ACTG_RAT
ID ACTG_RAT Reviewed; 375 AA.
AC P63259; P02571; P14104; P99022;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 150.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RX PubMed=2402472; DOI=10.1093/nar/18.17.5312;
RA Brown C.W., McHugh K.M., Lessard J.L.;
RT "A cDNA sequence encoding cytoskeletal gamma-actin from rat.";
RL Nucleic Acids Res. 18:5312-5312(1990).
RN [2]
RP PROTEIN SEQUENCE OF 4-19 AND 228-231.
RX PubMed=2372296; DOI=10.1016/0006-291x(90)91281-v;
RA Akamizu T., Saji M., Kohn L.D.;
RT "A microsequencing approach to identify proteins which appear to interact
RT with thyrotropin in rat FRTL-5 thyroid cells.";
RL Biochem. Biophys. Res. Commun. 170:351-358(1990).
RN [3]
RP PROTEIN SEQUENCE OF 29-37; 51-62 AND 85-95, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Chen W.-Q.;
RL Submitted (APR-2007) to UniProtKB.
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. Interacts with TWF1, CAPZB, cofilin and
CC profilin. {ECO:0000250|UniProtKB:P63261}.
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: Monomethylation at Lys-84 (K84me1) regulates actin-myosin
CC interaction and actomyosin-dependent processes. Demethylation by ALKBH4
CC is required for maintaining actomyosin dynamics supporting normal
CC cleavage furrow ingression during cytokinesis and cell migration.
CC {ECO:0000250|UniProtKB:P63261}.
CC -!- PTM: [Actin, cytoplasmic 2, N-terminally processed]: N-terminal
CC acetylation by NAA80 affects actin filament depolymerization and
CC elongation, including elongation driven by formins. In contrast,
CC filament nucleation by the Arp2/3 complex is not affected.
CC {ECO:0000250|UniProtKB:P63261}.
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; X52815; CAA36999.1; -; mRNA.
DR PIR; A38571; ATRTC.
DR PIR; S11222; S11222.
DR RefSeq; NP_001120921.1; NM_001127449.1.
DR RefSeq; XP_002729242.3; XM_002729196.4.
DR RefSeq; XP_017452655.1; XM_017597166.1.
DR AlphaFoldDB; P63259; -.
DR SMR; P63259; -.
DR BioGRID; 252365; 3.
DR CORUM; P63259; -.
DR IntAct; P63259; 3.
DR STRING; 10116.ENSRNOP00000051859; -.
DR CarbonylDB; P63259; -.
DR iPTMnet; P63259; -.
DR PhosphoSitePlus; P63259; -.
DR World-2DPAGE; 0004:P63259; -.
DR jPOST; P63259; -.
DR PRIDE; P63259; -.
DR Ensembl; ENSRNOT00000108494; ENSRNOP00000096150; ENSRNOG00000036701.
DR GeneID; 100361457; -.
DR GeneID; 287876; -.
DR KEGG; rno:100361457; -.
DR KEGG; rno:287876; -.
DR CTD; 71; -.
DR RGD; 1304556; Actg1.
DR GeneTree; ENSGT00950000182960; -.
DR HOGENOM; CLU_027965_0_2_1; -.
DR InParanoid; P63259; -.
DR OMA; WICKSEY; -.
DR OrthoDB; 649708at2759; -.
DR PhylomeDB; P63259; -.
DR TreeFam; TF354237; -.
DR Reactome; R-RNO-114608; Platelet degranulation.
DR Reactome; R-RNO-190873; Gap junction degradation.
DR Reactome; R-RNO-196025; Formation of annular gap junctions.
DR Reactome; R-RNO-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-RNO-3928662; EPHB-mediated forward signaling.
DR Reactome; R-RNO-418990; Adherens junctions interactions.
DR Reactome; R-RNO-437239; Recycling pathway of L1.
DR Reactome; R-RNO-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-RNO-445095; Interaction between L1 and Ankyrins.
DR Reactome; R-RNO-446353; Cell-extracellular matrix interactions.
DR Reactome; R-RNO-5626467; RHO GTPases activate IQGAPs.
DR Reactome; R-RNO-5663213; RHO GTPases Activate WASPs and WAVEs.
DR Reactome; R-RNO-5663220; RHO GTPases Activate Formins.
DR Reactome; R-RNO-5674135; MAP2K and MAPK activation.
DR Reactome; R-RNO-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-RNO-9013418; RHOBTB2 GTPase cycle.
DR PRO; PR:P63259; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000036701; Expressed in frontal cortex and 8 other tissues.
DR Genevisible; P63259; RN.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:RGD.
DR GO; GO:0005884; C:actin filament; ISO:RGD.
DR GO; GO:0043296; C:apical junction complex; ISO:RGD.
DR GO; GO:0045177; C:apical part of cell; ISO:RGD.
DR GO; GO:0120220; C:basal body patch; ISO:RGD.
DR GO; GO:0044305; C:calyx of Held; ISO:RGD.
DR GO; GO:0005911; C:cell-cell junction; ISO:RGD.
DR GO; GO:0005856; C:cytoskeleton; ISS:AgBase.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0097433; C:dense body; ISS:AgBase.
DR GO; GO:0070062; C:extracellular exosome; ISO:RGD.
DR GO; GO:0031941; C:filamentous actin; ISO:RGD.
DR GO; GO:0005925; C:focal adhesion; ISS:AgBase.
DR GO; GO:0030016; C:myofibril; ISO:RGD.
DR GO; GO:0045335; C:phagocytic vesicle; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISS:AgBase.
DR GO; GO:0098871; C:postsynaptic actin cytoskeleton; IDA:SynGO.
DR GO; GO:0099143; C:presynaptic actin cytoskeleton; IDA:SynGO.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0005522; F:profilin binding; ISO:RGD.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; ISO:RGD.
DR GO; GO:0098973; F:structural constituent of postsynaptic actin cytoskeleton; IDA:SynGO.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
DR GO; GO:0001525; P:angiogenesis; ISO:RGD.
DR GO; GO:0071346; P:cellular response to interferon-gamma; ISO:RGD.
DR GO; GO:0001738; P:morphogenesis of a polarized epithelium; ISO:RGD.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0090303; P:positive regulation of wound healing; ISO:RGD.
DR GO; GO:1902396; P:protein localization to bicellular tight junction; ISO:RGD.
DR GO; GO:0051893; P:regulation of focal adhesion assembly; ISO:RGD.
DR GO; GO:0051492; P:regulation of stress fiber assembly; ISO:RGD.
DR GO; GO:0150111; P:regulation of transepithelial transport; ISO:RGD.
DR GO; GO:0051592; P:response to calcium ion; IEP:RGD.
DR GO; GO:0009612; P:response to mechanical stimulus; IEP:RGD.
DR GO; GO:0045214; P:sarcomere organization; ISO:RGD.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; ISO:RGD.
DR GO; GO:0120192; P:tight junction assembly; ISO:RGD.
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 1: Evidence at protein level;
KW Acetylation; ATP-binding; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Methylation; Nucleotide-binding; Oxidation;
KW Reference proteome.
FT CHAIN 1..375
FT /note="Actin, cytoplasmic 2"
FT /id="PRO_0000000835"
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_0000367102"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P63261"
FT MOD_RES 2
FT /note="N-acetylglutamate; 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:P63258"
FT MOD_RES 84
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63261"
SQ 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
