ACTB_PIG
ID ACTB_PIG Reviewed; 375 AA.
AC Q6QAQ1;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 137.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Lee H.Y., Cui X.S., Jeong Y.J., Shin M.L., Hwang K.C., Kim N.H.;
RT "Identification of differentially expressed genes in porcine embryos.";
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
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. Each
CC actin can bind to 4 others. Identified in a IGF2BP1-dependent mRNP
CC granule complex containing untranslated mRNAs. Component of the BAF
CC complex, which includes at least actin (ACTB), ARID1A, ARID1B/BAF250,
CC SMARCA2, SMARCA4/BRG1, ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57
CC SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1, and one or more of
CC SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C. In muscle cells, the
CC BAF complex also contains DPF3. Found in a complex with XPO6, Ran, ACTB
CC and PFN1. Interacts with XPO6 and EMD. Interacts with ERBB2. Interacts
CC with GCSAM (By similarity). Interacts with TBC1D21. Interacts with
CC CPNE1 (via VWFA domain) and CPNE4 (via VWFA domain) (By similarity).
CC Interacts with DHX9 (via C-terminus); this interaction is direct and
CC mediates the attachment to nuclear ribonucleoprotein complexes.
CC Interacts with FAM107A (By similarity). {ECO:0000250|UniProtKB:P60709,
CC ECO:0000250|UniProtKB:P60710}.
CC -!- INTERACTION:
CC Q6QAQ1; Q05G10: g1; Xeno; NbExp=4; IntAct=EBI-12513903, EBI-12685051;
CC Q6QAQ1; Q5U8X5; Xeno; NbExp=6; IntAct=EBI-12513903, EBI-12557210;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P60709}. Nucleus {ECO:0000250|UniProtKB:P60709}.
CC Note=Localized in cytoplasmic mRNP granules containing untranslated
CC mRNAs. {ECO:0000250|UniProtKB:P60709}.
CC -!- PTM: ISGylated. {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. {ECO:0000250|UniProtKB:P60710}.
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:P60709}.
CC -!- PTM: [Actin, cytoplasmic 1, 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:P60709}.
CC -!- PTM: Methylated at His-73 by SETD3 (By similarity). Methylation at His-
CC 73 is required for smooth muscle contraction of the laboring uterus
CC during delivery (By similarity). {ECO:0000250|UniProtKB:P60709,
CC ECO:0000250|UniProtKB:P60710}.
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:P60709}.
CC -!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAS55927.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY550069; AAS55927.1; ALT_INIT; mRNA.
DR RefSeq; XP_003124328.1; XM_003124280.4.
DR PDB; 5ADX; EM; 4.00 A; H=6-375.
DR PDB; 5AFU; EM; 3.50 A; H=6-375.
DR PDB; 6F1T; EM; 3.50 A; H=1-375.
DR PDB; 6F38; EM; 6.70 A; H=1-375.
DR PDB; 6F3A; EM; 8.20 A; H=1-375.
DR PDB; 6ZNL; EM; 3.80 A; H=1-375.
DR PDB; 6ZNM; EM; 4.10 A; H=1-375.
DR PDB; 6ZNN; EM; 4.50 A; H=1-375.
DR PDB; 6ZNO; EM; 6.80 A; H=1-375.
DR PDB; 6ZO4; EM; 8.20 A; H=1-375.
DR PDBsum; 5ADX; -.
DR PDBsum; 5AFU; -.
DR PDBsum; 6F1T; -.
DR PDBsum; 6F38; -.
DR PDBsum; 6F3A; -.
DR PDBsum; 6ZNL; -.
DR PDBsum; 6ZNM; -.
DR PDBsum; 6ZNN; -.
DR PDBsum; 6ZNO; -.
DR PDBsum; 6ZO4; -.
DR AlphaFoldDB; Q6QAQ1; -.
DR SMR; Q6QAQ1; -.
DR IntAct; Q6QAQ1; 2.
DR STRING; 9823.ENSSSCP00000008105; -.
DR PaxDb; Q6QAQ1; -.
DR PeptideAtlas; Q6QAQ1; -.
DR PRIDE; Q6QAQ1; -.
DR Ensembl; ENSSSCT00000042531; ENSSSCP00000035521; ENSSSCG00000007585.
DR Ensembl; ENSSSCT00005032891; ENSSSCP00005020052; ENSSSCG00005020690.
DR Ensembl; ENSSSCT00005032974; ENSSSCP00005020098; ENSSSCG00005020690.
DR Ensembl; ENSSSCT00030004519; ENSSSCP00030001789; ENSSSCG00030003451.
DR Ensembl; ENSSSCT00035051497; ENSSSCP00035020643; ENSSSCG00035038792.
DR Ensembl; ENSSSCT00040066726; ENSSSCP00040028298; ENSSSCG00040049462.
