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P63260 (ACTG_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Actin, cytoplasmic 2
Alternative name(s):
Gamma-actin

Cleaved into the following chain:

  1. Actin, cytoplasmic 2, N-terminally processed
Gene names
Name:Actg1
Synonyms:Actg
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length375 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

Cytoplasmcytoskeleton.

Post-translational modification

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.

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.

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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Kcnma1Q084604EBI-351301,EBI-1633915

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 375375Actin, cytoplasmic 2
PRO_0000367101
Initiator methionine11Removed; alternate Ref.1
Chain2 – 375374Actin, cytoplasmic 2, N-terminally processed
PRO_0000000833

Amino acid modifications

Modified residue11N-acetylmethionine; in Actin, cytoplasmic 2; alternate
Modified residue21N-acetylglutamate; in Actin, cytoplasmic 2, N-terminally processed
Modified residue441Methionine (R)-sulfoxide
Modified residue471Methionine (R)-sulfoxide
Modified residue731Tele-methylhistidine Ref.1
Modified residue841N6-methyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P63260 [UniParc].

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

FASTA37541,793
        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' 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. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai 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]"MsrB1 and MICALs regulate actin assembly and macrophage function via reversible stereoselective methionine oxidation."
Lee B.C., Peterfi Z., Hoffmann F.W., Moore R.E., Kaya A., Avanesov A., Tarrago L., Zhou Y., Weerapana E., Fomenko D.E., Hoffmann P.R., Gladyshev V.N.
Mol. Cell 51:397-404(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: OXIDATION AT MET-44 AND MET-47, DEOXIDATION AT MET-44 AND MET-47.
+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.
PIRATMSG. A30243.
RefSeqNP_033739.1. NM_009609.2.
UniGeneMm.196173.
Mm.426706.
Mm.470166.

3D structure databases

ProteinModelPortalP63260.
SMRP63260. Positions 6-375.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid197946. 17 interactions.
IntActP63260. 25 interactions.

PTM databases

PhosphoSiteP63260.

2D gel databases

COMPLUYEAST-2DPAGEP63260.
REPRODUCTION-2DPAGEP63260.
UCD-2DPAGEP63260.

Proteomic databases

PRIDEP63260.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000071555; ENSMUSP00000071486; ENSMUSG00000062825.
ENSMUST00000106215; ENSMUSP00000101822; ENSMUSG00000062825.
GeneID11465.
KEGGmmu:11465.
UCSCuc007msi.1. mouse.

Organism-specific databases

CTD71.
MGIMGI:87906. Actg1.

Phylogenomic databases

HOGENOMHOG000233340.
HOVERGENHBG003771.
KOK05692.
OMATANASRW.
OrthoDBEOG72RMZ1.
PhylomeDBP63260.
TreeFamTF354237.

Enzyme and pathway databases

ReactomeREACT_147847. Translocation of Glut4 to the Plasma Membrane.

Gene expression databases

BgeeP63260.
CleanExMM_ACTG1.
GenevestigatorP63260.

Family and domain databases

InterProIPR004000. Actin-related.
IPR020902. Actin/actin-like_CS.
IPR004001. Actin_CS.
[Graphical view]
PANTHERPTHR11937. PTHR11937. 1 hit.
PfamPF00022. Actin. 1 hit.
[Graphical view]
PRINTSPR00190. ACTIN.
SMARTSM00268. ACTIN. 1 hit.
[Graphical view]
PROSITEPS00406. ACTINS_1. 1 hit.
PS00432. ACTINS_2. 1 hit.
PS01132. ACTINS_ACT_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSACTG1. mouse.
NextBio278792.
PMAP-CutDBP63260.
PROP63260.
SOURCESearch...

Entry information

Entry nameACTG_MOUSE
AccessionPrimary (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: April 16, 2014
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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