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Protein

Actin, cytoplasmic 1

Gene

ACTB

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.By similarity

Miscellaneous

In vertebrates 3 main groups of actin isoforms, alpha, beta and gamma have been identified. The alpha actins are found in muscle tissues and are a major constituent of the contractile apparatus. The beta and gamma actins coexist in most cell types as components of the cytoskeleton and as mediators of internal cell motility (By similarity).By similarity

GO - Molecular functioni

Keywordsi

LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-SSC-190873. Gap junction degradation.
R-SSC-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-SSC-3928662. EPHB-mediated forward signaling.
R-SSC-418990. Adherens junctions interactions.
R-SSC-437239. Recycling pathway of L1.
R-SSC-4420097. VEGFA-VEGFR2 Pathway.
R-SSC-445095. Interaction between L1 and Ankyrins.
R-SSC-446353. Cell-extracellular matrix interactions.
R-SSC-5250924. B-WICH complex positively regulates rRNA expression.
R-SSC-5626467. RHO GTPases activate IQGAPs.
R-SSC-5663213. RHO GTPases Activate WASPs and WAVEs.
R-SSC-5663220. RHO GTPases Activate Formins.
R-SSC-5689603. UCH proteinases.
R-SSC-5696394. DNA Damage Recognition in GG-NER.
R-SSC-8856828. Clathrin-mediated endocytosis.

Names & Taxonomyi

Protein namesi
Recommended name:
Actin, cytoplasmic 1
Alternative name(s):
Beta-actin
Cleaved into the following chain:
Gene namesi
Name:ACTB
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Chromosome 3

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002918691 – 375Actin, cytoplasmic 1Add BLAST375
Initiator methionineiRemoved; alternateBy similarity
ChainiPRO_00003670782 – 375Actin, cytoplasmic 1, N-terminally processedAdd BLAST374

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei2N-acetylaspartate; in Actin, cytoplasmic 1, N-terminally processedBy similarity1
Modified residuei44Methionine (R)-sulfoxideBy similarity1
Modified residuei47Methionine (R)-sulfoxideBy similarity1
Modified residuei73Tele-methylhistidineBy similarity1
Modified residuei84N6-methyllysineBy similarity1

Post-translational modificationi

ISGylated.By similarity
Oxidation of Met-44 and Met-47 by MICALs (MICAL1, MICAL2 or MICAL3) to form methionine sulfoxide promotes actin filament depolymerization. MICAL1 and MICAL2 produce the (R)-S-oxide form. The (R)-S-oxide form is reverted by MSRB1 and MSRB2, which promote actin repolymerization (By similarity).By similarity
Monomethylation at Lys-84 (K84me1) regulates actin-myosin interaction and actomyosin-dependent processes. Demethylation by ALKBH4 is required for maintaining actomyosin dynamics supporting normal cleavage furrow ingression during cytokinesis and cell migration (By similarity).By similarity

Keywords - PTMi

Acetylation, Methylation, Oxidation, Ubl conjugation

Proteomic databases

PaxDbiQ6QAQ1.
PeptideAtlasiQ6QAQ1.
PRIDEiQ6QAQ1.

Expressioni

Gene expression databases

BgeeiENSSSCG00000007585.
GenevisibleiQ6QAQ1. SS.

Interactioni

Subunit structurei

Polymerization of globular actin (G-actin) leads to a structural filament (F-actin) in the form of a two-stranded helix. Each actin can bind to 4 others. Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Component of the BAF complex, which includes at least actin (ACTB), ARID1A, ARID1B/BAF250, SMARCA2, SMARCA4/BRG1, ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57, SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1, and one or more of SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C. In muscle cells, the BAF complex also contains DPF3. Found in a complex with XPO6, Ran, ACTB and PFN1. Component of the MLL5-L complex, at least composed of KMT2E/MLL5, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT. Interacts with XPO6 and EMD. Interacts with ERBB2. Interacts with GCSAM. Interacts with CPNE1 (via VWFA domain) and CPNE4 (via VWFA domain). Interacts with TBC1D21. Interacts with DHX9 (via C-terminus); this interaction is direct and mediates the attachment to nuclear ribonucleoprotein complexes.By similarity

Binary interactionsi

Show more details

Protein-protein interaction databases

IntActiQ6QAQ1. 2 interactors.
STRINGi9823.ENSSSCP00000008105.

