ID   ACTM_APLCA              Reviewed;         376 AA.
AC   P17304;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Actin, muscle;
DE   Flags: Precursor;
OS   Aplysia californica (California sea hare).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Heterobranchia; Euthyneura; Tectipleura; Aplysiida; Aplysioidea;
OC   Aplysiidae; Aplysia.
OX   NCBI_TaxID=6500;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Muscle;
RX   PubMed=2362821; DOI=10.1093/nar/18.12.3654;
RA   Desgroseillers L., Auclair D., Wickham L.;
RT   "Nucleotide sequence of an actin cDNA gene from Aplysia californica.";
RL   Nucleic Acids Res. 18:3654-3654(1990).
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   -!- TISSUE SPECIFICITY: Expressed in the muscular cells of the sheath
CC       surrounding abdominal ganglions.
CC   -!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X52868; CAA37049.1; -; mRNA.
DR   PIR; S12730; S12730.
DR   RefSeq; NP_001191580.1; NM_001204651.1.
DR   AlphaFoldDB; P17304; -.
DR   SMR; P17304; -.
DR   PRIDE; P17304; -.
DR   GeneID; 100533357; -.
DR   OrthoDB; 649708at2759; -.
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.
FT   PROPEP          1..2
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000000608"
FT   CHAIN           3..376
FT                   /note="Actin, muscle"
FT                   /id="PRO_0000000609"
FT   MOD_RES         3
FT                   /note="N-acetylaspartate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   376 AA;  41766 MW;  B33A6CBA030D0C96 CRC64;
     MCDDEVAALV VDNGSGMCKA GFAGDDAPRA VFPSIVGRPR HQGVMVGMGQ KDSYVGDEAQ
     SKRGILTLKY PIEHGIVTNW DDMEKIWHHT FYNELRVPPE EHPVLLTEAP LNPKANREKM
     TQIMFETFNA PAMYVAIQAV LSLYASGRTT GIVLDSGDGV THTVPIYEGY ALPHAILRLD
     LAGRDLTDYL SKILTERGYS FTTTAEREIV RDIKEKLCYV ALDFEQEMAT AASSSSLEKS
     YELPDGQVIT IGNERFRCPE SLFQPILLGM ESAGIHETTY NSIMKCDVDI RKDLYANTVL
     SGGTTMFPGI ADRMQKEITS LAPSTMKIKI IAPPERKYSV WIGGSILASL STFQQMWISK
     QEYDESGPSI VHRKCF