Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - P68135 (ACTS_RABIT)

Entry version 131 (17 Jun 2020)
Sequence version 1 (21 Jul 1986)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Actin, alpha skeletal muscle

Gene

ACTA1

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.

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.

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionMuscle protein
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P68135

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Actin, alpha skeletal muscle
Alternative name(s):
Alpha-actin-1
Cleaved into the following chain:
Actin, alpha skeletal muscle, intermediate form
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:ACTA1
Synonyms:ACTA
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiOryctolagus cuniculus (Rabbit)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9986 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000001811 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004428112 – 377Actin, alpha skeletal muscle, intermediate formBy similarityAdd BLAST376
ChainiPRO_00004428123 – 377Actin, alpha skeletal muscle2 PublicationsAdd BLAST375

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylcysteine; in intermediate formBy similarity1
Modified residuei3N-acetylaspartate; in Actin, alpha skeletal muscle1 Publication1
Modified residuei46Methionine (R)-sulfoxideBy similarity1
Modified residuei49Methionine (R)-sulfoxideBy similarity1
Modified residuei63N6-malonyllysineBy similarity1
Modified residuei75Tele-methylhistidineCombined sources5 Publications1
Modified residuei86N6-methyllysineBy similarity1
Modified residuei179ADP-ribosylarginine; by SpvB1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Oxidation of Met-46 and Met-49 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 promotes actin repolymerization.By similarity
Can be mono-ADP-ribosylated on Arg-179 by SpvB of Salmonella spp. This modification blocks subsequent polymerization and leads to cell death.1 Publication
Monomethylation at Lys-86 (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
Methylated at His-75 by SETD3.By similarity

Keywords - PTMi

Acetylation, ADP-ribosylation, Methylation, Oxidation

Proteomic databases

PRoteomics IDEntifications database

More...PRIDEi		P68135

PTM databases

CarbonylDB database of protein carbonylation sites

More...CarbonylDBi		P68135

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P68135

MetOSite database of methionine sulfoxide sites

More...MetOSitei		P68135

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

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).

Identified in a complex composed of ACTA1, COBL, GSN AND TMSB4X.

By similarity2 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details
P68135
With#Exp.IntAct
itself30EBI-367540,EBI-367540
ARP8 [Q12386] from Saccharomyces cerevisiae (strain ATCC 204508 / S288c).2EBI-367540,EBI-2967
cib [Q8IRS7] from Drosophila melanogaster.2EBI-367540,EBI-15573246
CNN1 [P26932] from Gallus gallus.5EBI-367540,EBI-8602797
COF1 [Q03048] from Saccharomyces cerevisiae (strain ATCC 204508 / S288c).3EBI-367540,EBI-4853
CRN1 [Q06440] from Saccharomyces cerevisiae (strain ATCC 204508 / S288c).3EBI-367540,EBI-4950
DNASE1 [P00639] from Bos taurus.3EBI-367540,EBI-8545986
EMD [P50402] from Homo sapiens.3EBI-367540,EBI-489887
Fmnl3 - isoform 1 [Q6ZPF4-1] from Mus musculus.3EBI-367540,EBI-16027300
Fscn1 [Q61553] from Mus musculus.2EBI-367540,EBI-2308857
GSN [P06396] from Homo sapiens.10EBI-367540,EBI-351506
mhcA [P08799] from Dictyostelium discoideum.8EBI-367540,EBI-2928504
Mrtfa [Q8K4J6] from Mus musculus.15EBI-367540,EBI-8291665
Mybpc3 [O70468] from Mus musculus.2EBI-367540,EBI-8347074
PFN1 [P07737] from Homo sapiens.2EBI-367540,EBI-713780
rtxA [Q9KS12] from Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).4EBI-367540,EBI-15741102
spir - isoform A [Q9U1K1-1] from Drosophila melanogaster.6EBI-367540,EBI-3431623
spvB [P21454] from Salmonella typhimurium.2EBI-367540,EBI-15595598
tarP [Q6GX35] from Chlamydia trachomatis serovar L2 (strain 434/Bu / ATCC VR-902B).4EBI-367540,EBI-15605056
toxofilin [Q9NG25] from Toxoplasma gondii.2EBI-367540,EBI-15662915
Tpm1 [P58771] from Mus musculus.2EBI-367540,EBI-298478
TWF1 [P53250] from Saccharomyces cerevisiae (strain ATCC 204508 / S288c).5EBI-367540,EBI-19663
Twf1 [Q91YR1] from Mus musculus.2EBI-367540,EBI-527441
VCL - isoform 1 [P12003-1] from Gallus gallus.2EBI-367540,EBI-6138078
VCL - isoform 1 [P18206-2] from Homo sapiens.2EBI-367540,EBI-11027067
VPA1370 [Q87GE5] from Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).10EBI-367540,EBI-15666619
WASL [O00401] from Homo sapiens.2EBI-367540,EBI-957615
Wasl [Q91YD9] from Mus musculus.5EBI-367540,EBI-642417
C5IZN1 from Vibrio cholerae.3EBI-367540,EBI-16066991
Isoform 4 [Q05193-5] from Homo sapiens.5EBI-367540,EBI-8446026

