ID   ACTX_TAKRU              Reviewed;         376 AA.
AC   P53483;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Actin, alpha anomalous;
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX   PubMed=8683572; DOI=10.1006/jmbi.1996.0347;
RA   Venkatesh B., Tay B.H., Elgar G., Brenner S.;
RT   "Isolation, characterization and evolution of nine pufferfish (Fugu
RT   rubripes) actin genes.";
RL   J. Mol. Biol. 259:655-665(1996).
CC   -!- FUNCTION: Actins are highly conserved proteins that are involved in
CC       various types of cell motility and are ubiquitously expressed in all
CC       eukaryotic cells.
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: Predominantly expressed in testis.
CC       {ECO:0000269|PubMed:8683572}.
CC   -!- PTM: Oxidation of Met-45 and Met-48 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   -!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
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DR   EMBL; U38962; AAC59897.1; -; Genomic_DNA.
DR   PIR; S71123; S71123.
DR   RefSeq; XP_011617599.1; XM_011619297.1.
DR   AlphaFoldDB; P53483; -.
DR   SMR; P53483; -.
DR   STRING; 31033.ENSTRUP00000013201; -.
DR   PRIDE; P53483; -.
DR   GeneID; 101074318; -.
DR   KEGG; tru:101074318; -.
DR   eggNOG; KOG0676; Eukaryota.
DR   HOGENOM; CLU_027965_0_2_1; -.
DR   InParanoid; P53483; -.
DR   OrthoDB; 649708at2759; -.
DR   TreeFam; TF354237; -.
DR   Proteomes; UP000005226; Unplaced.
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   ATP-binding; Cytoplasm; Cytoskeleton; Nucleotide-binding; Oxidation;
KW   Reference proteome.
FT   CHAIN           1..376
FT                   /note="Actin, alpha anomalous"
FT                   /id="PRO_0000089056"
FT   MOD_RES         45
FT                   /note="Methionine (R)-sulfoxide"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         48
FT                   /note="Methionine (R)-sulfoxide"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   376 AA;  41979 MW;  DB037F47BA1371D8 CRC64;
     MSDYDETALV CDNGSGLVKA GFAGDDTPRA VFHAIVGRPR HQDDMDDMGK KGYYVGDEAQ
     SKRDILSLKH PIERGIITNW DDMEKIWHHT FYNELCVAPE EHPTLLTEAP LNPKANREKM
     TQIMLETFNM PAMYVSIQAV LSLYASGRTT GIVLDSGEGV THAVPIAEGY ALPPAIMRLN
     LAGRDLTDYL MKILNERGYS FVTTAEREIV RDIKEKLCYV ALDFENEMAT AASSSSLEKR
     YELPDGQVIT IGNERFCCPE TLFQPSFMGM ESAGIHEITH SSIMKCDIEI RKDLYANNVL
     TGGATLFPGI ADRMQKEITA LAPSTMKIQI IAPPERKYSV WIGGSILASL STFQQMWISK
     QEYEEIGPSI IHCKCF