ID   ACTC_BIOGL              Reviewed;         376 AA.
AC   P92179; Q964E4;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 2.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Actin, cytoplasmic;
DE   Contains:
DE     RecName: Full=Actin, cytoplasmic, intermediate form;
DE   Flags: Precursor;
OS   Biomphalaria glabrata (Bloodfluke planorb) (Freshwater snail).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Heterobranchia; Euthyneura; Panpulmonata; Hygrophila; Lymnaeoidea;
OC   Planorbidae; Biomphalaria.
OX   NCBI_TaxID=6526;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Albino;
RX   PubMed=9524815; DOI=10.3109/10425179709034055;
RA   Lardans V., Ringaut V., Duclermortier P., Cadoret J.P., Dissous C.;
RT   "Nucleotide and deduced amino acid sequences of Biomphalaria glabrata actin
RT   cDNA.";
RL   DNA Seq. 7:353-356(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=M-line;
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; Z72387; CAA96527.1; -; mRNA.
DR   EMBL; U53348; AAB49413.1; -; mRNA.
DR   EMBL; AF329436; AAK68710.1; -; Genomic_DNA.
DR   AlphaFoldDB; P92179; -.
DR   SMR; P92179; -.
DR   STRING; 6526.P92179; -.
DR   VEuPathDB; VectorBase:BGLB003971; -.
DR   Proteomes; UP000076420; Genome assembly.
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; 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_0000443006"
FT   CHAIN           3..376
FT                   /note="Actin, cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P68135"
FT                   /id="PRO_0000000625"
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"
FT   CONFLICT        272..273
FT                   /note="AA -> VV (in Ref. 1; CAA96527/AAB49413)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   376 AA;  41881 MW;  EFD29899498FD633 CRC64;
     MCDEDVAALV VDNGSGMCKA GFAGDDAPRA VFPSIVGRPR HQGVMVGMGQ KDSYVGDEAQ
     SKRGILTLKY PIEHGIVTNW DDMEKIWHHT FYNELRVAPE EHPVLLTEAP LNPKANREKM
     TQIMFETFNT PAMYVAIQAV LSLYASGRTT GIVMDSGDGV THTVPIYEGY ALPHAIMRLD
     LAGRDLTDYL MKILTERGYS FTTTAEREIV RDIKEKLCYV ALDFEQEMQT ASTSSSLEKS
     YELPDGQVIT IGNERFRCPE ATFQPSFLGM EAAGIHETTY NSIMKCDVDI RKDLYANTVL
     SGGSTMFPGI ADRMQKEITA LAPPTMKIKI IAPPERKYSV WIGGSILASL STFQQMWISK
     QEYDESGPSI VHRKCF