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

Database of interacting proteins

More...DIPi		DIP-29021N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...ELMi		P68135

Protein interaction database and analysis system

More...IntActi		P68135, 88 interactors

Molecular INTeraction database

More...MINTi		P68135

STRING: functional protein association networks

More...STRINGi		9986.ENSOCUP00000006542

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1377
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P68135

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P68135

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the actin family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0676 Eukaryota
COG5277 LUCA

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P68135

Family and domain databases

Intrinsically Disordered proteins with Extensive Annotations and Literature

More...IDEALi		IID50082

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR004000 Actin
IPR020902 Actin/actin-like_CS
IPR004001 Actin_CS
IPR043129 ATPase_NBD

The PANTHER Classification System

More...PANTHERi		PTHR11937 PTHR11937, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00022 Actin, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00190 ACTIN

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00268 ACTIN, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF53067 SSF53067, 2 hits

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00406 ACTINS_1, 1 hit
PS00432 ACTINS_2, 1 hit
PS01132 ACTINS_ACT_LIKE, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P68135-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MCDEDETTAL VCDNGSGLVK AGFAGDDAPR AVFPSIVGRP RHQGVMVGMG 
        60         70         80         90        100
QKDSYVGDEA QSKRGILTLK YPIEHGIITN WDDMEKIWHH TFYNELRVAP 
       110        120        130        140        150
EEHPTLLTEA PLNPKANREK MTQIMFETFN VPAMYVAIQA VLSLYASGRT 
       160        170        180        190        200
TGIVLDSGDG VTHNVPIYEG YALPHAIMRL DLAGRDLTDY LMKILTERGY 
       210        220        230        240        250
SFVTTAEREI VRDIKEKLCY VALDFENEMA TAASSSSLEK SYELPDGQVI 
       260        270        280        290        300
TIGNERFRCP ETLFQPSFIG MESAGIHETT YNSIMKCDID IRKDLYANNV 
       310        320        330        340        350
MSGGTTMYPG IADRMQKEIT ALAPSTMKIK IIAPPERKYS VWIGGSILAS 
       360        370 
LSTFQQMWIT KQEYDEAGPS IVHRKCF
Length:377
Mass (Da):42,051
Last modified:July 21, 1986 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iDF2A3A046346A179
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
V00872 mRNA Translation: CAA24241.1
V00873 mRNA Translation: CAA24242.1
V00874 mRNA Translation: CAA24243.1

Protein sequence database of the Protein Information Resource

More...PIRi		A92182 ATRB
I46471
I46472
I46473

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00872 mRNA Translation: CAA24241.1
V00873 mRNA Translation: CAA24242.1
V00874 mRNA Translation: CAA24243.1
PIRiA92182 ATRB
I46471
I46472
I46473

