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Reviewed, UniProtKB/Swiss-Prot P68138 (ACTS_BOVIN)

Last modified November 24, 2009. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Actin, alpha skeletal muscle
Alternative name(s):
    Alpha-actin-1
Gene names
Name: ACTA1
Synonyms: ACTA
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length377 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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. Interacts with TTID By similarity.

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_0000000842
Chain3 – 377375Actin, alpha skeletal muscle
PRO_0000000843

Amino acid modifications

Modified residue31N-acetylaspartate
Modified residue551Phosphotyrosine By similarity
Modified residue631N6-acetyllysine By similarity
Modified residue701N6-acetyllysine By similarity
Modified residue751Tele-methylhistidine
Modified residue931Phosphotyrosine By similarity
Modified residue1931N6-acetyllysine By similarity
Modified residue2421Phosphotyrosine By similarity
Modified residue3281N6-acetyllysine By similarity
Modified residue3301N6-acetyllysine By similarity

Experimental info

Sequence conflict3491A → R in AAA82873. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P68138-1 [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

« Hide 'large scale' references
[1]"The nucleotide sequence, structure, and preliminary studies on the transcriptional regulation of the bovine alpha skeletal actin gene."
Davey H.W., Kelly J.K., Wildeman A.G.
DNA Cell Biol. 14:609-618(1995) [PubMed: 7626220] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Liver.
[2]NIH - Mammalian Gene Collection (MGC) project
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Crossbred X Angus.
Tissue: Ileum.
[3]"The complete amino acid sequence of actins from bovine aorta, bovine heart, bovine fast skeletal muscle, and rabbit slow skeletal muscle. A protein-chemical analysis of muscle actin differentiation."
Vandekerckhove J., Weber K.
Differentiation 14:123-133(1979) [PubMed: 499690] [Abstract]
Cited for: PROTEIN SEQUENCE OF 3-377.
+Additional computationally mapped references.

Cross-references

Sequence databases

U02285 Genomic DNA. Translation: AAA82873.1.
BC102376 mRNA. Translation: AAI02377.1.
IPIIPI00697648.
RefSeqNP_776650.1.
UniGeneBt.88733

3D structure databases

SMRP68138. Positions 6-373.
ModBaseSearch...

Protein-protein interaction databases

STRINGP68138.

Genome annotation databases

EnsemblENSBTAT00000006534; ENSBTAP00000006534; ENSBTAG00000004965; Bos taurus. [Genome view]
GeneID281592.
KEGGbta:281592.

Organism-specific databases

CTD281592.

Phylogenomic databases

HOVERGENP68138.
OMAFVGMESA

Family and domain databases

InterProIPR004000. Actin-like.
IPR004001. Actin_CS.
[Graphical view]
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_BOVIN
AccessionPrimary (citable) accession number: P68138
Secondary accession number(s): P02568, P99020, Q3ZCG3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 24, 2009
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents