ID   ACT2_XENTR              Reviewed;         377 AA.
AC   P20399; Q6GSH4;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Actin, alpha cardiac muscle 2;
DE   AltName: Full=Actin alpha 2;
DE            Short=alpha2T;
DE   Flags: Precursor;
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]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Sarcomere;
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=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (DEC-2003) 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 a different expression pattern to Xenopus
CC       laevis act2. Expressed in stage 24 and 42 embryos as well as in adult
CC       heart, but not adult skeletal muscle. {ECO:0000269|PubMed:3653078}.
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.
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; X05393; CAB43617.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BC064152; AAH64152.1; -; mRNA.
DR   PIR; B29686; B29686.
DR   RefSeq; NP_989355.1; NM_204024.1.
DR   AlphaFoldDB; P20399; -.
DR   SMR; P20399; -.
DR   STRING; 8364.ENSXETP00000046309; -.
DR   PaxDb; P20399; -.
DR   DNASU; 394982; -.
DR   Ensembl; ENSXETT00000016355; ENSXETP00000097660; ENSXETG00000027434.
DR   GeneID; 394982; -.
DR   KEGG; xtr:394982; -.
DR   Xenbase; XB-GENE-22063999; mgc75582.
DR   eggNOG; KOG0676; Eukaryota.
DR   OrthoDB; 177884at2759; -.
DR   PhylomeDB; P20399; -.
DR   Proteomes; UP000008143; Chromosome 1.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000027434; Expressed in skeletal muscle tissue and 6 other tissues.
DR   GO; GO:0044297; C:cell body; ISS:AgBase.
DR   GO; GO:0005737; C:cytoplasm; ISS:AgBase.
DR   GO; GO:0005869; C:dynactin complex; IBA:GO_Central.
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   PROPEP          1..2
FT                   /note="Removed in mature form"
FT                   /id="PRO_0000000824"
FT   CHAIN           3..377
FT                   /note="Actin, alpha cardiac muscle 2"
FT                   /id="PRO_0000000825"
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;  42033 MW;  E5C40FF19730CAD2 CRC64;
     MCDDEETTAL 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 MESAGIHETT YNSIMKCDID IRKDLYANNV
     LSGGTTMYPG IADRMQKEIT ALAPSTMKIK IIAPPERKYS VWIGGSILAS LSTFQQMWIT
     KQEYDEAGPS IVHRKCF