DR Ensembl; ENSSSCT00045046823; ENSSSCP00045032503; ENSSSCG00045027458.
DR Ensembl; ENSSSCT00050088575; ENSSSCP00050037989; ENSSSCG00050065025.
DR Ensembl; ENSSSCT00055024985; ENSSSCP00055019840; ENSSSCG00055012597.
DR Ensembl; ENSSSCT00055025023; ENSSSCP00055019871; ENSSSCG00055012597.
DR Ensembl; ENSSSCT00055025117; ENSSSCP00055019955; ENSSSCG00055012597.
DR Ensembl; ENSSSCT00060025751; ENSSSCP00060010890; ENSSSCG00060019124.
DR Ensembl; ENSSSCT00065051863; ENSSSCP00065022539; ENSSSCG00065037921.
DR Ensembl; ENSSSCT00065051865; ENSSSCP00065022540; ENSSSCG00065037921.
DR Ensembl; ENSSSCT00065051872; ENSSSCP00065022543; ENSSSCG00065037921.
DR Ensembl; ENSSSCT00070022245; ENSSSCP00070018415; ENSSSCG00070011353.
DR Ensembl; ENSSSCT00070022248; ENSSSCP00070018418; ENSSSCG00070011353.
DR GeneID; 414396; -.
DR KEGG; ssc:414396; -.
DR CTD; 60; -.
DR VGNC; VGNC:96915; ACTB.
DR eggNOG; KOG0676; Eukaryota.
DR GeneTree; ENSGT00950000182960; -.
DR HOGENOM; CLU_027965_0_2_1; -.
DR InParanoid; Q6QAQ1; -.
DR OMA; FHTTAER; -.
DR OrthoDB; 649708at2759; -.
DR TreeFam; TF354237; -.
DR Reactome; R-SSC-190873; Gap junction degradation.
DR Reactome; R-SSC-196025; Formation of annular gap junctions.
DR Reactome; R-SSC-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-SSC-3928662; EPHB-mediated forward signaling.
DR Reactome; R-SSC-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-SSC-446353; Cell-extracellular matrix interactions.
DR Reactome; R-SSC-5250924; B-WICH complex positively regulates rRNA expression.
DR Reactome; R-SSC-5626467; RHO GTPases activate IQGAPs.
DR Reactome; R-SSC-5663213; RHO GTPases Activate WASPs and WAVEs.
DR Reactome; R-SSC-5663220; RHO GTPases Activate Formins.
DR Reactome; R-SSC-5674135; MAP2K and MAPK activation.
DR Reactome; R-SSC-5689603; UCH proteinases.
DR Reactome; R-SSC-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-SSC-9035034; RHOF GTPase cycle.
DR Proteomes; UP000008227; Chromosome 3.
DR Proteomes; UP000314985; Chromosome 3.
DR Bgee; ENSSSCG00000007585; Expressed in lung and 42 other tissues.
DR ExpressionAtlas; Q6QAQ1; baseline and differential.
DR Genevisible; Q6QAQ1; SS.
DR GO; GO:0015629; C:actin cytoskeleton; ISS:UniProtKB.
DR GO; GO:0005884; C:actin filament; IBA:GO_Central.
DR GO; GO:0005912; C:adherens junction; IEA:Ensembl.
DR GO; GO:0043296; C:apical junction complex; IEA:Ensembl.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0044305; C:calyx of Held; IEA:Ensembl.
DR GO; GO:0030863; C:cortical cytoskeleton; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IEA:Ensembl.
DR GO; GO:0005856; C:cytoskeleton; ISS:AgBase.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0097433; C:dense body; ISS:AgBase.
DR GO; GO:0005925; C:focal adhesion; ISS:AgBase.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IBA:GO_Central.
DR GO; GO:0000786; C:nucleosome; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:AgBase.
DR GO; GO:0098871; C:postsynaptic actin cytoskeleton; IEA:Ensembl.
DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:Ensembl.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0070160; C:tight junction; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0019894; F:kinesin binding; IEA:Ensembl.
DR GO; GO:0050998; F:nitric-oxide synthase binding; IEA:Ensembl.
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:0030957; F:Tat protein binding; IEA:Ensembl.
DR GO; GO:0034333; P:adherens junction assembly; IEA:Ensembl.
DR GO; GO:0045176; P:apical protein localization; IEA:Ensembl.
DR GO; GO:0007409; P:axonogenesis; IBA:GO_Central.
DR GO; GO:0048870; P:cell motility; IBA:GO_Central.
DR GO; GO:0072749; P:cellular response to cytochalasin B; IEA:Ensembl.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IEA:Ensembl.
DR GO; GO:0043968; P:histone H2A acetylation; IEA:Ensembl.