Structurei

Secondary structure

1375
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi8 – 11Combined sources4
Beta strandi14 – 23Combined sources10
Beta strandi28 – 32Combined sources5
Helixi56 – 60Combined sources5
Turni61 – 64Combined sources4
Beta strandi70 – 74Combined sources5
Helixi79 – 90Combined sources12
Turni91 – 94Combined sources4
Turni98 – 100Combined sources3
Beta strandi103 – 107Combined sources5
Helixi113 – 124Combined sources12
Beta strandi130 – 136Combined sources7
Helixi137 – 145Combined sources9
Beta strandi151 – 155Combined sources5
Beta strandi160 – 163Combined sources4
Beta strandi165 – 168Combined sources4
Helixi172 – 174Combined sources3
Beta strandi176 – 179Combined sources4
Helixi182 – 195Combined sources14
Helixi203 – 215Combined sources13
Helixi223 – 232Combined sources10
Beta strandi234 – 236Combined sources3
Beta strandi238 – 241Combined sources4
Beta strandi243 – 245Combined sources3
Beta strandi247 – 251Combined sources5
Helixi253 – 256Combined sources4
Helixi259 – 262Combined sources4
Turni264 – 268Combined sources5
Helixi274 – 284Combined sources11
Helixi287 – 289Combined sources3
Helixi291 – 295Combined sources5
Beta strandi297 – 301Combined sources5
Helixi302 – 304Combined sources3
Helixi309 – 320Combined sources12
Helixi338 – 348Combined sources11
Helixi351 – 354Combined sources4
Helixi359 – 364Combined sources6
Helixi367 – 369Combined sources3
Helixi370 – 374Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5ADXelectron microscopy4.00H6-375[»]
5AFUelectron microscopy3.50H6-375[»]
ProteinModelPortaliQ6QAQ1.
SMRiQ6QAQ1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the actin family.Curated

Phylogenomic databases

eggNOGiKOG0676. Eukaryota.
COG5277. LUCA.
GeneTreeiENSGT00760000118957.
HOGENOMiHOG000233340.
HOVERGENiHBG003771.
InParanoidiQ6QAQ1.
KOiK05692.
OMAiMERGYPF.
OrthoDBiEOG091G08LD.
TreeFamiTF354237.

Family and domain databases

InterProiView protein in InterPro
IPR004000. Actin.
IPR020902. Actin/actin-like_CS.
IPR004001. Actin_CS.
PANTHERiPTHR11937. PTHR11937. 1 hit.
PfamiView protein in Pfam
PF00022. Actin. 1 hit.
PRINTSiPR00190. ACTIN.
SMARTiView protein in SMART
SM00268. ACTIN. 1 hit.
PROSITEiView protein in PROSITE
PS00406. ACTINS_1. 1 hit.
PS00432. ACTINS_2. 1 hit.
PS01132. ACTINS_ACT_LIKE. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q6QAQ1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDDDIAALVV DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK
60 70 80 90 100
DSYVGDEAQS KRGILTLKYP IEHGIVTNWD DMEKIWHHTF YNELRVAPEE
110 120 130 140 150
HPVLLTEAPL NPKANREKMT QIMFETFNTP AMYVAIQAVL SLYASGRTTG
160 170 180 190 200
IVMDSGDGVT HTVPIYEGYA LPHAILRLDL AGRDLTDYLM KILTERGYSF
210 220 230 240 250
TTTAEREIVR DIKEKLCYVA LDFEQEMATA ASSSSLEKSY ELPDGQVITI
260 270 280 290 300
GNERFRCPEA LFQPSFLGME SCGIHETTFN SIMKCDVDIR KDLYANTVLS
310 320 330 340 350
GGTTMYPGIA DRMQKEITAL APSTMKIKII APPERKYSVW IGGSILASLS
360 370
TFQQMWISKQ EYDESGPSIV HRKCF
Length:375
Mass (Da):41,737
Last modified:June 26, 2007 - v2
Checksum:i6AFD05CA94E360E2
GO

Sequence cautioni

The sequence AAS55927 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY550069 mRNA. Translation: AAS55927.1. Different initiation.
RefSeqiXP_003124328.1. XM_003124280.4.
UniGeneiSsc.10316.

Genome annotation databases

EnsembliENSSSCT00000048365; ENSSSCP00000051515; ENSSSCG00000007585.
ENSSSCT00000063067; ENSSSCP00000058234; ENSSSCG00000007585.
ENSSSCT00000065139; ENSSSCP00000034004; ENSSSCG00000007585.
GeneIDi414396.
KEGGissc:414396.

Similar proteinsi

Entry informationi

Entry nameiACTB_PIG
AccessioniPrimary (citable) accession number: Q6QAQ1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: June 26, 2007
Last modified: November 22, 2017
This is version 106 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families