ID   ACTB_CHICK              Reviewed;         375 AA.
AC   P60706; P02570; P70514; P99021; Q11211; Q64316;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1988, sequence version 1.
DT   02-SEP-2026, entry version 158.
DE   RecName: Full=Actin, cytoplasmic 1;
DE            EC=3.6.4.- {ECO:0000250|UniProtKB:P68137};
DE   AltName: Full=Beta-actin;
DE   Contains:
DE     RecName: Full=Actin, cytoplasmic 1, N-terminally processed;
GN   Name=ACTB;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6324080; DOI=10.1093/nar/11.23.8287;
RA   Kost T.A., Theodorakis N., Hughes S.H.;
RT   "The nucleotide sequence of the chick cytoplasmic beta-actin gene.";
RL   Nucleic Acids Res. 11:8287-8301(1983).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Wang H., Morais R.;
RT   "Nucleotide sequence of a beta-actin cDNA from mitochondrial DNA-depleted
RT   chicken cells.";
RL   Submitted (JAN-1993) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PROTEIN SEQUENCE OF 2-37; 85-113; 178-191; 197-206; 239-254; 291-326 AND
RP   360-372, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ASP-2, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=B-cell lymphoma;
RA   Bienvenut W.V., Black E.J., Gillespie D.A.;
RL   Submitted (JAN-2007) to UniProtKB.
RN   [4]
RP   METHYLATION AT HIS-73, AND MUTAGENESIS OF HIS-73.
RX   PubMed=11955010; DOI=10.1006/jmbi.2002.5436;
RA   Nyman T., Schueler H., Korenbaum E., Schutt C.E., Karlsson R., Lindberg U.;
RT   "The role of MeH73 in actin polymerization and ATP hydrolysis.";
RL   J. Mol. Biol. 317:577-589(2002).
RN   [5]
RP   METHYLATION AT HIS-73.
RX   PubMed=30626964; DOI=10.1038/s41586-018-0821-8;
RA   Wilkinson A.W., Diep J., Dai S., Liu S., Ooi Y.S., Song D., Li T.M.,
RA   Horton J.R., Zhang X., Liu C., Trivedi D.V., Ruppel K.M.,
RA   Vilches-Moure J.G., Casey K.M., Mak J., Cowan T., Elias J.E.,
RA   Nagamine C.M., Spudich J.A., Cheng X., Carette J.E., Gozani O.;
RT   "SETD3 is an actin histidine methyltransferase that prevents primary
RT   dystocia.";
RL   Nature 565:372-376(2019).
CC   -!- FUNCTION: Actin is a highly conserved protein that polymerizes to
CC       produce filaments that form cross-linked networks in the cytoplasm of
CC       cells. Actin exists in both monomeric (G-actin) and polymeric (F-actin)
CC       forms, both forms playing key functions, such as cell motility and
CC       contraction. In addition to their role in the cytoplasmic cytoskeleton,
CC       G- and F-actin also localize in the nucleus, and regulate gene
CC       transcription and motility and repair of damaged DNA.
CC       {ECO:0000250|UniProtKB:P60709}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + phosphate + H(+); Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000250|UniProtKB:P68137};
CC   -!- SUBUNIT: Polymerization of globular actin (G-actin) leads to a
CC       structural filament (F-actin) in the form of a two-stranded helix (By
CC       similarity). Each actin can bind to 4 others (By similarity).
CC       {ECO:0000250|UniProtKB:P60709, ECO:0000250|UniProtKB:P60710}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:P60710}. Nucleus {ECO:0000250|UniProtKB:O93400}.
CC   -!- PTM: [Actin, cytoplasmic 1]: N-terminal cleavage of acetylated
CC       methionine of immature cytoplasmic actin by ACTMAP.
CC       {ECO:0000250|UniProtKB:P60709}.
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 (By similarity). {ECO:0000250|UniProtKB:P60710}.
CC   -!- PTM: Methylation at His-73 by SETD3 (PubMed:30626964). Methylation
CC       stabilizes actin filaments (PubMed:11955010).
CC       {ECO:0000269|PubMed:11955010, ECO:0000269|PubMed:30626964}.
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. {ECO:0000250|UniProtKB:O93400}.
CC   -!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
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DR   EMBL; X00182; CAA25004.1; -; Genomic_DNA.
DR   EMBL; L08165; AAA48615.1; -; mRNA.
DR   PIR; A20888; ATCHB.
DR   RefSeq; NP_990849.1; NM_205518.2.
DR   PDB; 3J0S; EM; 9.00 A; A/B/C/D/E/F/G/H/I/J/K/L=2-375.
DR   AlphaFoldDB; P60706; -.
DR   EMDB; EMD-5354; -.
DR   SASBDB; P60706; -.
DR   SMR; P60706; -.
DR   BioGRID; 676771; 5.
DR   DIP; DIP-41284N; -.
DR   FunCoup; P60706; 2342.
DR   IntAct; P60706; 1.
