P60712 (ACTB_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Actin, cytoplasmic 1

Alternative name(s):
Beta-actin

Cleaved into the following chain:

1. Actin, cytoplasmic 1, N-terminally processed

Gene names

Name:

ACTB

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

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. Interacts with ERBB2 By similarity.
Subcellular location	Cytoplasm › cytoskeleton. Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs By similarity.
Post-translational modification	ISGylated 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 Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	chaperone mediated protein folding independent of cofactor Traceable author statement. Source: Reactome
Cellular component	NuA4 histone acetyltransferase complex Inferred from sequence or structural similarity. Source: AgBase cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Traceable author statement. Source: Reactome
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW
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_0000367066

Initiator methionine

1

1

Removed; alternate By similarity

Chain

2 – 375

374

Actin, cytoplasmic 1, N-terminally processed

PRO_0000000757

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

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

Experimental info

Sequence conflict

126

1

T → A in AAI42414. Ref.3

Sequence conflict

204 – 206

3

AER → GRA in AAM98378. Ref.1

Sequence conflict

281

1

S → F in AAM98378. Ref.1

Secondary structure

1

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375

Helix Strand Turn

Details...

Beta strand

8 – 12

5

Beta strand

14 – 21

8

Beta strand

30 – 32

3

Beta strand

35 – 38

4

Beta strand

51 – 54

4

Helix

57 – 61

5

Turn

62 – 64

3

Beta strand

65 – 68

4

Helix

79 – 91

13

Turn

92 – 94

3

Helix

98 – 100

3

Beta strand

103 – 107

5

Helix

113 – 125

13

Beta strand

130 – 136

7

Helix

137 – 144

8

Beta strand

148 – 155

8

Beta strand

160 – 166

7

Helix

172 – 174

3

Beta strand

176 – 179

4

Helix

182 – 193

12

Helix

194 – 196

3

Beta strand

202 – 204

3

Helix

206 – 216

11

Helix

223 – 231

9

Beta strand

234 – 236

3

Beta strand

238 – 241

4

Beta strand

243 – 245

3

Beta strand

247 – 251

5

Helix

252 – 256

5

Helix

258 – 260

3

Helix

264 – 267

4

Helix

274 – 284

11

Helix

287 – 293

7

Beta strand

297 – 301

5

Helix

302 – 304

3

Helix

309 – 318

10

Turn

333 – 336

4

Helix

338 – 346

9

Helix

350 – 354

5

Beta strand

356 – 358

3

Helix

359 – 365

7

Helix

369 – 373

5

Sequences

	Sequence		Length	Mass (Da)
	P60712 [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

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Bovine mammary gene expression profiling using a cDNA microarray enhanced for mammary-specific transcripts." Suchyta S.P., Sipkovsky S., Halgren R.G., Kruska R., Elftman M., Weber-Nielsen M., Vandehaar M.J., Xiao L., Tempelman R.J., Coussens P.M. Physiol. Genomics 16:8-18(2003) [PubMed: 14559974] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Mammary gland.
[2]	"Characterization of 954 bovine full-CDS cDNA sequences." Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L. BMC Genomics 6:166-166(2005) [PubMed: 16305752] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	NIH - Mammalian Gene Collection (MGC) project Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Crossbred X Angus and Hereford. Tissue: Ileum and Thymus.
[4]	"Actin amino-acid sequences. Comparison of actins from calf thymus, bovine brain, and SV40-transformed mouse 3T3 cells with rabbit skeletal muscle actin." Vandekerckhove J., Weber K. Eur. J. Biochem. 90:451-462(1978) [PubMed: 213279] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-375. Tissue: Brain.
[5]	"Regulation of protein synthesis in mitogen-activated bovine lymphocytes. Analysis of actin-specific and total mRNA accumulation and utilization." Degen J.L., Neubauer M.G., Friezner Degen S.J., Seyfried C.E., Morris D.R. J. Biol. Chem. 258:12153-12162(1983) [PubMed: 6195151] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 77-228 AND 345-375.
[6]	"The structure of crystalline profilin-beta-actin." Schutt C.E., Myslik J.C., Rozycki M.D., Goonesekere N.C.W., Lindberg U. Nature 365:810-816(1993) [PubMed: 8413665] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF COMPLEX WITH PROFILIN.
[7]	"The structure of an open state of beta-actin at 2.65-A resolution." Chik J.K., Lindberg U., Schutt C.E. J. Mol. Biol. 263:607-623(1996) [PubMed: 8918942] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF COMPLEX WITH PROFILIN.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AY141970 mRNA. Translation: AAM98378.1.
BT030480 mRNA. Translation: ABQ12920.1.
BC102948 mRNA. Translation: AAI02949.1.
BC142413 mRNA. Translation: AAI42414.1.
K00622 mRNA. Translation: AAA30352.1.
K00623 mRNA. Translation: AAA30353.1.

IPI

IPI00698900.

PIR

ATBOB. E14185.

RefSeq

NP_776404.2. NM_173979.3.

UniGene

Bt.14186.
Bt.38667.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1HLU	X-ray	2.65	A	2-375	[»]
2BTF	X-ray	2.55	A	2-375	[»]
2OAN	X-ray	2.61	A/B/C/D	1-375	[»]

ProteinModelPortal

P60712.

SMR

P60712. Positions 2-375.

ModBase

Search...

Protein-protein interaction databases

STRING

P60712.

Proteomic databases

PRIDE

P60712.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

280979.

KEGG

bta:280979.

Organism-specific databases

CTD

60.

Phylogenomic databases

eggNOG

maNOG18915.

HOVERGEN

HBG003771.

InParanoid

P60712.

OrthoDB

EOG41JZC9.

PhylomeDB

P60712.

Enzyme and pathway databases

Reactome

REACT_108005. Metabolism of proteins.
REACT_17056. Cooperation of Prefoldin and TriC/CCT in actin and tubulin folding.

Family and domain databases

InterPro

IPR004000. Actin-like.
IPR020902. Actin/actin-like_CS.
IPR004001. Actin_CS.
[Graphical view]

KO

K05692.

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_BOVIN

Accession

Primary (citable) accession number: P60712
Secondary accession number(s): A5D961 , A5PKA1, P02570, P70514, P99021, Q11211, Q3SZD2, Q64316, Q8MIJ0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	April 1, 1988
Last modified:	November 16, 2011
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program