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Actin, alpha cardiac muscle 1 (Alpha-cardiac actin) [Cleaved into: Actin, alpha cardiac muscle 1, intermediate form]

 ACTC_MOUSE              Reviewed;         377 AA.
P68033; P04270;
20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
20-MAR-1987, sequence version 1.
05-DEC-2018, entry version 121.
RecName: Full=Actin, alpha cardiac muscle 1;
AltName: Full=Alpha-cardiac actin;
Contains:
RecName: Full=Actin, alpha cardiac muscle 1, intermediate form;
Flags: Precursor;
Name=Actc1; Synonyms=Actc;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Head;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Limb;
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).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 3-377.
PubMed=3028523; DOI=10.1007/BF01116542;
Leader D.P., Gall I., Campbell P.C.;
"The structure of a cDNA clone corresponding to mouse cardiac muscle
actin mRNA.";
Biosci. Rep. 6:741-747(1986).
[4]
PROTEIN SEQUENCE OF 71-97 AND 241-256, AND IDENTIFICATION BY MASS
SPECTROMETRY.
STRAIN=OF1; TISSUE=Hippocampus;
Lubec G., Sunyer B., Chen W.-Q.;
Submitted (JAN-2009) to UniProtKB.
[5]
OXIDATION AT MET-46 AND MET-49, AND DEOXIDATION AT MET-46 AND MET-49.
PubMed=23911929; DOI=10.1016/j.molcel.2013.06.019;
Lee B.C., Peterfi Z., Hoffmann F.W., Moore R.E., Kaya A., Avanesov A.,
Tarrago L., Zhou Y., Weerapana E., Fomenko D.E., Hoffmann P.R.,
Gladyshev V.N.;
"MsrB1 and MICALs regulate actin assembly and macrophage function via
reversible stereoselective methionine oxidation.";
Mol. Cell 51:397-404(2013).
-!- 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.
-!- INTERACTION:
O70468:Mybpc3; NbExp=3; IntAct=EBI-352284, EBI-8347074;
-!- 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
promotes actin repolymerization. {ECO:0000269|PubMed:23911929}.
-!- PTM: Monomethylation at Lys-86 (K86me1) 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:0000250|UniProtKB:P68032}.
-!- 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; AK014303; BAB29258.1; -; mRNA.
EMBL; BC062138; AAH62138.1; -; mRNA.
EMBL; M15501; AAA37167.1; -; mRNA.
CCDS; CCDS16564.1; -.
PIR; A54728; A54728.
RefSeq; NP_033738.1; NM_009608.4.
UniGene; Mm.686; -.
ProteinModelPortal; P68033; -.
SMR; P68033; -.
BioGrid; 197945; 6.
IntAct; P68033; 4.
STRING; 10090.ENSMUSP00000087736; -.
iPTMnet; P68033; -.
PhosphoSitePlus; P68033; -.
SwissPalm; P68033; -.
PaxDb; P68033; -.
PeptideAtlas; P68033; -.
PRIDE; P68033; -.
Ensembl; ENSMUST00000090269; ENSMUSP00000087736; ENSMUSG00000068614.
GeneID; 11464; -.
KEGG; mmu:11464; -.
UCSC; uc008lpz.1; mouse.
CTD; 70; -.
MGI; MGI:87905; Actc1.
eggNOG; KOG0676; Eukaryota.
eggNOG; COG5277; LUCA.
GeneTree; ENSGT00940000154710; -.
HOGENOM; HOG000233340; -.
HOVERGEN; HBG003771; -.
InParanoid; P68033; -.
KO; K12314; -.
OMA; KCDESIC; -.
OrthoDB; EOG091G08LD; -.
PhylomeDB; P68033; -.
TreeFam; TF354237; -.
Reactome; R-MMU-390522; Striated Muscle Contraction.
ChiTaRS; Actc1; mouse.
PRO; PR:P68033; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000068614; Expressed in 303 organ(s), highest expression level in heart left ventricle.
CleanEx; MM_ACTC1; -.
ExpressionAtlas; P68033; baseline and differential.
Genevisible; P68033; MM.
GO; GO:0005884; C:actin filament; ISO:MGI.
GO; GO:0042643; C:actomyosin, actin portion; ISO:MGI.
GO; GO:0044297; C:cell body; ISS:AgBase.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0030175; C:filopodium; ISS:AgBase.
GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
GO; GO:0031674; C:I band; IDA:MGI.
GO; GO:0030027; C:lamellipodium; ISS:AgBase.
GO; GO:0030017; C:sarcomere; ISO:MGI.
GO; GO:0045202; C:synapse; IDA:SynGO.
GO; GO:0005524; F:ATP binding; ISO:MGI.
GO; GO:0016887; F:ATPase activity; ISO:MGI.
GO; GO:0017022; F:myosin binding; ISO:MGI.
GO; GO:0030048; P:actin filament-based movement; ISO:MGI.
GO; GO:0070252; P:actin-mediated cell contraction; IMP:MGI.
GO; GO:0033275; P:actin-myosin filament sliding; ISO:MGI.
GO; GO:0031032; P:actomyosin structure organization; IMP:MGI.
GO; GO:0060048; P:cardiac muscle contraction; ISO:MGI.
GO; GO:0055008; P:cardiac muscle tissue morphogenesis; IMP:MGI.
GO; GO:0055003; P:cardiac myofibril assembly; IMP:MGI.
GO; GO:0060047; P:heart contraction; ISO:MGI.
GO; GO:0090131; P:mesenchyme migration; ISS:AgBase.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
GO; GO:0010628; P:positive regulation of gene expression; ISS:AgBase.
GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
GO; GO:0030240; P:skeletal muscle thin filament assembly; IMP:MGI.
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;
Acetylation; ATP-binding; Complete proteome; Cytoplasm; Cytoskeleton;
Direct protein sequencing; Methylation; Muscle protein;
Nucleotide-binding; Oxidation; Reference proteome.
INIT_MET 1 1 Removed.
CHAIN 2 377 Actin, alpha cardiac muscle 1,
intermediate form.
{ECO:0000250|UniProtKB:P62737}.
/FTId=PRO_0000442999.
CHAIN 3 377 Actin, alpha cardiac muscle 1.
{ECO:0000250|UniProtKB:P68135}.
/FTId=PRO_0000000815.
MOD_RES 2 2 N-acetylcysteine; in intermediate form.
{ECO:0000250|UniProtKB:P62737}.
MOD_RES 46 46 Methionine (R)-sulfoxide.
{ECO:0000269|PubMed:23911929}.
MOD_RES 49 49 Methionine (R)-sulfoxide.
{ECO:0000269|PubMed:23911929}.
MOD_RES 75 75 Tele-methylhistidine.
{ECO:0000250|UniProtKB:P62739}.
MOD_RES 86 86 N6-methyllysine.
{ECO:0000250|UniProtKB:P68032}.
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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