ACT3_XENTR
ID ACT3_XENTR Reviewed; 377 AA.
AC Q6P8G3;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Actin, alpha sarcomeric/skeletal {ECO:0000250|UniProtKB:P04752};
DE AltName: Full=Actin alpha 3 {ECO:0000250|UniProtKB:P04752};
DE Flags: Precursor;
GN Name=act3 {ECO:0000312|Xenbase:XB-GENE-6469705}; ORFNames=TNeu071i12.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1] {ECO:0000312|EMBL:CAJ82467.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Neurula {ECO:0000312|EMBL:CAJ82467.1};
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|EMBL:CAJ82467.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tadpole {ECO:0000312|EMBL:AAH61264.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL 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).
CC -!- FUNCTION: Actins are highly conserved proteins that are involved in
CC various types of cell motility. {ECO:0000305}.
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. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: In tailbud embryos, expressed in embryonic muscle
CC (myotomes). {ECO:0000269|PubMed:3172214}.
CC -!- DEVELOPMENTAL STAGE: Unlike Xenopus laevis act3, expression is
CC restricted to embryonic and tadpole stages. Not expressed in adults.
CC {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 promote actin
CC repolymerization (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: Xenopus contains at least three different sarcomeric
CC alpha actin genes that are preferentially expressed in either heart or
CC skeletal muscle. {ECO:0000305}.
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. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the actin family. {ECO:0000255}.
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DR EMBL; CR760277; CAJ82467.1; -; mRNA.
DR EMBL; BC061264; AAH61264.1; -; mRNA.
DR RefSeq; NP_989076.1; NM_203745.1.
DR AlphaFoldDB; Q6P8G3; -.
DR SMR; Q6P8G3; -.
DR DNASU; 394673; -.
DR Ensembl; ENSXETT00000088760; ENSXETP00000096734; ENSXETG00000002714.
DR GeneID; 394673; -.
DR KEGG; xtr:394673; -.
DR CTD; 394673; -.
DR Xenbase; XB-GENE-6469705; acta4.
DR InParanoid; Q6P8G3; -.
DR OrthoDB; 649708at2759; -.
DR Proteomes; UP000008143; Chromosome 4.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000002714; Expressed in neurula embryo and 11 other tissues.
DR ExpressionAtlas; Q6P8G3; baseline.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005869; C:dynactin complex; IBA:GO_Central.
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 /evidence="ECO:0000250|UniProtKB:P68138"
FT /id="PRO_0000399457"
FT CHAIN 3..377
FT /note="Actin, alpha sarcomeric/skeletal"
FT /evidence="ECO:0000250|UniProtKB:P68138"
FT /id="PRO_0000399458"
FT MOD_RES 3
FT /note="N-acetylaspartate"
FT /evidence="ECO:0000250|UniProtKB:P68138"
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|UniProtKB:P68138"
SQ SEQUENCE 377 AA; 41984 MW; DF99432AA27DF946 CRC64;
MCDDDETTAL VCDNGSGLVK AGFAGDDAPR AVFPSIVGRP RHQGVMVGMG QKDSYVGDEA
QSKRGILTLK YPIEHGIITN WDDMEKIWHH TFYNELRVAP EEHPTLLTEA PLNPKANREK
MTQIMFETFN VPAMYVAIQA VLSLYASGRT TGIVLDSGDG VTHNVPIYEG YALPHAIQRL
DLAGRDLTDY LMKILTERGY SFVTTAEREI VRDIKEKLAY VALDFENEMA TAATSSSLEK
SYELPDGQVI TIGNERFRCP ETLFQPSFIG MESAGIHETT YNSIMKCDID IRKDLYANNV
LSGGTTMYPG IADRMQKEIT ALAPSTMKIK IIAPPERKYS VWIGGSILAS LSTFQQMWIS
KQEYDEAGPS IVHRKCF
