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Actin, cytoplasmic 1 (Beta-actin) [Cleaved into: Actin, cytoplasmic 1, N-terminally processed]

 ACTB_MESAU              Reviewed;         375 AA.
Q711N9;
11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
05-DEC-2018, entry version 90.
RecName: Full=Actin, cytoplasmic 1;
AltName: Full=Beta-actin;
Contains:
RecName: Full=Actin, cytoplasmic 1, N-terminally processed;
Name=ACTB;
Mesocricetus auratus (Golden hamster).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Cricetidae; Cricetinae; Mesocricetus.
NCBI_TaxID=10036;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Kidney;
Posthuma C.C.;
"Sequence of the beta actin gene from baby hamster kidney (BHK-21)
cells.";
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
[2]
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=20400973; DOI=10.1038/aja.2010.19;
Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B.,
Shivaji S.;
"Glucose-regulated protein precursor (GRP78) and tumor rejection
antigen (GP96) are unique to hamster caput epididymal spermatozoa.";
Asian J. Androl. 12:344-355(2010).
-!- FUNCTION: Actin is a highly conserved protein that polymerizes to
produce filaments that form cross-linked networks in the cytoplasm
of cells. Actin exists in both monomeric (G-actin) and polymeric
(F-actin) forms, both forms playing key functions, such as cell
motility and contraction. In addition to their role in the
cytoplasmic cytoskeleton, G- and F-actin also localize in the
nucleus, and regulate gene transcription and motility and repair
of damaged DNA. {ECO:0000250|UniProtKB:P60709}.
-!- SUBUNIT: Polymerization of globular actin (G-actin) leads to a
structural filament (F-actin) in the form of a two-stranded helix.
Each actin can bind to 4 others. Identified in a IGF2BP1-dependent
mRNP granule complex containing untranslated mRNAs. Component of
the BAF complex, which includes at least actin (ACTB), ARID1A,
ARID1B/BAF250, SMARCA2, SMARCA4/BRG1, ACTL6A/BAF53, ACTL6B/BAF53B,
SMARCE1/BAF57 SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1,
and one or more of SMARCD1/BAF60A, SMARCD2/BAF60B, or
SMARCD3/BAF60C. In muscle cells, the BAF complex also contains
DPF3. Found in a complex with XPO6, Ran, ACTB and PFN1. Interacts
with XPO6 and EMD. Interacts with ERBB2. Interacts with GCSAM (By
similarity). Interacts with TBC1D21. Interacts with CPNE1 (via
VWFA domain) and CPNE4 (via VWFA domain) (By similarity).
Interacts with DHX9 (via C-terminus); this interaction is direct
and mediates the attachment to nuclear ribonucleoprotein
complexes. Interacts with FAM107A (By similarity).
{ECO:0000250|UniProtKB:P60709, ECO:0000250|UniProtKB:P60710}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
{ECO:0000250|UniProtKB:P60709}. Nucleus
{ECO:0000250|UniProtKB:P60709}. Note=Localized in cytoplasmic mRNP
granules containing untranslated mRNAs.
{ECO:0000250|UniProtKB:P60709}.
-!- PTM: ISGylated. {ECO:0000250|UniProtKB:P60709}.
-!- PTM: Oxidation of Met-44 and Met-47 by MICALs (MICAL1, MICAL2 or
MICAL3) to form methionine sulfoxide promotes actin filament
depolymerization. MICAL1 and MICAL2 produce the (R)-S-oxide form.
The (R)-S-oxide form is reverted by MSRB1 and MSRB2, which promote
actin repolymerization. {ECO:0000250|UniProtKB:P60710}.
-!- PTM: Monomethylation at Lys-84 (K84me1) regulates actin-myosin
interaction and actomyosin-dependent processes. Demethylation by
ALKBH4 is required for maintaining actomyosin dynamics supporting
normal cleavage furrow ingression during cytokinesis and cell
migration. {ECO:0000250|UniProtKB:P60709}.
-!- PTM: Actin, cytoplasmic 1, N-terminally processed: N-terminal
acetylation by NAA80 affects actin filament depolymerization and
elongation, including elongation driven by formins. In contrast,
filament nucleation by the Arp2/3 complex is not affected.
