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

 ACTC_XENLA              Reviewed;         377 AA.
P04751; Q6AZU8;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
13-AUG-1987, sequence version 1.
28-FEB-2018, entry version 97.
RecName: Full=Actin, alpha cardiac muscle 1;
AltName: Full=Actin alpha 1;
AltName: Full=Alpha-cardiac actin;
Contains:
RecName: Full=Actin, alpha cardiac muscle 1, intermediate form;
Flags: Precursor;
Name=actc1; Synonyms=acta1, actc;
Xenopus laevis (African clawed frog).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
Xenopus.
NCBI_TaxID=8355;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3816759;
Mohun T.J., Garrett N., Gurdon J.B.;
"Upstream sequences required for tissue-specific activation of the
cardiac actin gene in Xenopus laevis embryos.";
EMBO J. 5:3185-3193(1986).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF
1-43.
PubMed=3009830; DOI=10.1016/0022-2836(86)90438-9;
Stutz F., Spohr G.;
"Isolation and characterization of sarcomeric actin genes expressed in
Xenopus laevis embryos.";
J. Mol. Biol. 187:349-361(1986).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Embryo, and Heart;
NIH - Xenopus Gene Collection (XGC) project;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=6548550; DOI=10.1038/311716a0;
Mohun T.J., Brennan S., Dathan N., Fairman S., Gurdon J.B.;
"Cell type-specific activation of actin genes in the early amphibian
embryo.";
Nature 311:716-721(1984).
[5]
TISSUE SPECIFICITY.
PubMed=3172214; DOI=10.1016/0022-2836(88)90519-0;
Mohun T.J., Garrett N., Stutz F., Spohr G.;
"A third striated muscle actin gene is expressed during early
development in the amphibian Xenopus laevis.";
J. Mol. Biol. 202:67-76(1988).
-!- FUNCTION: Actins are highly conserved proteins that are involved
in various types of cell motility.
-!- 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.
-!- TISSUE SPECIFICITY: Shows overlapping but distinct expression
patterns with other actins. In tailbud embryos, expressed in
embryonic muscle (myotomes). In adults, expressed only in heart
muscle. {ECO:0000269|PubMed:3172214, ECO:0000269|PubMed:6548550}.
-!- DEVELOPMENTAL STAGE: Expressed from the end of gastrulation.
{ECO:0000269|PubMed:6548550}.
-!- 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:0000250|UniProtKB:P68033}.
-!- 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: Xenopus contains at least three sarcomeric alpha
actin genes that are preferentially expressed in either heart or
skeletal muscle. Due to the tetraploid nature of Xenopus laevis,
each of these three alpha actin genes is present in at least two
copies.
-!- MISCELLANEOUS: The cardiac versus skeletal expression patterns of
actins are probably sequence-dependent. For example, cardiac
actins contain a Glu at position 3 of the mature peptide, whereas
skeletal actins contain an Asp at this position.
-!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
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EMBL; X04669; CAA28375.1; -; Genomic_DNA.
EMBL; X03469; CAA27186.1; -; mRNA.
EMBL; BC041197; AAH41197.1; -; mRNA.
EMBL; BC077221; AAH77221.1; -; mRNA.
EMBL; BC099316; AAH99316.1; -; mRNA.
PIR; A25705; A24848.
RefSeq; NP_001080060.1; NM_001086591.2.
RefSeq; XP_018084109.1; XM_018228620.1.
UniGene; Xl.1115; -.
ProteinModelPortal; P04751; -.
SMR; P04751; -.
PRIDE; P04751; -.
GeneID; 379752; -.
KEGG; xla:379752; -.
CTD; 379752; -.
Xenbase; XB-GENE-865367; actc1.
HOVERGEN; HBG003771; -.
KO; K12314; -.
GO; GO:0044297; C:cell body; ISS:AgBase.
GO; GO:0005737; C:cytoplasm; ISS:AgBase.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0030175; C:filopodium; ISS:AgBase.
GO; GO:0030027; C:lamellipodium; ISS:AgBase.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0090131; P:mesenchyme migration; ISS:AgBase.
GO; GO:0010628; P:positive regulation of gene expression; ISS:AgBase.
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.
2: Evidence at transcript level;
Acetylation; ATP-binding; Cytoplasm; Cytoskeleton; Methylation;
Muscle protein; Nucleotide-binding; Oxidation.
INIT_MET 1 1 Removed.
CHAIN 2 377 Actin, alpha cardiac muscle 1,
intermediate form.
{ECO:0000250|UniProtKB:P62737}.
/FTId=PRO_0000443002.
CHAIN 3 377 Actin, alpha cardiac muscle 1.
{ECO:0000250|UniProtKB:P68135}.
/FTId=PRO_0000000821.
MOD_RES 2 2 N-acetylcysteine; in intermediate form.
{ECO:0000250|UniProtKB:P62737}.
MOD_RES 3 3 N-acetylaspartate; in Actin, alpha
cardiac muscle 1.
{ECO:0000250|UniProtKB:P68135}.
MOD_RES 46 46 Methionine (R)-sulfoxide.
{ECO:0000250|UniProtKB:P68033}.
MOD_RES 49 49 Methionine (R)-sulfoxide.
{ECO:0000250|UniProtKB:P68033}.
MOD_RES 75 75 Tele-methylhistidine.
{ECO:0000250|UniProtKB:P62739}.
MOD_RES 86 86 N6-methyllysine.
{ECO:0000250|UniProtKB:P68032}.
SEQUENCE 377 AA; 42016 MW; C3E276EFA11CD1B5 CRC64;
MCDDEETTAL VCDNGSGLVK AGFAGDDAPR AVFPSIVGRP RHQGVMVGMG QKDSYVGDEA
QSKRGILTLK YPIEHGIITN WDDMEKIWHH TFYNELRVAP EEHPTLLTEA PLNPKANREK
MTQIMFETFN VPAMYVAIQA VLSLYASGRT TGIVLDSGDG VTHNVPIYEG YALPHAIQRL
DLAGRDLTDY LMKILTERGY SFVTTAEREI VRDIKEKLCY VALDFENEMA TAASSSSLEK
SYELPDGQVI TIGNERFRCP ETLFQPSFIG MESAGIHETT YNSIMKCDID IRKDLYANNV
LSGGTTMYPG IADRMQKEIT ALAPSTMKIK IIAPPERKYS VWIGGSILAS LSTFQQMWIS
KQEYDEAGPS IVHRKCF


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