ACT2_BACDO
ID ACT2_BACDO Reviewed; 376 AA.
AC P45885;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Actin-2, muscle-specific;
DE Flags: Precursor;
OS Bactrocera dorsalis (Oriental fruit fly) (Dacus dorsalis).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Tephritoidea;
OC Tephritidae; Bactrocera; Bactrocera.
OX NCBI_TaxID=27457;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Puna;
RX PubMed=7951267; DOI=10.1016/0965-1748(94)90018-3;
RA He M., Haymer D.S.;
RT "The actin gene family in the oriental fruit fly Bactrocera dorsalis.
RT Muscle specific actins.";
RL Insect Biochem. Mol. Biol. 24:891-906(1994).
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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- TISSUE SPECIFICITY: Muscle.
CC -!- PTM: Oxidation of Met-45 to form methionine sulfoxide promotes actin
CC filament depolymerization. Methionine sulfoxide is produced
CC stereospecifically, but it is not known whether the (S)-S-oxide or the
CC (R)-S-oxide is produced (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
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DR EMBL; L12254; AAA62342.1; -; Genomic_DNA.
DR RefSeq; XP_011202215.1; XM_011203913.2.
DR AlphaFoldDB; P45885; -.
DR SMR; P45885; -.
DR GeneID; 105225453; -.
DR Proteomes; UP000504616; 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 Acetylation; ATP-binding; Cytoplasm; Cytoskeleton; Muscle protein;
KW Nucleotide-binding; Oxidation; Reference proteome.
FT PROPEP 1..2
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000000616"
FT CHAIN 3..376
FT /note="Actin-2, muscle-specific"
FT /id="PRO_0000000617"
FT MOD_RES 3
FT /note="N-acetylaspartate"
FT /evidence="ECO:0000250"
FT MOD_RES 45
FT /note="Methionine sulfoxide"
FT /evidence="ECO:0000250"
FT MOD_RES 48
FT /note="Methionine sulfoxide"
FT /evidence="ECO:0000250"
SQ SEQUENCE 376 AA; 41803 MW; 7BA03B70CD2A5DEB CRC64;
MCDDEVAALV VDNGSGMCKA GFAGDDAPRA VFPSIVGRPR HQGVMVGMGQ KDSYVGDEAQ
SKRGILTLKY PIEHGIITNW DDMEKIWHHT FYNELRVAPE EHPVLLTEAP LNPKANREKM
TQIMFETFNS PAMYVAIQAV LSLYASGRTT GIVLDSGDGV SHTVPIYEGY ALPHAILRLD
LAGRDLTDYL MKILTERGYS FTTTAEREIV RDIKEKLCYV ALDFEQEMAT AAASTSLEKS
YELPDGQVIT IGNERFRCPE SLFQPSFLGM ESSGIHETVY NSIMKCDVDI RKDLYANIVM
SGGTTMYPGI ADRMQKEITA LAPSTIKIKI IAPPERKYSV WIGGSILASL STFQQMWISK
EEYDESGPGI VHRKCF