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

 ACTB_CANLF              Reviewed;         375 AA.
O18840; Q11209; Q8SPX4; Q95164;
26-APR-2005, integrated into UniProtKB/Swiss-Prot.
13-NOV-2007, sequence version 3.
22-NOV-2017, entry version 136.
RecName: Full=Actin, cytoplasmic 1;
AltName: Full=Beta-actin;
Contains:
RecName: Full=Actin, cytoplasmic 1, N-terminally processed;
Name=ACTB;
Canis lupus familiaris (Dog) (Canis familiaris).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
Canis.
NCBI_TaxID=9615;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Cocker spaniel; TISSUE=Kidney;
Ortiz-Garcia D.M., Guaderrama M., Salgado L.M., Meza I.;
Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-189.
TISSUE=Heart;
Tiwari N., Mishra S., Rastogi S., Sabbah H.N., Gupta R.C.;
"Cloning of the beta-actin gene from dog heart.";
Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 23-206.
STRAIN=Beagle; TISSUE=Blood;
Gilmore W.H., Carter S.D., Bennett M., Barnes A., Kelly D.F.;
"Expression of canine TNF, IL-1 and IL-6 mRNAs in peripheral blood
monocytes and cell lines.";
Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 282-341.
PubMed=8855304; DOI=10.1073/pnas.93.20.11035;
Lee Y.A., Liang C.S., Lee M.A., Lindpaintner K.;
"Local stress, not systemic factors, regulate gene expression of the
cardiac renin-angiotensin system in vivo: a comprehensive study of all
its components in the dog.";
Proc. Natl. Acad. Sci. U.S.A. 93:11035-11040(1996).
-!- FUNCTION: Actins are highly conserved proteins that are involved
in various types of cell motility and are ubiquitously expressed
in all eukaryotic cells. {ECO:0000250}.
-!- 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. Component
of the MLL5-L complex, at least composed of KMT2E/MLL5, STK38,
PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT. Interacts with XPO6
and EMD. Interacts with ERBB2. Interacts with GCSAM. Interacts
with CPNE1 (via VWFA domain) and CPNE4 (via VWFA domain).
Interacts with DHX9 (via C-terminus); this interaction is direct
and mediates the attachment to nuclear ribonucleoprotein
complexes. Interacts with TBC1D21. {ECO:0000250,
ECO:0000250|UniProtKB:P60709, ECO:0000250|UniProtKB:P60710}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Note=Localized in
cytoplasmic mRNP granules containing untranslated mRNAs.
{ECO:0000250}.
-!- PTM: ISGylated. {ECO:0000250}.
-!- 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 (By similarity). {ECO:0000250}.
-!- 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 (By similarity). {ECO:0000250}.
-!- 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.
-!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF021873; AAB71610.2; -; mRNA.
EMBL; AF484115; AAL92020.1; -; mRNA.
EMBL; Z70044; CAA93907.1; -; mRNA.
EMBL; U67202; AAC48640.1; -; mRNA.
RefSeq; NP_001182774.2; NM_001195845.2.
UniGene; Cfa.17735; -.
UniGene; Cfa.32424; -.
UniGene; Cfa.39123; -.
ProteinModelPortal; O18840; -.
SMR; O18840; -.
IntAct; O18840; 1.
MINT; MINT-3375148; -.
STRING; 9615.ENSCAFP00000023597; -.
PaxDb; O18840; -.
PRIDE; O18840; -.
Ensembl; ENSCAFT00000025413; ENSCAFP00000023597; ENSCAFG00000016020.
GeneID; 403580; -.
KEGG; cfa:403580; -.
CTD; 60; -.
eggNOG; KOG0676; Eukaryota.
eggNOG; COG5277; LUCA.
GeneTree; ENSGT00760000118957; -.
HOGENOM; HOG000233340; -.
HOVERGEN; HBG003771; -.
InParanoid; O18840; -.
KO; K05692; -.
OMA; MERGYPF; -.
OrthoDB; EOG091G08LD; -.
TreeFam; TF354237; -.
Reactome; R-CFA-190873; Gap junction degradation.
