ID   ACTC_BIOPF              Reviewed;         376 AA.
AC   Q964E2;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 64.
DE   RecName: Full=Actin, cytoplasmic;
DE   Contains:
DE     RecName: Full=Actin, cytoplasmic, intermediate form;
DE   Flags: Precursor;
OS   Biomphalaria pfeifferi (Bloodfluke planorb) (Freshwater snail).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Heterobranchia; Euthyneura; Panpulmonata; Hygrophila; Lymnaeoidea;
OC   Planorbidae; Biomphalaria.
OX   NCBI_TaxID=112525;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Adema C.M.;
RT   "Comparative study of cytoplasmic actin DNA from six species of Planorbidae
RT   (Gastropoda: Basommatophora).";
RL   J. Molluscan Stud. 68:17-23(2002).
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   -!- PTM: Oxidation of Met-45 and Met-48 by MICALs (MICAL1, MICAL2 or
CC       MICAL3) to form methionine sulfoxide promotes actin filament
CC       depolymerization. MICAL1 and MICAL2 produce the (R)-S-oxide form. The
CC       (R)-S-oxide form is reverted by MSRB1 and MSRB2, which promotes actin
CC       repolymerization. {ECO:0000250|UniProtKB:P68033}.
CC   -!- PTM: Monomethylation at Lys-85 (K85me1) regulates actin-myosin
CC       interaction and actomyosin-dependent processes. Demethylation by ALKBH4
CC       is required for maintaining actomyosin dynamics supporting normal
CC       cleavage furrow ingression during cytokinesis and cell migration.
CC       {ECO:0000250|UniProtKB:P68032}.
CC   -!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
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DR   EMBL; AF329438; AAK68712.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q964E2; -.
DR   SMR; Q964E2; -.
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; Methylation;
KW   Nucleotide-binding; Oxidation.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..376
FT                   /note="Actin, cytoplasmic, intermediate form"
FT                   /evidence="ECO:0000250|UniProtKB:P62737"
FT                   /id="PRO_0000443008"
FT   CHAIN           3..376
FT                   /note="Actin, cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P68135"
FT                   /id="PRO_0000000629"
FT   MOD_RES         2
FT                   /note="N-acetylcysteine; in intermediate form"
FT                   /evidence="ECO:0000250|UniProtKB:P62737"
FT   MOD_RES         3
FT                   /note="N-acetylaspartate; in Actin, cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P68135"
FT   MOD_RES         45
FT                   /note="Methionine (R)-sulfoxide"
FT                   /evidence="ECO:0000250|UniProtKB:P68033"
FT   MOD_RES         48
FT                   /note="Methionine (R)-sulfoxide"
FT                   /evidence="ECO:0000250|UniProtKB:P68033"
FT   MOD_RES         74
FT                   /note="Tele-methylhistidine"
FT                   /evidence="ECO:0000250|UniProtKB:P62739"
FT   MOD_RES         85
FT                   /note="N6-methyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P68032"
SQ   SEQUENCE   376 AA;  41870 MW;  C40F17388E5A73C3 CRC64;
     MCDEDVAALV VDNGSGMCKA GFAGDDAPRA VFPSIVGRPR HQGVMVGMGQ KDSYVGDEAQ
     SKRGILTLKY PIEHGIVTNW DDMEKIWHHT FYNELRVAPE EHPVLLTEAP LNPKANREKM
     TQIMFETFNT PAMYVAIQAV LSLYASGRTT GIVLDSGDGV THTVPIYEGY ALPHAIMRLD
     LAGRDLTDYL MKILTERGYS FTTTAEREIV RDIKEKLCYV ALDFEQEMHT AATSSSLEKS
     YELPDGQVIT IGNERFRCPE AVFQPSFLGM ESAGIHETTY NSIMKCDVDI RKDLYANTVL
     SGGSTMFPGI ADRMQKEITA LAPPTMKIKI IAPPERKYSV WIGGSILASL STFQQMWISK
     QEYDESGPSI VHRKCF