DR GO; GO:0043967; P:histone H4 acetylation; IEA:Ensembl.
DR GO; GO:0001738; P:morphogenesis of a polarized epithelium; IEA:Ensembl.
DR GO; GO:0032091; P:negative regulation of protein binding; IEA:Ensembl.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; IEA:Ensembl.
DR GO; GO:0071896; P:protein localization to adherens junction; IEA:Ensembl.
DR GO; GO:0051726; P:regulation of cell cycle; IEA:Ensembl.
DR GO; GO:0051621; P:regulation of norepinephrine uptake; IEA:Ensembl.
DR GO; GO:1903076; P:regulation of protein localization to plasma membrane; IEA:Ensembl.
DR GO; GO:0150111; P:regulation of transepithelial transport; IEA:Ensembl.
DR GO; GO:0022898; P:regulation of transmembrane transporter activity; IEA:Ensembl.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IEA:Ensembl.
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 Methylation; Nucleotide-binding; Nucleus; Oxidation; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..375
FT /note="Actin, cytoplasmic 1"
FT /id="PRO_0000291869"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000250|UniProtKB:P60709"
FT CHAIN 2..375
FT /note="Actin, cytoplasmic 1, N-terminally processed"
FT /id="PRO_0000367078"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P60709"
FT MOD_RES 2
FT /note="N-acetylaspartate; in Actin, cytoplasmic 1, N-
FT terminally processed"
FT /evidence="ECO:0000250|UniProtKB:P60709"
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:0000250|UniProtKB:P60710"
FT MOD_RES 84
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:P60709"
FT STRAND 8..11
FT /evidence="ECO:0007829|PDB:5AFU"
FT STRAND 14..23
FT /evidence="ECO:0007829|PDB:5AFU"
FT STRAND 28..32
FT /evidence="ECO:0007829|PDB:5AFU"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:6F1T"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:6F1T"
FT HELIX 56..60
FT /evidence="ECO:0007829|PDB:5AFU"
FT TURN 61..64
FT /evidence="ECO:0007829|PDB:5AFU"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:6F1T"
FT STRAND 70..74
FT /evidence="ECO:0007829|PDB:5AFU"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:6F1T"
FT HELIX 79..90
FT /evidence="ECO:0007829|PDB:5AFU"
FT TURN 91..94
FT /evidence="ECO:0007829|PDB:5AFU"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:5AFU"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:5AFU"
FT HELIX 113..124
FT /evidence="ECO:0007829|PDB:5AFU"
FT STRAND 130..136
FT /evidence="ECO:0007829|PDB:5AFU"
FT HELIX 137..145
FT /evidence="ECO:0007829|PDB:5AFU"
FT STRAND 151..155
FT /evidence="ECO:0007829|PDB:5AFU"
FT STRAND 160..163
FT /evidence="ECO:0007829|PDB:5AFU"
FT STRAND 165..168
FT /evidence="ECO:0007829|PDB:5AFU"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:5AFU"
FT STRAND 176..179
FT /evidence="ECO:0007829|PDB:5AFU"
FT HELIX 182..195
FT /evidence="ECO:0007829|PDB:5AFU"
FT HELIX 203..215
FT /evidence="ECO:0007829|PDB:5AFU"
FT HELIX 223..232
FT /evidence="ECO:0007829|PDB:5AFU"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:5AFU"
FT STRAND 238..241
FT /evidence="ECO:0007829|PDB:5AFU"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:5AFU"
FT STRAND 247..251
FT /evidence="ECO:0007829|PDB:5AFU"
FT HELIX 253..256
FT /evidence="ECO:0007829|PDB:5AFU"
FT HELIX 259..262
FT /evidence="ECO:0007829|PDB:5AFU"
FT TURN 264..268
FT /evidence="ECO:0007829|PDB:5AFU"
FT HELIX 274..284
FT /evidence="ECO:0007829|PDB:5AFU"
FT HELIX 287..289
FT /evidence="ECO:0007829|PDB:5AFU"
FT HELIX 291..295
FT /evidence="ECO:0007829|PDB:5AFU"
FT STRAND 297..301
FT /evidence="ECO:0007829|PDB:5AFU"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:5AFU"
FT HELIX 309..320
FT /evidence="ECO:0007829|PDB:5AFU"
FT TURN 333..336
FT /evidence="ECO:0007829|PDB:6F1T"
FT HELIX 338..348
FT /evidence="ECO:0007829|PDB:5AFU"
FT HELIX 351..354
FT /evidence="ECO:0007829|PDB:5AFU"
FT HELIX 359..364
FT /evidence="ECO:0007829|PDB:5AFU"
FT HELIX 367..369
FT /evidence="ECO:0007829|PDB:5AFU"
FT HELIX 370..374
FT /evidence="ECO:0007829|PDB:5AFU"
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
