ACTG_TRISC
ID ACTG_TRISC Reviewed; 375 AA.
AC Q8JJB8;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=Actin, cytoplasmic 2;
DE AltName: Full=Gamma-actin;
DE Contains:
DE RecName: Full=Actin, cytoplasmic 2, N-terminally processed;
GN Name=actg1; Synonyms=actg;
OS Triakis scyllium (Banded houndshark) (Hemigaleus pingi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Galeomorphii; Galeoidea; Carcharhiniformes; Triakidae;
OC Triakis.
OX NCBI_TaxID=30494;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Haruta C., Inoue Y., Moritomo T., Nakanishi T.;
RT "Molecular cloning and sequencing of Triakis scyllium beta actin.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000250|UniProtKB:P63261}.
CC -!- SUBUNIT: Polymerization of globular actin (G-actin) leads to a
CC structural filament (F-actin) in the form of a two-stranded helix. Each
CC actin can bind to 4 others.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P63261}.
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:P63260}.
CC -!- PTM: Methylated at His-73 by SETD3. {ECO:0000250|UniProtKB:P63261}.
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.
CC -!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
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DR EMBL; AB084472; BAB91355.1; -; mRNA.
DR AlphaFoldDB; Q8JJB8; -.
DR SMR; Q8JJB8; -.
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: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 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Cytoplasm; Cytoskeleton; Methylation;
KW Nucleotide-binding; Oxidation.
FT CHAIN 1..375
FT /note="Actin, cytoplasmic 2"
FT /id="PRO_0000367107"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63261"
FT CHAIN 2..375
FT /note="Actin, cytoplasmic 2, N-terminally processed"
FT /id="PRO_0000280379"
FT MOD_RES 1
FT /note="N-acetylmethionine; in Actin, cytoplasmic 2;
FT alternate"
FT /evidence="ECO:0000250|UniProtKB:P63261"
FT MOD_RES 2
FT /note="N-acetylaspartate; in Actin, cytoplasmic 2, N-
FT terminally processed"
FT /evidence="ECO:0000250|UniProtKB:P63261"
FT MOD_RES 44
FT /note="Methionine (R)-sulfoxide"
FT /evidence="ECO:0000250|UniProtKB:P63260"
FT MOD_RES 47
FT /note="Methionine (R)-sulfoxide"
FT /evidence="ECO:0000250|UniProtKB:P63260"
FT MOD_RES 73
FT /note="Tele-methylhistidine"
FT /evidence="ECO:0000250|UniProtKB:P63260"
SQ SEQUENCE 375 AA; 41751 MW; 7FFDF0CAA6FFD639 CRC64;
MDDEIAALVV DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS
KRGILTLKYP IEHGIVTNWD DMEKIWHHTF YNELRVAPEE HPVLLTEAPL NPKANREKMT
QIMFETFNTP AMYVAIQAVL SLYASGRTTG IVMDSGDGVT HTVPIYEGYA LPHAILRLDL
AGRDLTDYLM KILTERGYSF TTTAEREIVR DIKEKLCYVA LDFEQEMATA ASSSSLEKSY
ELPDGQVITI GNERFRCPEA LFQPSFLGME SCGIHETTFN SIMKCDVDIR KDLYANTVLS
GGTTMYPGIA DRMQKEITAL APSTMKIKII APPERKYSVW IGGSILASLS TFQQMWISKQ
EYDESGPSIV HRKCF