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Actin, cytoplasmic 2 (Gamma-actin) [Cleaved into: Actin, cytoplasmic 2, N-terminally processed]

 ACTG_RAT                Reviewed;         375 AA.
P63259; P02571; P14104; P99022;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
10-OCT-2018, entry version 130.
RecName: Full=Actin, cytoplasmic 2;
AltName: Full=Gamma-actin;
Contains:
RecName: Full=Actin, cytoplasmic 2, N-terminally processed;
Name=Actg1; Synonyms=Actg;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Kidney;
PubMed=2402472; DOI=10.1093/nar/18.17.5312;
Brown C.W., McHugh K.M., Lessard J.L.;
"A cDNA sequence encoding cytoskeletal gamma-actin from rat.";
Nucleic Acids Res. 18:5312-5312(1990).
[2]
PROTEIN SEQUENCE OF 4-19 AND 228-231.
PubMed=2372296; DOI=10.1016/0006-291X(90)91281-V;
Akamizu T., Saji M., Kohn L.D.;
"A microsequencing approach to identify proteins which appear to
interact with thyrotropin in rat FRTL-5 thyroid cells.";
Biochem. Biophys. Res. Commun. 170:351-358(1990).
[3]
PROTEIN SEQUENCE OF 29-37; 51-62 AND 85-95, AND IDENTIFICATION BY MASS
SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
Lubec G., Chen W.-Q.;
Submitted (APR-2007) to UniProtKB.
-!- 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|UniProtKB:P63261}.
-!- 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. Interacts with TWF1, CAPZB,
cofilin and profilin. {ECO:0000250|UniProtKB:P63261}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
{ECO:0000250|UniProtKB:P63261}.
-!- 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:P63260}.
-!- 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:P63261}.
-!- PTM: Actin, cytoplasmic 2, 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:P63261}.
-!- 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; X52815; CAA36999.1; -; mRNA.
PIR; A38571; ATRTC.
PIR; S11222; S11222.
RefSeq; NP_001120921.1; NM_001127449.1.
RefSeq; XP_002729242.3; XM_002729196.4.
RefSeq; XP_017452655.1; XM_017597166.1.
UniGene; Rn.101464; -.
UniGene; Rn.106826; -.
UniGene; Rn.228774; -.
ProteinModelPortal; P63259; -.
SMR; P63259; -.
BioGrid; 252365; 2.
CORUM; P63259; -.
IntAct; P63259; 3.
CarbonylDB; P63259; -.
iPTMnet; P63259; -.
PhosphoSitePlus; P63259; -.
World-2DPAGE; 0004:P63259; -.
PRIDE; P63259; -.
Ensembl; ENSRNOT00000054976; ENSRNOP00000051859; ENSRNOG00000036701.
Ensembl; ENSRNOT00000079310; ENSRNOP00000072273; ENSRNOG00000053452.
GeneID; 100361457; -.
GeneID; 287876; -.
KEGG; rno:100361457; -.
KEGG; rno:287876; -.
CTD; 71; -.
RGD; 1304556; Actg1.
eggNOG; KOG0676; Eukaryota.
eggNOG; COG5277; LUCA.
GeneTree; ENSGT00760000118957; -.
HOGENOM; HOG000233340; -.
HOVERGEN; HBG003771; -.
InParanoid; P63259; -.
KO; K05692; -.
OMA; MIGRECS; -.
OrthoDB; EOG091G08LD; -.
PhylomeDB; P63259; -.
TreeFam; TF354237; -.
Reactome; R-RNO-190873; Gap junction degradation.
Reactome; R-RNO-196025; Formation of annular gap junctions.
Reactome; R-RNO-2029482; Regulation of actin dynamics for phagocytic cup formation.
Reactome; R-RNO-3928662; EPHB-mediated forward signaling.
Reactome; R-RNO-418990; Adherens junctions interactions.
Reactome; R-RNO-437239; Recycling pathway of L1.
Reactome; R-RNO-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-RNO-445095; Interaction between L1 and Ankyrins.
Reactome; R-RNO-446353; Cell-extracellular matrix interactions.
Reactome; R-RNO-5626467; RHO GTPases activate IQGAPs.
Reactome; R-RNO-5663213; RHO GTPases Activate WASPs and WAVEs.
Reactome; R-RNO-5663220; RHO GTPases Activate Formins.
Reactome; R-RNO-5674135; MAP2K and MAPK activation.
Reactome; R-RNO-8856828; Clathrin-mediated endocytosis.
PRO; PR:P63259; -.
Proteomes; UP000002494; Chromosome 10.
Proteomes; UP000002494; Chromosome 3.
Bgee; ENSRNOG00000036701; Expressed in 9 organ(s), highest expression level in testis.
Genevisible; P63259; RN.
GO; GO:0005856; C:cytoskeleton; ISS:AgBase.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0097433; C:dense body; ISS:AgBase.
GO; GO:0005925; C:focal adhesion; ISS:AgBase.
GO; GO:0005886; C:plasma membrane; ISS:AgBase.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0098974; P:postsynaptic actin cytoskeleton organization; IEA:GOC.
GO; GO:0051592; P:response to calcium ion; IEP:RGD.
GO; GO:0009612; P:response to mechanical stimulus; IEP:RGD.
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;
Direct protein sequencing; Methylation; Nucleotide-binding; Oxidation;
Reference proteome.
CHAIN 1 375 Actin, cytoplasmic 2.
/FTId=PRO_0000000835.
INIT_MET 1 1 Removed; alternate.
{ECO:0000250|UniProtKB:P63261}.
CHAIN 2 375 Actin, cytoplasmic 2, N-terminally
processed.
/FTId=PRO_0000367102.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:P63261}.
MOD_RES 2 2 N-acetylglutamate; in Actin, cytoplasmic
2, N-terminally processed.
{ECO:0000250|UniProtKB:P63261}.
MOD_RES 44 44 Methionine (R)-sulfoxide.
{ECO:0000250|UniProtKB:P63260}.
MOD_RES 47 47 Methionine (R)-sulfoxide.
{ECO:0000250|UniProtKB:P63260}.
MOD_RES 73 73 Tele-methylhistidine.
{ECO:0000250|UniProtKB:P63258}.
MOD_RES 84 84 N6-methyllysine.
{ECO:0000250|UniProtKB:P63261}.
SEQUENCE 375 AA; 41793 MW; 54D08F986964EFD5 CRC64;
MEEEIAALVI 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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