Actin, cytoplasmic 2 - Mus musculus (Mouse)

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P63260 (ACTG_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 88. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Actin, cytoplasmic 2

Alternative name(s):
Gamma-actin

Cleaved into the following chain:

Actin, cytoplasmic 2, N-terminally processed

Gene names

Name:	Actg1
Synonyms:	Actg

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

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.
Subcellular location	Cytoplasm › cytoskeleton.
Post-translational modification	Oxidation of Met-44 by MICALs (MICAL1, MICAL2 or MICAL3) to form methionine sulfoxide promotes actin filament depolymerization. Methionine sulfoxide is produced stereospecifically, but it is not known whether the (S)-S-oxide or the (R)-S-oxide is produced 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 Oxidation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	sarcomere organization Inferred from direct assay PubMed 15194427. Source: MGI
Cellular_component	costamere Traceable author statement PubMed 15194427. Source: MGI filamentous actin Inferred from direct assay PubMed 16510873 PubMed 18796539. Source: MGI
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW structural constituent of cytoskeleton Inferred from direct assay PubMed 15194427. Source: MGI
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Kcnma1	Q08460	4	EBI-351301,EBI-1633915

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 375

375

Actin, cytoplasmic 2

PRO_0000367101

Initiator methionine

Removed; alternate Ref.1

Chain

2 – 375

374

Actin, cytoplasmic 2, N-terminally processed

PRO_0000000833

Amino acid modifications

Modified residue

N-acetylmethionine; in Actin, cytoplasmic 2; alternate

Modified residue

N-acetylglutamate; in Actin, cytoplasmic 2, N-terminally processed

Modified residue

Methionine sulfoxide By similarity

Modified residue

Tele-methylhistidine Ref.1

Modified residue

169

Phosphotyrosine Ref.7

Sequences

Sequence

Length

Mass (Da)

Tools

P63260 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 54D08F986964EFD5
Show »

FASTA

375

41,793

        10         20         30         40         50         60 
MEEEIAALVI 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

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-375, METHYLATION AT HIS-73.
[2]	"Isolation of cDNA clones for mouse cytoskeletal gamma-actin and differential expression of cytoskeletal actin mRNAs in mouse cells." Tokunaga K., Takeda K., Kamiyama K., Kageyama H., Takenaga K., Sakiyama S. Mol. Cell. Biol. 8:3929-3933(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J and NOD. Tissue: Thymus.
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N and NMRI. Tissue: Colon and Mammary tumor.
[5]	"Mouse cytoskeletal gamma-actin: analysis and implications of the structure of cloned cDNA and processed pseudogenes." Peter B., Man Y.M., Begg C.E., Gall I., Leader D.P. J. Mol. Biol. 203:665-675(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 8-375.
[6]	Lubec G., Yang J.W., Zigmond M. Submitted (JUL-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 29-39. Tissue: Brain.
[7]	"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-169, MASS SPECTROMETRY. Tissue: Brain.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X13055 mRNA. Translation: CAA31455.1. AK076081 mRNA. Translation: BAC36167.1. AK087983 mRNA. Translation: BAC40075.1. BC003337 mRNA. Translation: AAH03337.1. BC021796 mRNA. Translation: AAH21796.1. BC023248 mRNA. Translation: AAH23248.1. M21495 mRNA. Translation: AAA37168.1.
IPI	IPI00874482.
PIR	ATMSG. A30243.
RefSeq	NP_033739.1. NM_009609.2.
UniGene	Mm.196173. Mm.426706.
3D structure databases
ProteinModelPortal	P63260.
ModBase	Search...
Protein-protein interaction databases
IntAct	P63260. 24 interactions.
PTM databases
PhosphoSite	P63260.
2D gel databases
COMPLUYEAST-2DPAGE	P63260.
REPRODUCTION-2DPAGE	P63260.
UCD-2DPAGE	P63260.
Proteomic databases
PRIDE	P63260.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000071555; ENSMUSP00000071486; ENSMUSG00000062825. ENSMUST00000106215; ENSMUSP00000101822; ENSMUSG00000062825.
GeneID	11465.
KEGG	mmu:11465.
Organism-specific databases
CTD	71.
MGI	MGI:87906. Actg1.
Phylogenomic databases
HOGENOM	HOG000233340.
HOVERGEN	HBG003771.
KO	K05692.
OMA	ADTEDIQ.
OrthoDB	EOG41JZC9.
Enzyme and pathway databases
Reactome	REACT_147847. Translocation of Glut4 to the Plasma Membrane. REACT_88307. Membrane Trafficking.
Gene expression databases
ArrayExpress	P63260.
Bgee	P63260.
CleanEx	MM_ACTG1.
Genevestigator	P63260.
GermOnline	ENSMUSG00000062825. Mus musculus.
Family and domain databases
InterPro	IPR004000. Actin-related. IPR020902. Actin/actin-like_CS. IPR004001. Actin_CS. [Graphical view]
PANTHER	PTHR11937. PTHR11937. 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...
Other
ChiTaRS	ACTG1. mouse.
NextBio	278792.
PMAP-CutDB	P63260.
SOURCE	Search...

Entry information

Entry name

ACTG_MOUSE

Accession

Primary (citable) accession number: P63260
Secondary accession number(s): P02571, P14104, P99022

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	May 1, 2013
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Cleaved into the following chain:

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents