Reviewed, UniProtKB/Swiss-Prot P60707 (ACTB_TRIVU)

Names and origin

Protein names

Recommended name:
    Actin, cytoplasmic 1
Alternative name(s):
    Beta-actin
Cleaved into the following chain:
    1- Recommended name:
            Actin, cytoplasmic 1, N-terminally processed

Gene names

Name:

ACTB

Organism

Trichosurus vulpecula (Brush-tailed possum)

Taxonomic identifier

9337 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Metatheria › Diprotodontia › Phalangeridae › Trichosurus

Protein attributes

Sequence length	375 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
Subunit structure	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 mRNP granule complex, at least composed of ACTB, ACTN4, DHX9, ERG, HNRNPA1, HNRNPA2B1, HNRNPAB, HNRNPD, HNRNPL, HNRNPR, HNRNPU, HSPA1, HSPA8, IGF2BP1, ILF2, ILF3, NCBP1, NCL, PABPC1, PABPC4, PABPN1, RPLP0, RPS3, RPS3A, RPS4X, RPS8, RPS9, SYNCRIP, TROVE2, YBX1 and 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 MLL5, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT. Interacts with XPO6 and EMD By similarity.
Subcellular location	Cytoplasm › cytoskeleton. Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs 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.
Sequence similarities	Belongs to the actin family.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton
Ligand	ATP-binding Nucleotide-binding
PTM	Acetylation Methylation Phosphoprotein
Gene Ontology (GO)
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 375	375	Actin, cytoplasmic 1		PRO_0000367085
	Initiator methionine	1	1	Removed; alternate By similarity
	Chain	2 – 375	374	Actin, cytoplasmic 1, N-terminally processed		PRO_0000000787
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine; in Actin, cytoplasmic 1; alternate By similarity
	Modified residue	2	1	N-acetylaspartate; in Actin, cytoplasmic 1, N-terminally processed By similarity
	Modified residue	53	1	Phosphotyrosine By similarity
	Modified residue	73	1	Tele-methylhistidine By similarity
	Modified residue	91	1	Phosphotyrosine By similarity
	Modified residue	166	1	Phosphotyrosine By similarity
	Modified residue	169	1	Phosphotyrosine By similarity
	Modified residue	198	1	Phosphotyrosine By similarity
	Modified residue	218	1	Phosphotyrosine By similarity
	Modified residue	294	1	Phosphotyrosine By similarity
	Modified residue	318	1	Phosphothreonine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P60707-1 [UniParc]. Last modified April 1, 1988. Version 1. Checksum: 6AFD05CA94E360E2	FASTA	375	41,737
	10 20 30 40 50 60 MDDDIAALVV DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS 70 80 90 100 110 120 KRGILTLKYP IEHGIVTNWD DMEKIWHHTF YNELRVAPEE HPVLLTEAPL NPKANREKMT 130 140 150 160 170 180 QIMFETFNTP AMYVAIQAVL SLYASGRTTG IVMDSGDGVT HTVPIYEGYA LPHAILRLDL 190 200 210 220 230 240 AGRDLTDYLM KILTERGYSF TTTAEREIVR DIKEKLCYVA LDFEQEMATA ASSSSLEKSY 250 260 270 280 290 300 ELPDGQVITI GNERFRCPEA LFQPSFLGME SCGIHETTFN SIMKCDVDIR KDLYANTVLS 310 320 330 340 350 360 GGTTMYPGIA DRMQKEITAL APSTMKIKII APPERKYSVW IGGSILASLS TFQQMWISKQ 370 EYDESGPSIV HRKCF

References

[1]	"Isolation of the full-length cDNA for beta-actin from the common brushtail possum." Wedlock D.N., Hickson R., Buddle B.M. Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF076190 mRNA. Translation: AAC26519.1.
3D structure databases
SMR	P60707. Positions 4-371.
ModBase	Search...
2-D gel databases
Cornea-2DPAGE	P02570.
Proteomic databases
PRIDE	P60707.
Phylogenomic databases
HOVERGEN	P60707.
Family and domain databases
InterPro	IPR004000. Actin-like. IPR004001. Actin_CS. [Graphical view]
PANTHER	PTHR11937. Actin_like. 1 hit.
Pfam	PF00022. Actin. 1 hit. [Graphical view]
PRINTS	PR00190. ACTIN.
SMART	SM00268. ACTIN. 1 hit. [Graphical view]
PROSITE	PS00406. ACTINS_1. 1 hit. PS00432. ACTINS_2. 1 hit. PS01132. ACTINS_ACT_LIKE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ACTB_TRIVU

Accession

Primary (citable) accession number: P60707
Secondary accession number(s): P02570 , P70514, P99021, Q11211, Q64316

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	April 1, 1988
Last modified:	November 3, 2009
This is version 46 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)