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB 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-ray1.54A3-377[»]
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-ray2.40B3-377[»]
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-ray1.60A3-377[»]
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[»]
3J4Kelectron microscopy8.00A/B/C/D/E3-377[»]
3J8Aelectron microscopy3.70A/B/C/D/E3-377[»]
3J8Ielectron microscopy4.70D/E/F/G/H1-377[»]
3J8Jelectron microscopy12.00A/B/C/D/E/F/G/H/I/J/K1-377[»]
3J8Kelectron microscopy12.00A/B/C/D/E/F/G/H/I/J1-377[»]
3JBIelectron microscopy8.50A/B3-377[»]
3JBJelectron microscopy7.60A/B3-377[»]
3JBKelectron microscopy8.20A/B3-377[»]
3M1FX-ray2.89A3-377[»]
3M3NX-ray7.00A/B3-377[»]
3M6GX-ray2.00A/B3-373[»]
3MFPelectron microscopy-A3-377[»]
3MN5X-ray1.50A3-377[»]
3SJHX-ray1.75A3-377[»]
3TPQX-ray3.45A/B/C/D/E3-377[»]
3TU5X-ray3.00A1-377[»]
3U8XX-ray2.00A/C3-377[»]
3U9ZX-ray2.09A3-377[»]
3UE5X-ray2.76A3-377[»]
4A7Felectron microscopy7.70A/D/E/F/I3-377[»]
4A7Helectron microscopy7.80A/D/E/F/G3-377[»]
4A7Lelectron microscopy8.10A/D/E/F/I3-377[»]
4A7Nelectron microscopy8.90A/B/C/D/E3-377[»]
4B1VX-ray1.75A/B2-377[»]
4B1WX-ray1.95B2-377[»]
4B1XX-ray1.80B2-377[»]
4B1YX-ray1.29B2-377[»]
4B1ZX-ray3.30A/B/C/D/E/F2-377[»]
4EAHX-ray3.40D/F/G/H1-377[»]
4GY2X-ray2.71B3-377[»]
4H03X-ray1.75B3-377[»]
4H0TX-ray2.20B3-377[»]
4H0VX-ray2.03B3-377[»]
4H0XX-ray2.33B3-377[»]
4H0YX-ray1.94B3-377[»]
4K41X-ray1.40A3-377[»]
4K42X-ray2.90A/B/C/D3-377[»]
4K43X-ray2.90A/B3-377[»]
4PKGX-ray1.80A1-377[»]
4PKHX-ray2.15A/D/F/I1-377[»]
4PKIX-ray2.30A1-377[»]
4PL8X-ray2.00A/B3-377[»]
4V0UX-ray7.88A/B/C/L/M3-377[»]
4WYBX-ray3.49A/C/E/G/I/K/M/O/Q/S/U/X1-377[»]
4Z94X-ray2.40A1-377[»]
5H53electron microscopy5.20D/E3-377[»]
5JLFelectron microscopy3.60A/B/C/D/E3-377[»]
5KG8electron microscopy9.10B/C/D3-377[»]
5MVAelectron microscopy27.70A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W3-377[»]
5MVYelectron microscopy28.40A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W3-377[»]
5ONVelectron microscopy4.10A/B/C/D/E3-377[»]
5OOCelectron microscopy3.60A/B/C/D/E3-377[»]
5OODelectron microscopy3.70A/B/C/D/E3-377[»]
5OOEelectron microscopy3.60A/B/C/D/E3-377[»]
5OOFelectron microscopy3.40A/B/C/D/E3-377[»]
5UBOX-ray2.39A1-377[»]
5YEEX-ray1.81B1-377[»]
5YPUX-ray2.00A/C7-374[»]
5ZZAX-ray1.53A5-377[»]
5ZZBX-ray2.30B/D7-377[»]
6AV9electron microscopy3.90A/B/C1-377[»]
6AVBelectron microscopy3.90A/B/C1-377[»]
6BIHelectron microscopy6.00C1-377[»]
6BNOelectron microscopy5.50A/B/C/D/E/F/G/H1-373[»]
6BNPelectron microscopy4.60A/B/C/D/E/F/G/H1-373[»]
6BNQelectron microscopy5.50A/B/C/D/E/F/G/H1-373[»]
6BNUelectron microscopy7.50A/B/C/D/E/F/G/H1-373[»]
6BNVelectron microscopy4.60A/B/C/D/E/F/G/H1-373[»]
6BNWelectron microscopy5.50A/B/C/D/E/F/G/H1-373[»]
6C1Delectron microscopy3.20A/B/C/D/E3-377[»]
6C1Gelectron microscopy3.80A/B/C/D/E3-377[»]
6C1Helectron microscopy3.90A/B/C/D/E3-377[»]
6FHLelectron microscopy3.30A/B/C/D/E3-377[»]
6FM2X-ray2.80A3-377[»]
6GVCX-ray2.60A/B/C/D1-377[»]
6JBKX-ray2.45A/C/E/G1-377[»]
6JCUX-ray2.30A/C1-377[»]
6JH8X-ray2.15A1-377[»]
6JH9X-ray1.74A1-377[»]
6KN7electron microscopy6.60A/B/C/D/E/F/G/H/I/J/K/L/M/N/O3-377[»]
6KN8electron microscopy4.80A/B/C/D/E/F/G/H/I/J/K/L/M/N/O3-377[»]
6MGOX-ray2.20A1-377[»]
6NASX-ray2.90A3-377[»]
6QRIX-ray2.40A/B1-377[»]
6RSWX-ray1.95A3-377[»]
6T1Yelectron microscopy3.30A/B/C/D/E3-377[»]
6T20electron microscopy3.70A/B/C/D/E3-377[»]
6T23electron microscopy3.10A/B/C/D/E3-377[»]
6T24electron microscopy3.70A/B/C/D/E3-377[»]
6T25electron microscopy3.60A/B/C/D/E3-377[»]
6UBYelectron microscopy7.50A/B/C/D/E/F/G/H1-377[»]
6UC0electron microscopy7.50A/B/C/D/E/F/G1-377[»]
6UC4electron microscopy9.20A/B/C/D/E/F/G/H/J/K/L1-377[»]
6VAOelectron microscopy3.40A/B/C/D/E1-377[»]
6VAUelectron microscopy3.50A/B/C/D/E1-377[»]
SMRiP68135
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

