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P63268 (ACTH_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 84. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Actin, gamma-enteric smooth muscle
Alternative name(s):
Alpha-actin-3
Gamma-2-actin
Smooth muscle gamma-actin
Gene names
Name:Actg2
Synonyms:Acta3, Actsg
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length376 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-45 and Met-48 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-85 (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.

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
   LigandATP-binding
Nucleotide-binding
   Molecular functionMuscle protein
   PTMOxidation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentcell periphery

Inferred from direct assay PubMed 12040017. Source: MGI

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 22Removed in mature form By similarity
PRO_0000000750
Chain3 – 376374Actin, gamma-enteric smooth muscle
PRO_0000000751

Amino acid modifications

Modified residue451Methionine (R)-sulfoxide
Modified residue481Methionine (R)-sulfoxide

Sequences

Sequence LengthMass (Da)Tools
P63268 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: 6EC08CD5EEAD445E

FASTA37641,877
        10         20         30         40         50         60 
MCEEETTALV CDNGSGLCKA GFAGDDAPRA VFPSIVGRPR HQGVMVGMGQ KDSYVGDEAQ 

        70         80         90        100        110        120 
SKRGILTLKY PIEHGIITNW DDMEKIWHHS FYNELRVAPE EHPTLLTEAP LNPKANREKM 

       130        140        150        160        170        180 
TQIMFETFNV PAMYVAIQAV LSLYASGRTT GIVLDSGDGV THNVPIYEGY ALPHAIMRLD 

       190        200        210        220        230        240 
LAGRDLTDYL MKILTERGYS FVTTAEREIV RDIKEKLCYV ALDFENEMAT AASSSSLEKS 

       250        260        270        280        290        300 
YELPDGQVIT IGNERFRCPE TLFQPSFIGM ESAGIHETTY NSIMKCDIDI RKDLYANNVL 

       310        320        330        340        350        360 
SGGTTMYPGI ADRMQKEITA LAPSTMKIKI IAPPERKYSV WIGGSILASL STFQQMWISK 

       370 
PEYDEAGPSI VHRKCF 

« Hide

References

« Hide 'large scale' references
[1]"Identification and developmental expression of a smooth-muscle gamma-actin in postmeiotic male germ cells of mice."
Kim E., Waters S.H., Hake L.E., Hecht N.B.
Mol. Cell. Biol. 9:1875-1881(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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: Czech II.
Tissue: Mammary tumor.
[3]"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-45 AND MET-48, DEOXIDATION AT MET-45 AND MET-48.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M26689 mRNA. Translation: AAA56841.1.
BC002042 mRNA. Translation: AAH02042.1.
CCDSCCDS51822.1.
PIRA32788.
RefSeqNP_033740.2. NM_009610.2.
UniGeneMm.292865.

3D structure databases

ProteinModelPortalP63268.
SMRP63268. Positions 3-376.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid197947. 1 interaction.
IntActP63268. 2 interactions.
MINTMINT-4086768.
STRING10090.ENSMUSP00000113552.

PTM databases

PhosphoSiteP63268.

Proteomic databases

MaxQBP63268.
PaxDbP63268.
PRIDEP63268.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000075161; ENSMUSP00000074658; ENSMUSG00000059430.
ENSMUST00000121731; ENSMUSP00000113552; ENSMUSG00000059430.
GeneID11468.
KEGGmmu:11468.
UCSCuc009cnr.1. mouse.

Organism-specific databases

CTD72.
MGIMGI:104589. Actg2.

Phylogenomic databases

eggNOGCOG5277.
HOGENOMHOG000233340.
HOVERGENHBG003771.
InParanoidP63268.
KOK12315.
OMAASMESAN.
OrthoDBEOG72RMZ1.
PhylomeDBP63268.
TreeFamTF354237.

Gene expression databases

ArrayExpressP63268.
BgeeP63268.
CleanExMM_ACTG2.
GenevestigatorP63268.

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

ChiTaRSACTG2. mouse.
NextBio278796.
PROP63268.
SOURCESearch...

Entry information

Entry nameACTH_MOUSE
AccessionPrimary (citable) accession number: P63268
Secondary accession number(s): P12718
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: July 9, 2014
This is version 84 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