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P68135 (ACTS_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 71. 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
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, alpha skeletal muscle
Alternative name(s):
Alpha-actin-1
Gene names
Name:ACTA1
Synonyms:ACTA
OrganismOryctolagus cuniculus (Rabbit) [Complete proteome]
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

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. Interacts with TTID. Interacts (via its C-terminus) with USP25 By similarity.

Subcellular location

Cytoplasm › cytoskeleton.

Post-translational modification

Can be mono-ADP-ribosylated on Arg-179 by SpvB of Salmonella spp. This modification blocks subsequent polymerization and leads to cell death.

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_0000000850
Chain3 – 377375Actin, alpha skeletal muscle
PRO_0000000851

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 residue1791ADP-ribosylarginine; by SpvB Probable
Modified residue1931N6-acetyllysine By similarity
Modified residue2421Phosphotyrosine By similarity
Modified residue3281N6-acetyllysine By similarity
Modified residue3301N6-acetyllysine By similarity

Secondary structure

1 ...................................................................... 377
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P68135 [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 primary structure of actin from rabbit skeletal muscle. Completion and analysis of the amino acid sequence."
Collins J.H., Elzinga M.
J. Biol. Chem. 250:5915-5920(1975) [PubMed: 1150665] [Abstract]
Cited for: PROTEIN SEQUENCE OF 3-377.
Tissue: Skeletal muscle.
[2]"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: 213279] [Abstract]
Cited for: SEQUENCE REVISION TO 5; 7; 14 AND 75-81.
[3]"Partial amino acid sequence of brain actin and its homology with muscle actin."
Lu R.C., Elzinga M.
Biochemistry 16:5801-5806(1977) [PubMed: 588555] [Abstract]
Cited for: SEQUENCE REVISION.
[4]"A new troponin T and cDNA clones for 13 different muscle proteins, found by shotgun sequencing."
Putney S.D., Herlihy W.C., Schimmel P.R.
Nature 302:718-721(1983) [PubMed: 6687628] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 74-147; 194-283 AND 311-377.
[5]"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.
Tissue: Skeletal muscle.
[6]"Atomic structure of the actin:DNase I complex."
Kabsch W., Mannherz H.G., Suck D., Pai E.F., Holmes K.C.
Nature 347:37-44(1990) [PubMed: 2395459] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[7]"Crystal structure of monomeric actin in the ATP state. Structural basis of nucleotide-dependent actin dynamics."
Graceffa P., Dominguez R.
J. Biol. Chem. 278:34172-34180(2003) [PubMed: 12813032] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
[8]"Actin crystal dynamics: structural implications for F-actin nucleation, polymerization, and branching mediated by the anti-parallel dimer."
Reutzel R., Yoshioka C., Govindasamy L., Yarmola E.G., Agbandje-McKenna M., Bubb M.R., McKenna R.
J. Struct. Biol. 146:291-301(2004) [PubMed: 15099571] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 3-377 IN COMPLEX WITH ATP.
[9]"A steric antagonism of actin polymerization by a Salmonella virulence protein."
Margarit S.M., Davidson W., Frego L., Stebbins C.E.
Structure 14:1219-1229(2006) [PubMed: 16905096] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 7-377 ADP-RIBOSYLATED BY SPVB.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		V00872 mRNA. Translation: CAA24241.1.
