Lys-Glu)
(interchain with E-272); by Vibrio toxins
RtxA and VgrG1.
{ECO:0000250|UniProtKB:P60709}.
CROSSLNK 272 272 Isoglutamyl lysine isopeptide (Glu-Lys)
(interchain with K-52); by Vibrio toxins
RtxA and VgrG1.
{ECO:0000250|UniProtKB:P60709}.
VARIANT 90 90 H -> Y (in CMH11; dbSNP:rs121912676).
{ECO:0000269|PubMed:18403758}.
/FTId=VAR_045924.
VARIANT 97 97 R -> C (in CMH11; dbSNP:rs759495229).
{ECO:0000269|PubMed:18403758}.
/FTId=VAR_045925.
VARIANT 101 101 E -> K (in CMH11; dbSNP:rs193922680).
{ECO:0000269|PubMed:10966831}.
/FTId=VAR_012857.
VARIANT 125 125 M -> V (in ASD5; reduced affinity for
myosin; normal actin filament
polymerization ability; normal actomyosin
motor function; dbSNP:rs121912677).
{ECO:0000269|PubMed:17947298}.
/FTId=VAR_046502.
VARIANT 166 166 P -> A (in CMH11; dbSNP:rs267606628).
{ECO:0000269|PubMed:10966831}.
/FTId=VAR_012858.
VARIANT 168 168 Y -> C (in CMH11).
{ECO:0000269|PubMed:14729850}.
/FTId=VAR_046503.
VARIANT 297 297 A -> S (in CMH11; dbSNP:rs121912675).
{ECO:0000269|PubMed:10330430}.
/FTId=VAR_012859.
VARIANT 307 307 M -> L (in CMH11).
{ECO:0000269|PubMed:14729850}.
/FTId=VAR_046504.
VARIANT 314 314 R -> H (in CMD1R; dbSNP:rs121912673).
{ECO:0000269|PubMed:9563954}.
/FTId=VAR_012860.
VARIANT 333 333 A -> P (in CMH11; dbSNP:rs267606629).
{ECO:0000269|PubMed:10966831}.
/FTId=VAR_012861.
VARIANT 363 363 E -> G (in CMD1R; dbSNP:rs121912674).
{ECO:0000269|PubMed:9563954}.
/FTId=VAR_012862.
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


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