{ECO:0000250|UniProtKB:P60709}.
-!- MISCELLANEOUS: In vertebrates 3 main groups of actin isoforms,
alpha, beta and gamma have been identified. The alpha actins are
found in muscle tissues and are a major constituent of the
contractile apparatus. The beta and gamma actins coexist in most
cell types as components of the cytoskeleton and as mediators of
internal cell motility. {ECO:0000250|UniProtKB:P60709}.
-!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
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EMBL; AJ312092; CAC38394.1; -; mRNA.
RefSeq; NP_001268524.1; NM_001281595.1.
RefSeq; XP_012975858.1; XM_013120404.1.
ProteinModelPortal; Q711N9; -.
SMR; Q711N9; -.
PRIDE; Q711N9; -.
Ensembl; ENSMAUT00000010774; ENSMAUP00000006968; ENSMAUG00000008763.
GeneID; 101844587; -.
CTD; 60; -.
HOVERGEN; HBG003771; -.
OrthoDB; EOG091G08LD; -.
Proteomes; UP000189706; Genome assembly.
GO; GO:0015629; C:actin cytoskeleton; ISS:UniProtKB.
GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IEA:Ensembl.
GO; GO:0005856; C:cytoskeleton; ISS:AgBase.
GO; GO:0097433; C:dense body; ISS:AgBase.
GO; GO:0005925; C:focal adhesion; ISS:AgBase.
GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IEA:Ensembl.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISS:AgBase.
GO; GO:0098871; C:postsynaptic actin cytoskeleton; IEA:Ensembl.
GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0019894; F:kinesin binding; IEA:Ensembl.
GO; GO:0050998; F:nitric-oxide synthase binding; IEA:Ensembl.
GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
GO; GO:0098973; F:structural constituent of postsynaptic actin cytoskeleton; IEA:Ensembl.
GO; GO:0030957; F:Tat protein binding; IEA:Ensembl.
GO; GO:0048870; P:cell motility; IEA:Ensembl.
GO; GO:0072749; P:cellular response to cytochalasin B; IEA:Ensembl.
GO; GO:0051621; P:regulation of norepinephrine uptake; IEA:Ensembl.
GO; GO:1903076; P:regulation of protein localization to plasma membrane; IEA:Ensembl.
GO; GO:0022898; P:regulation of transmembrane transporter activity; IEA:Ensembl.
InterPro; IPR004000; Actin.
InterPro; IPR020902; Actin/actin-like_CS.
InterPro; IPR004001; Actin_CS.
PANTHER; PTHR11937; PTHR11937; 1.
Pfam; PF00022; Actin; 1.
PRINTS; PR00190; ACTIN.
SMART; SM00268; ACTIN; 1.
PROSITE; PS00406; ACTINS_1; 1.
PROSITE; PS00432; ACTINS_2; 1.
PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
1: Evidence at protein level;
Acetylation; ATP-binding; Complete proteome; Cytoplasm; Cytoskeleton;
Methylation; Nucleotide-binding; Nucleus; Oxidation;
Reference proteome; Ubl conjugation.
CHAIN 1 375 Actin, cytoplasmic 1.
/FTId=PRO_0000000773.
INIT_MET 1 1 Removed; alternate.
{ECO:0000250|UniProtKB:P60709}.
CHAIN 2 375 Actin, cytoplasmic 1, N-terminally
processed.
/FTId=PRO_0000367075.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:P60709}.
MOD_RES 2 2 N-acetylaspartate; in Actin, cytoplasmic
1, N-terminally processed.
{ECO:0000250|UniProtKB:P60709}.
MOD_RES 44 44 Methionine (R)-sulfoxide.
{ECO:0000250|UniProtKB:P60710}.
MOD_RES 47 47 Methionine (R)-sulfoxide.
{ECO:0000250|UniProtKB:P60710}.
MOD_RES 73 73 Tele-methylhistidine.
{ECO:0000250|UniProtKB:P60710}.
MOD_RES 84 84 N6-methyllysine.
{ECO:0000250|UniProtKB:P60709}.
SEQUENCE 375 AA; 41737 MW; 6AFD05CA94E360E2 CRC64;
MDDDIAALVV 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


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