V00873 mRNA. Translation: CAA24242.1.
V00874 mRNA. Translation: CAA24243.1.
PIRATRB. A92182.
I46471.
I46472.
I46473.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ALMmodel-V/W/X/Y/Z3-374[»]
1ATNX-ray2.80A3-374[»]
1EQYX-ray2.30A1-377[»]
1ESVX-ray2.00A1-377[»]
1H1VX-ray3.00A3-377[»]
1IJJX-ray2.85A/B1-377[»]
1J6ZX-ray1.54A4-377[»]
1KXPX-ray2.10A3-377[»]
1LCUX-ray3.50A/B7-377[»]
1LOTX-ray2.50B3-377[»]
1M8Qelectron microscopy70.000/1/2/3/4/5/7/8/9/V/W/X/Y/Z3-377[»]
1MA9X-ray2.40B8-372[»]
1MVWelectron microscopy70.001/2/3/4/5/6/7/8/9/V/W/X/Y/Z3-377[»]
1NWKX-ray1.85A3-377[»]
1O18electron microscopy70.001/2/3/4/5/6/7/8/9/V/W/X/Y/Z3-377[»]
1O19electron microscopy70.001/2/3/4/5/6/7/8/9/V/W/X/Y/Z3-377[»]
1O1Aelectron microscopy70.001/2/3/4/5/6/7/8/9/V/W/X/Y/Z3-377[»]
1O1Belectron microscopy70.000/1/2/3/4/5/7/8/9/V/W/X/Y/Z3-377[»]
1O1Celectron microscopy70.000/1/2/3/4/5/7/8/9/V/W/X/Y/Z3-377[»]
1O1Delectron microscopy70.000/1/2/3/4/5/7/8/9/V/W/X/Y/Z3-377[»]
1O1Eelectron microscopy70.001/2/3/4/5/6/7/8/9/V/W/X/Y/Z3-377[»]
1O1Felectron microscopy70.000/1/2/3/4/5/6/7/8/V/W/X/Y/Z3-377[»]
1O1Gelectron microscopy70.001/2/3/4/5/6/7/8/9/V/W/X/Y/Z3-377[»]
1P8ZX-ray2.60A1-377[»]
1QZ5X-ray1.45A3-377[»]
1QZ6X-ray1.60A3-377[»]
1RDWX-ray2.30X3-377[»]
1RFQX-ray3.00A/B3-377[»]
1RGIX-ray3.00A1-377[»]
1S22X-ray1.60A3-375[»]
1SQKX-ray2.50A1-377[»]
1T44X-ray2.00A8-377[»]
1UY5model-A3-374[»]
1WUAX-ray1.45A3-377[»]
1Y64X-ray3.05A3-377[»]
1YXQX-ray2.01A/B3-377[»]
2A3ZX-ray2.08A3-377[»]
2A40X-ray1.80A/D3-377[»]
2A41X-ray2.60A3-377[»]
2A42X-ray1.85A3-377[»]
2A5XX-ray2.49A3-377[»]
2ASMX-ray1.60A3-377[»]
2ASOX-ray1.70A3-377[»]
2ASPX-ray1.64A3-377[»]
2D1KX-ray2.50A3-377[»]
2FF3X-ray2.00B3-377[»]
2FF6X-ray2.05A3-377[»]
2FXUX-ray1.35A3-377[»]
2GWJX-ray1.90A7-377[»]
2GWKX-ray2.00A/B7-377[»]
2HMPX-ray1.90A/B3-377[»]
2PAVX-ray1.80A3-377[»]
2PBDX-ray1.50A1-377[»]
2Q0RX-ray1.70A3-377[»]
2Q0UX-ray1.45A3-377[»]
2Q1NX-ray2.70A/B3-377[»]
2Q31X-ray2.70A/B3-377[»]
2Q36X-ray2.50A3-377[»]
2Q97X-ray2.50A3-377[»]
2V51X-ray2.35B/D1-377[»]
2V52X-ray1.45B1-377[»]
2VCPX-ray3.20A/B3-377[»]
2VYPX-ray2.35A/B1-377[»]
2W49electron microscopy35.00D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S3-374[»]
2W4Uelectron microscopy35.00D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S3-374[»]
2Y83electron microscopy22.90O/P/Q/R/S/T3-377[»]
2YJEX-ray3.10A/B/C1-377[»]
2YJFX-ray3.50A/B/C/D/E1-377[»]
2ZWHfiber diffraction3.30A3-377[»]
3B5Uelectron microscopy-A/B/C/D/E/F/G/H/I/J/K/L/M/N1-377[»]
3BUZX-ray2.81B3-377[»]
3CJBX-ray3.21A1-377[»]
3CJCX-ray3.90A1-377[»]
3DAWX-ray2.55A1-377[»]
3FFKX-ray3.00B/E1-377[»]
3G37electron microscopy-O/P/Q/R/S/T/U/V/W/X/Y/Z3-377[»]
3HBTX-ray2.70A3-377[»]
3M1FX-ray2.89A3-377[»]
3M3NX-ray7.00A/B3-377[»]
3M6GX-ray2.00A/B3-373[»]
3MFPelectron microscopy-A3-377[»]
3MN5X-ray1.50A3-377[»]
3TPQX-ray3.45A/B/C/D/E3-377[»]
ProteinModelPortalP68135.
SMRP68135. Positions 6-377.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-29021N.
IntActP68135. 4 interactions.
MINTMINT-1489367.
STRINGP68135.

Proteomic databases

PRIDEP68135.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG003771.
OrthoDBEOG4W9J40.

Family and domain databases

InterProIPR004000. Actin-like.
IPR020902. Actin/actin-like_CS.
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_RABIT
AccessionPrimary (citable) accession number: P68135
Secondary accession number(s): P02568, P99020
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: December 14, 2011
This is version 71 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents