ACTB1_DANRE
ID ACTB1_DANRE Reviewed; 375 AA.
AC Q7ZVI7; O73815; P12714; Q6P3K9;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Actin, cytoplasmic 1;
DE AltName: Full=Beta-actin-1;
DE Contains:
DE RecName: Full=Actin, cytoplasmic 1, N-terminally processed;
GN Name=actba; Synonyms=bact, bactin1, bactzf;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Embryo;
RX PubMed=9987040; DOI=10.1046/j.1460-9568.1999.00474.x;
RA Barrallo A., Gonzalez-Sarmiento R., Garcia-Isidoro M., Cidad P.,
RA Porteros A., Rodriguez R.E.;
RT "Differential brain expression of a new beta-actin gene from zebrafish
RT (Danio rerio).";
RL Eur. J. Neurosci. 11:369-372(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 -!- TISSUE SPECIFICITY: Skeletal muscle, heart, gill, digestive tissue and
CC brain (PubMed:9987040). Widespread expression throughout the brain,
CC with highest levels in regions where neuronal proliferation is greatest
CC (PubMed:9987040). {ECO:0000269|PubMed:9987040}.
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. Methylation stabilizes actin
CC filaments. {ECO:0000250|UniProtKB:P60706}.
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; AF057040; AAC13314.1; -; mRNA.
DR EMBL; BC045846; AAH45846.1; -; mRNA.
DR EMBL; BC063950; AAH63950.1; -; mRNA.
DR RefSeq; NP_571106.1; NM_131031.1.
DR AlphaFoldDB; Q7ZVI7; -.
DR SMR; Q7ZVI7; -.
DR IntAct; Q7ZVI7; 1.
DR MINT; Q7ZVI7; -.
DR STRING; 7955.ENSDARP00000054986; -.
DR PaxDb; Q7ZVI7; -.
DR Ensembl; ENSDART00000054987; ENSDARP00000054986; ENSDARG00000037746.
DR Ensembl; ENSDART00000182072; ENSDARP00000154160; ENSDARG00000113649.
DR GeneID; 57934; -.
DR KEGG; dre:57934; -.
DR CTD; 57934; -.
DR ZFIN; ZDB-GENE-000329-1; actb1.
DR eggNOG; KOG0676; Eukaryota.
DR GeneTree; ENSGT00950000182960; -.
DR InParanoid; Q7ZVI7; -.
DR OMA; WICKSEY; -.
DR OrthoDB; 649708at2759; -.
DR PhylomeDB; Q7ZVI7; -.
DR TreeFam; TF354237; -.
DR Reactome; R-DRE-190873; Gap junction degradation.
DR Reactome; R-DRE-196025; Formation of annular gap junctions.
DR Reactome; R-DRE-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-DRE-3928662; EPHB-mediated forward signaling.
DR Reactome; R-DRE-3928665; EPH-ephrin mediated repulsion of cells.
DR Reactome; R-DRE-418990; Adherens junctions interactions.
DR Reactome; R-DRE-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-DRE-446353; Cell-extracellular matrix interactions.
DR Reactome; R-DRE-5250924; B-WICH complex positively regulates rRNA expression.
DR Reactome; R-DRE-5626467; RHO GTPases activate IQGAPs.
DR Reactome; R-DRE-5663213; RHO GTPases Activate WASPs and WAVEs.
DR Reactome; R-DRE-5663220; RHO GTPases Activate Formins.
DR Reactome; R-DRE-5674135; MAP2K and MAPK activation.
DR Reactome; R-DRE-5689603; UCH proteinases.
DR Reactome; R-DRE-5696394; DNA Damage Recognition in GG-NER.
DR Reactome; R-DRE-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-DRE-9035034; RHOF GTPase cycle.
DR PRO; PR:Q7ZVI7; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 1.
DR Bgee; ENSDARG00000037746; Expressed in granulocyte and 27 other tissues.
DR ExpressionAtlas; Q7ZVI7; 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:0005856; C:cytoskeleton; ISS:AgBase.
DR GO; GO:0097433; C:dense body; ISS:AgBase.
DR GO; GO:0005925; C:focal adhesion; ISS:AgBase.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:AgBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0098973; F:structural constituent of postsynaptic actin cytoskeleton; 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 Acetylation; ATP-binding; Cytoplasm; Cytoskeleton; Methylation;
KW Nucleotide-binding; Nucleus; Oxidation; Reference proteome.
FT CHAIN 1..375
FT /note="Actin, cytoplasmic 1"
FT /id="PRO_0000367087"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000250|UniProtKB:P60706"
FT CHAIN 2..375
FT /note="Actin, cytoplasmic 1, N-terminally processed"
FT /id="PRO_0000000795"
FT MOD_RES 1
FT /note="N-acetylmethionine; in Actin, cytoplasmic 1;
FT alternate"
FT /evidence="ECO:0000250|UniProtKB:P60706"
FT MOD_RES 2
FT /note="N-acetylaspartate; in Actin, cytoplasmic 1, N-
FT terminally processed"
FT /evidence="ECO:0000250|UniProtKB:P60706"
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:30626964"
FT CONFLICT 66
FT /note="T -> S (in Ref. 2; AAH45846)"
FT /evidence="ECO:0000305"
FT CONFLICT 104
FT /note="L -> V (in Ref. 1; AAC13314)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 375 AA; 41767 MW; CDAC90490F8F11AF CRC64;
MDEEIAALVV DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS
KRGILTLKYP IEHGIVTNWD DMEKIWHHTF YNELRVAPEE HPVLLTEAPL NPKANREKMT
QIMFETFNTP AMYVAIQAVL SLYASGRTTG IVMDSGDGVT HTVPIYEGYA LPHAILRLDL
AGRDLTDYLM KILTERGYSF TTTAEREIVR DIKEKLCYVA LDFEQEMGTA ASSSSLEKSY
ELPDGQVITI GNERFRCPEA LFQPSFLGME SCGIHETTFN SIMKCDVDIR KDLYANTVLS
GGTTMYPGIA DRMQKEITSL APSTMKIKII APPERKYSVW IGGSILASLS TFQQMWISKQ
EYDESGPSIV HRKCF
