ID   ACTM_STYCL              Reviewed;         378 AA.
AC   P26198;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Actin, muscle;
OS   Styela clava (Sea squirt).
OC   Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Stolidobranchia;
OC   Styelidae; Styela.
OX   NCBI_TaxID=7725;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Muscle;
RX   PubMed=8315656; DOI=10.1007/bf00182183;
RA   Kovilur S., Jacobson J.W., Beach R.L., Jeffery W.R., Tomlinson C.R.;
RT   "Evolution of the chordate muscle actin gene.";
RL   J. Mol. Evol. 36:361-368(1993).
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   -!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
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DR   EMBL; X61040; CAA43375.1; -; mRNA.
DR   PIR; S21907; S21907.
DR   AlphaFoldDB; P26198; -.
DR   SMR; P26198; -.
DR   PRIDE; P26198; -.
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; Muscle protein; Nucleotide-binding.
FT   CHAIN           1..378
FT                   /note="Actin, muscle"
FT                   /id="PRO_0000089027"
SQ   SEQUENCE   378 AA;  42067 MW;  6EB5E99FAFBF499E CRC64;
     MSDGEEDQTA IVCDNGSGLV KSGFAGDDAP RAVFPSIVGR PRHQGVMVGM GQKDSYVGDE
     AQSKRGILTL KYPIEHGIIT NWDDMEKIWH HTMYNELRVA PEEHPTLLTE APHNPKANRE
     KMTQIMFETF NVPAMYVAIQ AVLSLYASGR TTGIVMDAGD GVSHNVPIYE GYALPHAIAR
     LDLAGRDLTD YLMKILTERG YSFVTTAERE IVRDIKEKLC YVALDFEQEM ATAASSTSLE
     KSYELPDGQV ITIGNERFRC PETLFQPSFI GMESAGIHET TYNSIMKCDI DIRKDLYANN
     VLSGGTTMYP GIADRMQKEI TALAPSTMKI KIIAPPERKY SVWIGGSILA SLSTFQQMWI
     SKQEYDEAGP SIVHRKCF