ID   ACT_PLAMG               Reviewed;         376 AA.
AC   Q26065;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Actin, adductor muscle;
DE   Flags: Precursor;
OS   Placopecten magellanicus (Sea scallop).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC   Autobranchia; Pteriomorphia; Pectinida; Pectinoidea; Pectinidae;
OC   Placopecten.
OX   NCBI_TaxID=6577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Adductor muscle;
RA   Patwary M.U., Reith M., Kenchington E.L.;
RT   "Isolation and characterization of a cDNA encoding an actin gene from sea
RT   scallop (Placopecten magellanicus).";
RL   J. Shellfish Res. 15:265-270(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   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC   -!- MISCELLANEOUS: There are at least 12 actin genes in P.magellanicus.
CC       Only one actin gene is expressed in the adductor muscle.
CC   -!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
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DR   EMBL; U55046; AAB02227.1; -; mRNA.
DR   AlphaFoldDB; Q26065; -.
DR   SMR; Q26065; -.
DR   PRIDE; Q26065; -.
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_0000000712"
FT   CHAIN           3..376
FT                   /note="Actin, adductor muscle"
FT                   /id="PRO_0000000713"
FT   MOD_RES         3
FT                   /note="N-acetylaspartate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   376 AA;  41762 MW;  BBFADB15F0158FD6 CRC64;
     MCDDEVAALV VDNGSGMCKA GFAGDDAPRA VFPSIVGRPR HQGVMVGMGQ KDSYVGDEAQ
     SKRGILTLKY PIEHGIVTNW DDMEKIWHHT FYNELRVAPE EHPVLLTEAP LNPKANREKM
     TQIMFETFNA PAMYVAIQAV LSLYASGRTT GIVLDSGDGV THTVPIYEGY ALPHAILRLD
     LAGRDLTDYL MKILTERGYS FTTTAEREIV RDIKEKLCYV ALDFENEMAT AASSSSLEKS
     YELPDGQVIT IGNERFRCPE SLFQPSFLGM ESAGIHETTY NSIMKCDVDI RKDLYANTVL
     SGGTTMFPGI ADRMQKEITA LAPSTMKIKI IAPPERKYSV WIGGSILASL STFQQMWISK
     QEYDESGPSI VHRKCF