ACT2_XENLA
ID ACT2_XENLA Reviewed; 377 AA.
AC P10995; A9ULV6; Q6GNN1;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Actin, alpha skeletal muscle 2;
DE AltName: Full=Actin alpha 2;
DE Short=alpha2;
DE Short=alpha2p;
DE Flags: Precursor;
GN Name=act2;
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], AND TISSUE SPECIFICITY.
RX PubMed=3653078; DOI=10.1002/j.1460-2075.1987.tb02462.x;
RA Stutz F., Spohr G.;
RT "A processed gene coding for a sarcomeric actin in Xenopus laevis and
RT Xenopus tropicalis.";
RL EMBO J. 6:1989-1995(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tail bud;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP 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 [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 Xenopus laevis actins. In tailbud embryos, expressed in
CC embryonic muscle (myotomes). In tadpoles, abundant in muscle from the
CC tadpole tail with minor expression in the heart and limb buds. In
CC adults, expressed mainly in skeletal muscle.
CC {ECO:0000269|PubMed:3172214, ECO:0000269|PubMed:3653078,
CC 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 promote actin
CC repolymerization (By similarity). {ECO:0000250}.
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; X05392; CAA28979.1; -; Genomic_DNA.
DR EMBL; BC073473; AAH73473.1; -; mRNA.
DR EMBL; BC157412; AAI57413.1; -; mRNA.
DR PIR; A29686; A29686.
DR RefSeq; NP_001090226.1; NM_001096757.1.
DR AlphaFoldDB; P10995; -.
DR SMR; P10995; -.
DR DNASU; 779129; -.
DR GeneID; 779129; -.
DR KEGG; xla:779129; -.
DR CTD; 779129; -.
DR Xenbase; XB-GENE-22064001; mgc75582.S.
DR OMA; QXEREIV; -.
DR OrthoDB; 649708at2759; -.
DR Proteomes; UP000186698; Chromosome 1S.
DR Bgee; 779129; Expressed in muscle tissue and 14 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 PROPEP 1..2
FT /note="Removed in mature form"
FT /id="PRO_0000000822"
FT CHAIN 3..377
FT /note="Actin, alpha skeletal muscle 2"
FT /id="PRO_0000000823"
FT MOD_RES 3
FT /note="N-acetylaspartate"
FT /evidence="ECO:0000250"
FT MOD_RES 46
FT /note="Methionine (R)-sulfoxide"
FT /evidence="ECO:0000250"
FT MOD_RES 49
FT /note="Methionine (R)-sulfoxide"
FT /evidence="ECO:0000250"
FT MOD_RES 75
FT /note="Tele-methylhistidine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 377 AA; 41989 MW; 049CA46921D9BBCF CRC64;
MCDDDETTAL 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 MESAGIHETA YNSIMKCDID IRKDLYANNV
LSGGTTMYPG IADRMQKEIT ALAPSTMKIK IIAPPERKYS VWIGGSILAS LSTFQQMWIT
KQEYDEAGPS IVHRKCF
