ACTB2_TAKRU
ID ACTB2_TAKRU Reviewed; 375 AA.
AC P53485;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=Actin, cytoplasmic 2;
DE AltName: Full=Beta-actin B;
DE Contains:
DE RecName: Full=Actin, cytoplasmic 2, N-terminally processed;
GN Name=actbb;
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8683572; DOI=10.1006/jmbi.1996.0347;
RA Venkatesh B., Tay B.H., Elgar G., Brenner S.;
RT "Isolation, characterization and evolution of nine pufferfish (Fugu
RT rubripes) actin genes.";
RL J. Mol. Biol. 259:655-665(1996).
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:0000250|UniProtKB:P60709}.
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 (By similarity).
CC {ECO:0000250|UniProtKB:P60709, ECO:0000250|UniProtKB:P60710}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P60710}. Nucleus {ECO:0000250|UniProtKB:O93400}.
CC -!- PTM: Oxidation of Met-44 and Met-47 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 promote actin
CC repolymerization. {ECO:0000250|UniProtKB:P60710}.
CC -!- PTM: Methylation at His-73 by SETD3. Methylation stabilizes actin
CC filaments. {ECO:0000250|UniProtKB:P60706}.
CC -!- MISCELLANEOUS: There are three different beta-cytoplasmic actins in
CC Fugu rubripes. {ECO:0000305}.
CC -!- MISCELLANEOUS: In vertebrates 3 main groups of actin isoforms, alpha,
CC beta and gamma have been identified. The alpha actins are found in
CC muscle tissues and are a major constituent of the contractile
CC apparatus. The beta and gamma actins coexist in most cell types as
CC components of the cytoskeleton and as mediators of internal cell
CC motility. {ECO:0000250|UniProtKB:O93400}.
CC -!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
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DR EMBL; U38848; AAC59890.1; -; Genomic_DNA.
DR PIR; S71125; S71125.
DR RefSeq; XP_003972351.1; XM_003972302.2.
DR AlphaFoldDB; P53485; -.
DR SMR; P53485; -.
DR STRING; 31033.ENSTRUP00000034556; -.
DR GeneID; 101079312; -.
DR KEGG; tru:101079312; -.
DR CTD; 57934; -.
DR eggNOG; KOG0676; Eukaryota.
DR HOGENOM; CLU_027965_0_2_1; -.
DR InParanoid; P53485; -.
DR OrthoDB; 649708at2759; -.
DR Proteomes; UP000005226; Unplaced.
DR GO; GO:0005856; C:cytoskeleton; ISS:AgBase.
DR GO; GO:0097433; C:dense body; ISS:AgBase.
DR GO; GO:0005925; C:focal adhesion; ISS:AgBase.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISS:AgBase.
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; Nucleus; Oxidation; Reference proteome.
FT CHAIN 1..375
FT /note="Actin, cytoplasmic 2"
FT /id="PRO_0000367095"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000250|UniProtKB:P60706"
FT CHAIN 2..375
FT /note="Actin, cytoplasmic 2, N-terminally processed"
FT /id="PRO_0000000811"
FT MOD_RES 1
FT /note="N-acetylmethionine; in Actin, cytoplasmic 2;
FT alternate"
FT /evidence="ECO:0000250|UniProtKB:P60706"
FT MOD_RES 2
FT /note="N-acetylaspartate; in Actin, cytoplasmic 2, N-
FT terminally processed"
FT /evidence="ECO:0000250|UniProtKB:P60706"
FT MOD_RES 44
FT /note="Methionine (R)-sulfoxide"
FT /evidence="ECO:0000250|UniProtKB:P60710"
FT MOD_RES 47
FT /note="Methionine (R)-sulfoxide"
FT /evidence="ECO:0000250|UniProtKB:P60710"
FT MOD_RES 73
FT /note="Tele-methylhistidine"
FT /evidence="ECO:0000250|UniProtKB:P60710"
SQ SEQUENCE 375 AA; 41767 MW; 1AE990BC0AED0D1C CRC64;
MDDEIAALVV DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS
KRGILTLKYP IEHGIVTNWD DMEKIWHHTF YNELRVAPEE HPVLLTEAPL NPKANREKMT
QIMFETFNTP AMYVAIQAVL SLYASGRTTG IVMDSGDGVT HTVPIYEGYA LPHAILRLDL
AGRDLTDYLM KILTERGYSF TTTAEREIVR DIKEKLCYVA LDFEQEMGTA ASSSSLEKSY
ELPDGQVITI GNERFRCPEA LFQPSFLGME SCGIHETTFN SIMKCDVDIR KDLYANTVLS
GGTTMYPGIA DRMQKEITSL APTTMKIKII APPERKYSVW IGGSILASLS TFQQMWISKQ
EYDESGPSIV HRKCF
