ACTB_CHICK
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 03-AUG-2022, entry version 140.
DE RecName: Full=Actin, cytoplasmic 1;
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 -!- 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: 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_205518.1.
DR PDB; 3J0S; EM; 9.00 A; A/B/C/D/E/F/G/H/I/J/K/L=2-375.
DR PDBsum; 3J0S; -.
DR AlphaFoldDB; P60706; -.
DR SMR; P60706; -.
DR BioGRID; 676771; 3.
DR DIP; DIP-41284N; -.
DR IntAct; P60706; 1.
DR MINT; P60706; -.
DR STRING; 9031.ENSGALP00000015657; -.
DR PRIDE; P60706; -.
DR Ensembl; ENSGALT00000015673; ENSGALP00000015657; ENSGALG00000009621.
DR Ensembl; ENSGALT00000089197; ENSGALP00000060844; ENSGALG00000009621.
DR GeneID; 396526; -.
DR KEGG; gga:396526; -.
DR CTD; 60; -.
DR VEuPathDB; HostDB:geneid_396526; -.
DR eggNOG; KOG0676; Eukaryota.
DR GeneTree; ENSGT00950000182960; -.
DR HOGENOM; CLU_027965_0_2_1; -.
DR InParanoid; P60706; -.
DR OMA; FHTTAER; -.
DR OrthoDB; 649708at2759; -.
DR Reactome; R-GGA-190873; Gap junction degradation.
DR Reactome; R-GGA-196025; Formation of annular gap junctions.
DR Reactome; R-GGA-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-GGA-3928662; EPHB-mediated forward signaling.
DR Reactome; R-GGA-3928665; EPH-ephrin mediated repulsion of cells.
DR Reactome; R-GGA-437239; Recycling pathway of L1.
DR Reactome; R-GGA-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-GGA-5626467; RHO GTPases activate IQGAPs.
DR Reactome; R-GGA-5663213; RHO GTPases Activate WASPs and WAVEs.
DR Reactome; R-GGA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-GGA-5674135; MAP2K and MAPK activation.
DR Reactome; R-GGA-5689603; UCH proteinases.
DR Reactome; R-GGA-5696394; DNA Damage Recognition in GG-NER.
DR Reactome; R-GGA-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-GGA-9035034; RHOF GTPase cycle.
DR PRO; PR:P60706; -.
DR Proteomes; UP000000539; Chromosome 14.
DR Bgee; ENSGALG00000009621; Expressed in colon and 12 other tissues.
DR ExpressionAtlas; P60706; baseline and differential.
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:0005524; F:ATP binding; IEA:UniProtKB-KW.
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 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 3D-structure; Acetylation; ATP-binding; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Methylation; Nucleotide-binding; Nucleus;
KW 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
