ID   A0SII9_ACHOL            Unreviewed;       158 AA.
AC   A0SII9;
DT   09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=Beta-actin {ECO:0000313|EMBL:ABF55272.1};
DE   Flags: Fragment;
OS   Achondrostoma oligolepis (Ruivaco) (Chondrostoma oligolepis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Leuciscidae; Leuciscinae; Achondrostoma.
OX   NCBI_TaxID=236538 {ECO:0000313|EMBL:ABF55272.1};
RN   [1] {ECO:0000313|EMBL:ABF55272.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=16949308; DOI=10.1016/j.ympev.2006.07.003;
RA   Robalo J.I., Almada V.C., Levy A., Doadrio I.;
RT   "Re-examination and phylogeny of the genus Chondrostoma based on
RT   mitochondrial and nuclear data and the definition of 5 new genera.";
RL   Mol. Phylogenet. Evol. 42:362-372(2007).
CC   -!- FUNCTION: Actin is a highly conserved protein that polymerizes to
CC       produce filaments that form cross-linked networks in the cytoplasm of
CC       cells. Actin exists in both monomeric (G-actin) and polymeric (F-actin)
CC       forms, both forms playing key functions, such as cell motility and
CC       contraction. In addition to their role in the cytoplasmic cytoskeleton,
CC       G- and F-actin also localize in the nucleus, and regulate gene
CC       transcription and motility and repair of damaged DNA.
CC       {ECO:0000256|ARBA:ARBA00037523}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000256|ARBA:ARBA00001836};
CC   -!- SUBUNIT: Polymerization of globular actin (G-actin) leads to a
CC       structural filament (F-actin) in the form of a two-stranded helix (By
CC       similarity). Each actin can bind to 4 others.
CC       {ECO:0000256|ARBA:ARBA00038685}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the actin family.
CC       {ECO:0000256|RuleBase:RU000487}.
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DR   EMBL; DQ447713; ABF55272.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0SII9; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR   Gene3D; 3.30.420.40; -; 2.
DR   InterPro; IPR004000; Actin.
DR   InterPro; IPR020902; Actin/actin-like_CS.
DR   InterPro; IPR004001; Actin_CS.
DR   InterPro; IPR043129; ATPase_NBD.
DR   PANTHER; PTHR11937; ACTIN; 1.
DR   PANTHER; PTHR11937:SF46; ACTIN-42A-RELATED; 1.
DR   Pfam; PF00022; Actin; 1.
DR   PRINTS; PR00190; ACTIN.
DR   SMART; SM00268; ACTIN; 1.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   PROSITE; PS00406; ACTINS_1; 1.
DR   PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE   3: Inferred from homology;
KW   Methylation {ECO:0000256|ARBA:ARBA00022481};
KW   Oxidation {ECO:0000256|ARBA:ARBA00023097}.
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ABF55272.1"
FT   NON_TER         158
FT                   /evidence="ECO:0000313|EMBL:ABF55272.1"
SQ   SEQUENCE   158 AA;  17566 MW;  22DCD50D0B58E6DA CRC64;
     GFAGDDAPRA VFPSIVGRPR HQGVMVGMGQ KDSYVGDEAQ SKRGILTLKY PIEHGIVTNW
     DDMEKIWHHT FYNELRVAPE EHPVLLTEAP LNPKANREKM TQIMFETFNT PAMYVAIQAV
     LSLYASGRTT GIVMDSGDGV THTVPIYEGY ALPHAILR
//