ACT1_BOMMO
ID ACT1_BOMMO Reviewed; 376 AA.
AC P07836;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Actin, muscle-type A1;
DE Flags: Precursor;
OS Bombyx mori (Silk moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Bombycidae; Bombycinae; Bombyx.
OX NCBI_TaxID=7091;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=703;
RX PubMed=3562238; DOI=10.1093/nar/15.6.2781;
RA Mounier N., Gaillard J., Prudhomme J.-C.;
RT "Nucleotide sequence of the coding region of two actin genes in Bombyx
RT mori.";
RL Nucleic Acids Res. 15:2781-2781(1987).
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 -!- FUNCTION: Multiple isoforms are involved in various cellular functions
CC such as cytoskeleton structure, cell mobility, chromosome movement and
CC muscle contraction.
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 -!- 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 -!- MISCELLANEOUS: There are at least 5 different actin genes in this
CC organism.
CC -!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
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DR EMBL; X05185; CAA28818.1; -; Genomic_DNA.
DR PIR; S09059; S09059.
DR RefSeq; NP_001119724.1; NM_001126252.1.
DR AlphaFoldDB; P07836; -.
DR SMR; P07836; -.
DR STRING; 7091.BGIBMGA013945-TA; -.
DR GeneID; 100145913; -.
DR KEGG; bmor:100145913; -.
DR CTD; 100145913; -.
DR eggNOG; KOG0676; Eukaryota.
DR HOGENOM; CLU_027965_0_2_1; -.
DR OrthoDB; 649708at2759; -.
DR Proteomes; UP000005204; Unassembled WGS sequence.
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 3: Inferred from homology;
KW Acetylation; ATP-binding; Cytoplasm; Cytoskeleton; Nucleotide-binding;
KW Oxidation; Reference proteome.
FT PROPEP 1..2
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000000632"
FT CHAIN 3..376
FT /note="Actin, muscle-type A1"
FT /id="PRO_0000000633"
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; 41876 MW; 10EF0819B4FE17FB CRC64;
MCDDDVRALV VDNGSGMCKA GFAGDDAPRA VFPSIVGRPR HQGLMVGMGQ KDSYVGDEAQ
SKRGILTLKY PIEHGIITNW DDMEKIWHHT FYNELRVAPE EHPVLLTEAP LNPKANREKM
TQIMFETFNS PAMYVAIQAV LSLYASGRTT GIVLDSGDGV SHTVPIYEGY ALPHAILRLD
LAGRDLTDYL MKILTERGYS FTTTAEREIV RDIKEKLCYV ALDFEQEMAT AAASTSLEKS
YELPDGQVIT IGNERFRCPE ALFQPSFLGM ESCGIHETVY NSIMKCDVDI RKDLYANTVM
SGGTTMYPGI ADRMQKEITA LAPSTIKIKI IAPPERKYSV WIGGSILASL STFQQMWISK
EEYDESGPGI VHRKCF