DIPiDIP-29021N
ELMiP68135
IntActiP68135, 88 interactors
MINTiP68135
STRINGi9986.ENSOCUP00000006542

PTM databases

CarbonylDBiP68135
iPTMnetiP68135
MetOSiteiP68135

Proteomic databases

PRIDEiP68135

Phylogenomic databases

eggNOGiKOG0676 Eukaryota
COG5277 LUCA
InParanoidiP68135

Enzyme and pathway databases

SABIO-RKiP68135

Miscellaneous databases

EvolutionaryTraceiP68135

Family and domain databases

IDEALiIID50082
InterProiView protein in InterPro
IPR004000 Actin
IPR020902 Actin/actin-like_CS
IPR004001 Actin_CS
IPR043129 ATPase_NBD
PANTHERiPTHR11937 PTHR11937, 1 hit
PfamiView protein in Pfam
PF00022 Actin, 1 hit
PRINTSiPR00190 ACTIN
SMARTiView protein in SMART
SM00268 ACTIN, 1 hit
SUPFAMiSSF53067 SSF53067, 2 hits
PROSITEiView protein in PROSITE
PS00406 ACTINS_1, 1 hit
PS00432 ACTINS_2, 1 hit
PS01132 ACTINS_ACT_LIKE, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiACTS_RABIT
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P68135
Secondary accession number(s): P02568, P99020
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: June 17, 2020
This is version 131 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again