ACT3_XENLA
ID ACT3_XENLA Reviewed; 377 AA.
AC P04752; B7ZR72; Q5D0D1;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Actin, alpha skeletal muscle 3;
DE AltName: Full=Actin alpha 3;
DE AltName: Full=Femoral (alpha 3) actin;
DE Contains:
DE RecName: Full=Actin, alpha skeletal muscle 3, intermediate form;
DE Flags: Precursor;
GN Name=act3;
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Oocyte, and Tail bud;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
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 exclusively in skeletal muscle.
CC {ECO:0000269|PubMed:3172214}.
CC -!- DEVELOPMENTAL STAGE: First expressed after neurulation (stage 18), and
CC expressed throughout development. {ECO:0000269|PubMed:3172214}.
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:P68134}.
CC -!- PTM: Monomethylation at Lys-86 (K84me1) 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:P68133}.
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: PubMed:3172214 suggest that the sequences isolated in
CC PubMed:3009830 (alpha3-II) and PubMed:3172214 (alpha3-I) may represent
CC paralogous genes in tetraploid Xenopus laevis.
CC -!- MISCELLANEOUS: The cardiac versus skeletal expression patterns of
CC actins are probably sequence-dependent; Xenopus cardiac actins contain
CC a Glu at position 3 of the mature peptide, whereas skeletal actins
CC contain an Asp at this position.
CC -!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
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DR EMBL; X03470; CAA27187.1; -; mRNA.
DR EMBL; X12525; CAA31041.1; -; Genomic_DNA.
DR EMBL; BC041199; AAH41199.1; -; mRNA.
DR EMBL; BC170065; AAI70065.1; -; mRNA.
DR PIR; B24848; B24848.
DR RefSeq; NP_001082366.1; NM_001088897.2.
DR RefSeq; NP_001090199.1; NM_001096730.1.
DR AlphaFoldDB; P04752; -.
DR SMR; P04752; -.
DR PRIDE; P04752; -.
DR DNASU; 398426; -.
DR GeneID; 398426; -.
DR GeneID; 779096; -.
DR KEGG; xla:398426; -.
DR KEGG; xla:779096; -.
DR CTD; 398426; -.
DR CTD; 779096; -.
DR Xenbase; XB-GENE-6253091; acta4.L.
DR Xenbase; XB-GENE-6256329; acta4.S.
DR OrthoDB; 649708at2759; -.
DR Proteomes; UP000186698; Chromosome 4L.
DR Proteomes; UP000186698; Chromosome 4S.
DR Bgee; 398426; Expressed in muscle tissue and 15 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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 skeletal muscle 3, intermediate form"
FT /evidence="ECO:0000250|UniProtKB:P62737"
FT /id="PRO_0000442831"
FT CHAIN 3..377
FT /note="Actin, alpha skeletal muscle 3"
FT /evidence="ECO:0000250|UniProtKB:P62737"
FT /id="PRO_0000442832"
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 skeletal muscle
FT 3"
FT /evidence="ECO:0000250|UniProtKB:P68135"
FT MOD_RES 46
FT /note="Methionine (R)-sulfoxide"
FT /evidence="ECO:0000250|UniProtKB:P68134"
FT MOD_RES 49
FT /note="Methionine (R)-sulfoxide"
FT /evidence="ECO:0000250|UniProtKB:P68134"
FT MOD_RES 75
FT /note="Tele-methylhistidine"
FT /evidence="ECO:0000250|UniProtKB:P68135"
FT MOD_RES 86
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:P68133"
SQ SEQUENCE 377 AA; 41984 MW; 7FBE432AA278F915 CRC64;
MCDDDETTAL VCDNGSGLVK AGFAGDDAPR AVFPSIVGRP RHQGVMVGMG QKDSYVGDEA
QSKRGILTLK YPIEHGIITN WDDMEKIWHH TFYNELRVAP EEHPTLLTEA PLNPKANREK
MTQIMFETFN VPAMYVAIQA VLSLYASGRT TGIVLDSGDG VTHNVPIYEG YALPHAIQRL
DLAGRDLTDY LMKILTERGY SFVTTAEREI VRDIKEKLAY VALDFENEMA TAASSSSLEK
SYELPDGQVI TIGNERFRCP ETLFQPSFIG MESAGIHETT YNSIMKCDID IRKDLYANNV
LSGGTTMYPG IADRMQKEIT ALAPSTMKIK IIAPPERKYS VWIGGSILAS LSTFQQMWIT
KQEYDEAGPS IVHRKCF