Reactome; R-CFA-196025; Formation of annular gap junctions.
Reactome; R-CFA-2029482; Regulation of actin dynamics for phagocytic cup formation.
Reactome; R-CFA-3928662; EPHB-mediated forward signaling.
Reactome; R-CFA-3928665; EPH-ephrin mediated repulsion of cells.
Reactome; R-CFA-437239; Recycling pathway of L1.
Reactome; R-CFA-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-CFA-445095; Interaction between L1 and Ankyrins.
Reactome; R-CFA-446353; Cell-extracellular matrix interactions.
Reactome; R-CFA-5250924; B-WICH complex positively regulates rRNA expression.
Reactome; R-CFA-5626467; RHO GTPases activate IQGAPs.
Reactome; R-CFA-5663213; RHO GTPases Activate WASPs and WAVEs.
Reactome; R-CFA-5663220; RHO GTPases Activate Formins.
Reactome; R-CFA-5689603; UCH proteinases.
Reactome; R-CFA-5696394; DNA Damage Recognition in GG-NER.
Reactome; R-CFA-8856828; Clathrin-mediated endocytosis.
Proteomes; UP000002254; Chromosome 6.
Bgee; ENSCAFG00000016020; -.
GO; GO:0015629; C:actin cytoskeleton; ISS:UniProtKB.
GO; GO:0072562; C:blood microparticle; IEA:Ensembl.
GO; GO:0030863; C:cortical cytoskeleton; IEA:Ensembl.
GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IEA:Ensembl.
GO; GO:0005856; C:cytoskeleton; ISS:AgBase.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0097433; C:dense body; ISS:AgBase.
GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
GO; GO:0005925; C:focal adhesion; ISS:AgBase.
GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IEA:Ensembl.
GO; GO:0000790; C:nuclear chromatin; IEA:Ensembl.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISS:AgBase.
GO; GO:0043234; C:protein 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:0031492; F:nucleosomal DNA binding; IEA:Ensembl.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0000980; F:RNA polymerase II distal enhancer sequence-specific DNA 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:0043044; P:ATP-dependent chromatin remodeling; IEA:Ensembl.
GO; GO:0070527; P:platelet aggregation; IEA:Ensembl.
GO; GO:0001895; P:retina homeostasis; IEA:Ensembl.
GO; GO:0021762; P:substantia nigra development; 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.
2: Evidence at transcript level;
Acetylation; ATP-binding; Complete proteome; Cytoplasm; Cytoskeleton;
Methylation; Nucleotide-binding; Oxidation; Reference proteome;
Ubl conjugation.
CHAIN 1 375 Actin, cytoplasmic 1.
/FTId=PRO_0000000761.
INIT_MET 1 1 Removed; alternate.
{ECO:0000250|UniProtKB:P60709}.
CHAIN 2 375 Actin, cytoplasmic 1, N-terminally
processed.
/FTId=PRO_0000367068.
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}.
MOD_RES 47 47 Methionine (R)-sulfoxide. {ECO:0000250}.
MOD_RES 73 73 Tele-methylhistidine.
{ECO:0000250|UniProtKB:P60710}.
MOD_RES 84 84 N6-methyllysine.
{ECO:0000250|UniProtKB:P60709}.
CONFLICT 4 4 D -> E (in Ref. 1; AAB71610).
{ECO:0000305}.
CONFLICT 46 46 G -> R (in Ref. 1; AAB71610).
{ECO:0000305}.
CONFLICT 101 101 H -> A (in Ref. 1; AAB71610).
{ECO:0000305}.
CONFLICT 131 131 A -> T (in Ref. 3; CAA93907).
{ECO:0000305}.
CONFLICT 215 230 KLCYVALDFEQEMATA -> EALLRRPGLRAGDGHG (in
Ref. 1; AAB71610). {ECO:0000305}.
CONFLICT 259 259 E -> K (in Ref. 1; AAB71610).
{ECO:0000305}.
CONFLICT 323 324 ST -> AR (in Ref. 1; AAB71610).
{ECO:0000305}.
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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