ACTC_XENLA
ID ACTC_XENLA Reviewed; 377 AA.
AC P04751; Q6AZU8;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Actin, alpha cardiac muscle 1;
DE AltName: Full=Actin alpha 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=acta1, actc;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3816759; DOI=10.1002/j.1460-2075.1986.tb04628.x;
RA Mohun T.J., Garrett N., Gurdon J.B.;
RT "Upstream sequences required for tissue-specific activation of the cardiac
RT actin gene in Xenopus laevis embryos.";
RL EMBO J. 5:3185-3193(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-43.
RX PubMed=3009830; DOI=10.1016/0022-2836(86)90438-9;
RA Stutz F., Spohr G.;
RT "Isolation and characterization of sarcomeric actin genes expressed in
RT Xenopus laevis embryos.";
RL J. Mol. Biol. 187:349-361(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo, and Heart;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=6548550; DOI=10.1038/311716a0;
RA Mohun T.J., Brennan S., Dathan N., Fairman S., Gurdon J.B.;
RT "Cell type-specific activation of actin genes in the early amphibian
RT embryo.";
RL Nature 311:716-721(1984).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=3172214; DOI=10.1016/0022-2836(88)90519-0;
RA Mohun T.J., Garrett N., Stutz F., Spohr G.;
RT "A third striated muscle actin gene is expressed during early development
RT in the amphibian Xenopus laevis.";
RL J. Mol. Biol. 202:67-76(1988).
CC -!- FUNCTION: Actins are highly conserved proteins that are involved in
CC various types of cell motility.
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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- TISSUE SPECIFICITY: Shows overlapping but distinct expression patterns
CC with other actins. In tailbud embryos, expressed in embryonic muscle
CC (myotomes). In adults, expressed only in heart muscle.
CC {ECO:0000269|PubMed:3172214, ECO:0000269|PubMed:6548550}.
CC -!- DEVELOPMENTAL STAGE: Expressed from the end of gastrulation.
CC {ECO:0000269|PubMed:6548550}.
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:0000250|UniProtKB:P68032}.
CC -!- PTM: Methylated at His-75 by SETD3. {ECO:0000250|UniProtKB:P68032}.
CC -!- MISCELLANEOUS: Xenopus contains at least three sarcomeric alpha actin
CC genes that are preferentially expressed in either heart or skeletal
CC muscle. Due to the tetraploid nature of Xenopus laevis, each of these
CC three alpha actin genes is present in at least two copies.
CC -!- MISCELLANEOUS: The cardiac versus skeletal expression patterns of
CC actins are probably sequence-dependent. For example, cardiac actins
CC contain a Glu at position 3 of the mature peptide, whereas skeletal
CC actins contain an Asp at this position.
CC -!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
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DR EMBL; X04669; CAA28375.1; -; Genomic_DNA.
DR EMBL; X03469; CAA27186.1; -; mRNA.
DR EMBL; BC041197; AAH41197.1; -; mRNA.
DR EMBL; BC077221; AAH77221.1; -; mRNA.
DR EMBL; BC099316; AAH99316.1; -; mRNA.
DR PIR; A25705; A24848.
DR RefSeq; NP_001080060.1; NM_001086591.2.
DR RefSeq; XP_018084109.1; XM_018228620.1.
DR AlphaFoldDB; P04751; -.
DR SMR; P04751; -.
DR BioGRID; 97994; 1.
DR DNASU; 379752; -.
DR GeneID; 379752; -.
DR KEGG; xla:379752; -.
DR CTD; 379752; -.
DR Xenbase; XB-GENE-865367; actc1.L.
DR OMA; ACTSIEI; -.
DR OrthoDB; 649708at2759; -.
DR Proteomes; UP000186698; Chromosome 8L.
DR Bgee; 379752; Expressed in neurula embryo and 18 other tissues.
DR GO; GO:0044297; C:cell body; ISS:AgBase.
DR GO; GO:0005737; C:cytoplasm; ISS:AgBase.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0030175; C:filopodium; ISS:AgBase.
DR GO; GO:0030027; C:lamellipodium; ISS:AgBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0090131; P:mesenchyme migration; ISS:AgBase.
DR GO; GO:0010628; P:positive regulation of gene expression; ISS:AgBase.
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 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Cytoplasm; Cytoskeleton; Methylation;
KW Muscle protein; Nucleotide-binding; 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_0000443002"
FT CHAIN 3..377
FT /note="Actin, alpha cardiac muscle 1"
FT /evidence="ECO:0000250|UniProtKB:P68135"
FT /id="PRO_0000000821"
FT MOD_RES 2
FT /note="N-acetylcysteine; in intermediate form"
FT /evidence="ECO:0000250|UniProtKB:P62737"
FT MOD_RES 3
FT /note="N-acetylaspartate; in Actin, alpha cardiac muscle 1"
FT /evidence="ECO:0000250|UniProtKB:P68135"
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:0000250|UniProtKB:P62739"
FT MOD_RES 86
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:P68032"
SQ 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
