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P68139 (ACTS_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Actin, alpha skeletal muscle
Alternative name(s):
Alpha-actin-1
Gene names
Name:ACTA1
Synonyms:ACTA
OrganismGallus gallus (Chicken)
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length377 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.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 22Removed in mature form
PRO_0000000854
Chain3 – 377375Actin, alpha skeletal muscle
PRO_0000000855

Amino acid modifications

Modified residue31N-acetylaspartate
Modified residue751Tele-methylhistidine

Secondary structure

......................................................................... 377
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P68139 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: DF2A3A046346A179

FASTA37742,051
        10         20         30         40         50         60 
MCDEDETTAL VCDNGSGLVK AGFAGDDAPR AVFPSIVGRP RHQGVMVGMG QKDSYVGDEA 

        70         80         90        100        110        120 
QSKRGILTLK YPIEHGIITN WDDMEKIWHH TFYNELRVAP EEHPTLLTEA PLNPKANREK 

       130        140        150        160        170        180 
MTQIMFETFN VPAMYVAIQA VLSLYASGRT TGIVLDSGDG VTHNVPIYEG YALPHAIMRL 

       190        200        210        220        230        240 
DLAGRDLTDY LMKILTERGY SFVTTAEREI VRDIKEKLCY VALDFENEMA TAASSSSLEK 

       250        260        270        280        290        300 
SYELPDGQVI TIGNERFRCP ETLFQPSFIG MESAGIHETT YNSIMKCDID IRKDLYANNV 

       310        320        330        340        350        360 
MSGGTTMYPG IADRMQKEIT ALAPSTMKIK IIAPPERKYS VWIGGSILAS LSTFQQMWIT 

       370 
KQEYDEAGPS IVHRKCF 

« Hide

References

[1]"The amino acid sequence of actin from chicken skeletal muscle actin and chicken gizzard smooth muscle actin."
Vandekerckhove J., Weber K.
FEBS Lett. 102:219-222(1979) [PubMed: 456601] [Abstract]
Cited for: PROTEIN SEQUENCE OF 3-377.
Tissue: Skeletal muscle.
[2]"The complete nucleotide sequence of the chick a-actin gene and its evolutionary relationship to the actin gene family."
Fornwald J.A., Kuncio G., Peng I., Ordahl C.P.
Nucleic Acids Res. 10:3861-3876(1982) [PubMed: 6287424] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Analysis of a CR1 (chicken repeat) sequence flanking the 5' end of the gene encoding alpha-skeletal actin."
French B.A., Bergsma D.J., Schwartz R.J.
Gene 88:173-180(1990) [PubMed: 2347492] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]Ordahl C.P.
Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Mammary gland.
[5]"Alpha-cardiac actin is the major sarcomeric isoform expressed in embryonic avian skeletal muscle."
Paterson B.M., Eldridge J.D.
Science 224:1436-1438(1984) [PubMed: 6729461] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-43.
Tissue: Mammary gland.
[6]"Isolation and characterization of six different chicken actin genes."
Chang K.S., Zimmer W.E. Jr., Bergsma D.J., Dodgson J.B., Schwartz R.J.
Mol. Cell. Biol. 4:2498-2508(1984) [PubMed: 6513927] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-19.
[7]"Structure of an F-actin trimer disrupted by gelsolin and implications for the mechanism of severing."
Dawson J.F., Sablin E.P., Spudich J.A., Fletterick R.J.
J. Biol. Chem. 278:1229-1238(2003) [PubMed: 12356759] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH ATP.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
V01507 Genomic DNA. Translation: CAA24753.1.
IPIIPI00582169.
PIRATCH. A93432.
RefSeqNP_001026234.1. NM_001031063.1.
UniGeneGga.45736.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MDUX-ray2.20B/E1-377[»]
ProteinModelPortalP68139.
SMRP68139. Positions 6-377.
ModBaseSearch...

Protein-protein interaction databases

IntActP68139. 1 interaction.
STRINGP68139.

Proteomic databases

PRIDEP68139.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID421534.
KEGGgga:421534.

Organism-specific databases

CTD58.

Phylogenomic databases

GeneTreeENSGT00590000082732.
HOVERGENHBG003771.
InParanoidP68139.
PhylomeDBP68139.

Family and domain databases

InterProIPR004000. Actin-like.
IPR020902. Actin/actin-like_CS.
IPR004001. Actin_CS.
[Graphical view]
KOK10354.
PANTHERPTHR11937. Actin_like. 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...

Entry information

Entry nameACTS_CHICK
AccessionPrimary (citable) accession number: P68139
Secondary accession number(s): P02568, P99020
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: January 25, 2012
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families