DR   MINT; P60706; -.
DR   STRING; 9031.ENSGALP00000060844; -.
DR   PaxDb; 9031-ENSGALP00000060844; -.
DR   GeneID; 396526; -.
DR   KEGG; gga:396526; -.
DR   CTD; 60; -.
DR   VEuPathDB; HostDB:geneid_396526; -.
DR   eggNOG; KOG0676; Eukaryota.
DR   HOGENOM; CLU_027965_0_2_1; -.
DR   InParanoid; P60706; -.
DR   OMA; FHTTAER; -.
DR   OrthoDB; 9240758at2759; -.
DR   EvolutionaryTrace; P60706; -.
DR   PRO; PR:P60706; -.
DR   Proteomes; UP000000539; Chromosome 14.
DR   Bgee; ENSGALG00000009621; Expressed in colon and 12 other cell types or tissues.
DR   GO; GO:0015629; C:actin cytoskeleton; ISS:UniProtKB.
DR   GO; GO:0005884; C:actin filament; IBA:GO_Central.
DR   GO; GO:0030424; C:axon; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IDA:AgBase.
DR   GO; GO:0005856; C:cytoskeleton; IDA:AgBase.
DR   GO; GO:0097433; C:dense body; IDA:AgBase.
DR   GO; GO:0005925; C:focal adhesion; IDA:AgBase.
DR   GO; GO:0030027; C:lamellipodium; IDA:AgBase.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:AgBase.
DR   GO; GO:0045202; C:synapse; IBA:GO_Central.
DR   GO; GO:0016887; F:ATP hydrolysis activity; ISS:UniProtKB.
DR   GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR   GO; GO:0098973; F:structural constituent of postsynaptic actin cytoskeleton; IBA:GO_Central.
DR   GO; GO:0007409; P:axonogenesis; IBA:GO_Central.
DR   GO; GO:0048870; P:cell motility; IBA:GO_Central.
DR   CDD; cd10224; ASKHA_NBD_actin; 1.
DR   FunFam; 3.30.420.40:FF:000131; Actin, alpha skeletal muscle; 1.
DR   FunFam; 3.30.420.40:FF:000291; Actin, alpha skeletal muscle; 1.
DR   FunFam; 3.90.640.10:FF:000047; Actin, alpha skeletal muscle; 1.
DR   FunFam; 3.30.420.40:FF:000058; Putative actin-related protein 5; 1.
DR   Gene3D; 3.30.420.40; -; 2.
DR   Gene3D; 3.90.640.10; Actin, Chain A, domain 4; 1.
DR   InterPro; IPR004000; Actin.
DR   InterPro; IPR020902; Actin/actin-like_CS.
DR   InterPro; IPR004001; Actin_CS.
DR   InterPro; IPR043129; ATPase_NBD.
DR   PANTHER; PTHR11937; ACTIN; 1.
DR   Pfam; PF00022; Actin; 1.
DR   PRINTS; PR00190; ACTIN.
DR   SMART; SM00268; ACTIN; 1.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   PROSITE; PS00406; ACTINS_1; 1.
DR   PROSITE; PS00432; ACTINS_2; 1.
DR   PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
DR   PDBsum; 3J0S; -.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; ATP-binding; Cytoplasm; Cytoskeleton;
KW   Direct protein sequencing; Hydrolase; Methylation; Nucleotide-binding;
KW   Nucleus; Oxidation; Reference proteome.
FT   CHAIN           1..375
FT                   /note="Actin, cytoplasmic 1"
FT                   /id="PRO_0000367086"
FT   INIT_MET        1
FT                   /note="Removed; alternate"
FT                   /evidence="ECO:0000269|Ref.3"
FT   CHAIN           2..375
FT                   /note="Actin, cytoplasmic 1, N-terminally processed"
FT                   /id="PRO_0000000789"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine; in Actin, cytoplasmic 1;
FT                   alternate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N-acetylaspartate; in Actin, cytoplasmic 1, N-
FT                   terminally processed"
FT                   /evidence="ECO:0000269|Ref.3"
FT   MOD_RES         44
FT                   /note="Methionine (R)-sulfoxide"
FT                   /evidence="ECO:0000250|UniProtKB:P60710"
FT   MOD_RES         47
FT                   /note="Methionine (R)-sulfoxide"
FT                   /evidence="ECO:0000250|UniProtKB:P60710"
FT   MOD_RES         73
FT                   /note="Tele-methylhistidine"
FT                   /evidence="ECO:0000269|PubMed:11955010,
FT                   ECO:0000269|PubMed:30626964"
FT   MUTAGEN         73
FT                   /note="H->A: ATP is exchanged at an increased rate;
FT                   decreased the thermal stability of actin monomers."
FT                   /evidence="ECO:0000269|PubMed:11955010"
FT   CONFLICT        336
FT                   /note="K -> R (in Ref. 1; CAA25004)"
FT                   /evidence="ECO:0000305"
SQ   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
//