Actin, cytoplasmic 1 - Gallus gallus (Chicken)

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P60706 (ACTB_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 70. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Actin, cytoplasmic 1

Alternative name(s):
Beta-actin

Cleaved into the following chain:

Actin, cytoplasmic 1, N-terminally processed

Gene names

Name:

ACTB

Organism

Gallus gallus (Chicken) [Reference proteome]

Taxonomic identifier

9031 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Protein attributes

Sequence length	375 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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	Cytoplasm › cytoskeleton.
Post-translational modification	Oxidation of Met-44 by MICALs (MICAL1, MICAL2 or MICAL3) to form methionine sulfoxide promotes actin filament depolymerization. Methionine sulfoxide is produced stereospecifically, but it is not known whether the (S)-S-oxide or the (R)-S-oxide is produced 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 component	Cytoplasm Cytoskeleton
Ligand	ATP-binding Nucleotide-binding
PTM	Acetylation Methylation Oxidation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 375

375

Actin, cytoplasmic 1

PRO_0000367086

Initiator methionine

Removed; alternate Ref.3

Chain

2 – 375

374

Actin, cytoplasmic 1, N-terminally processed

PRO_0000000789

Amino acid modifications

Modified residue

N-acetylmethionine; in Actin, cytoplasmic 1; alternate By similarity

Modified residue

N-acetylaspartate; in Actin, cytoplasmic 1, N-terminally processed Ref.3

Modified residue

Methionine sulfoxide By similarity

Modified residue

Tele-methylhistidine By similarity

Experimental info

Sequence conflict

336

K → R in CAA25004. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P60706 [UniParc].

Last modified April 1, 1988. Version 1.
Checksum: 6AFD05CA94E360E2
Show »

FASTA

375

41,737

        10         20         30         40         50         60 
MDDDIAALVV DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS 

        70         80         90        100        110        120 
KRGILTLKYP IEHGIVTNWD DMEKIWHHTF YNELRVAPEE HPVLLTEAPL NPKANREKMT 

       130        140        150        160        170        180 
QIMFETFNTP AMYVAIQAVL SLYASGRTTG IVMDSGDGVT HTVPIYEGYA LPHAILRLDL 

       190        200        210        220        230        240 
AGRDLTDYLM KILTERGYSF TTTAEREIVR DIKEKLCYVA LDFEQEMATA ASSSSLEKSY 

       250        260        270        280        290        300 
ELPDGQVITI GNERFRCPEA LFQPSFLGME SCGIHETTFN SIMKCDVDIR KDLYANTVLS 

       310        320        330        340        350        360 
GGTTMYPGIA DRMQKEITAL APSTMKIKII APPERKYSVW IGGSILASLS TFQQMWISKQ 

       370 
EYDESGPSIV HRKCF

« Hide

References

[1]	"The nucleotide sequence of the chick cytoplasmic beta-actin gene." Kost T.A., Theodorakis N., Hughes S.H. Nucleic Acids Res. 11:8287-8301(1983) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Nucleotide sequence of a beta-actin cDNA from mitochondrial DNA-depleted chicken cells." Wang H., Morais R. Submitted (JAN-1993) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	Bienvenut W.V., Black E.J., Gillespie D.A. Submitted (JAN-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-37; 85-113; 178-191; 197-206; 239-254; 291-326 AND 360-372, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ASP-2, MASS SPECTROMETRY. Tissue: B-cell lymphoma.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X00182 Genomic DNA. Translation: CAA25004.1.
L08165 mRNA. Translation: AAA48615.1.

IPI

IPI00655503.

PIR

ATCHB. A20888.

RefSeq

NP_990849.1. NM_205518.1.

UniGene

Gga.43416.
Gga.48207.
Gga.6076.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3J0S	electron microscopy	9.00	A/B/C/D/E/F/G/H/I/J/K/L	2-375	[»]

ProteinModelPortal

P60706.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-41284N.

MINT

MINT-199239.

Proteomic databases

PRIDE

P60706.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

396526.

KEGG

gga:396526.

Organism-specific databases

CTD

60.

Phylogenomic databases

HOGENOM

HOG000233340.

HOVERGEN

HBG003771.

InParanoid

P60706.

K05692.

Family and domain databases

InterPro

IPR004000. Actin-related.
IPR020902. Actin/actin-like_CS.
IPR004001. Actin_CS.
[Graphical view]

PANTHER

PTHR11937. PTHR11937. 1 hit.

Pfam

PF00022. Actin. 1 hit.
[Graphical view]

PRINTS

PR00190. ACTIN.

SMART

SM00268. ACTIN. 1 hit.
[Graphical view]

PROSITE

PS00406. ACTINS_1. 1 hit.
PS00432. ACTINS_2. 1 hit.
PS01132. ACTINS_ACT_LIKE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

20816563.

Entry information

Entry name

ACTB_CHICK

Accession

Primary (citable) accession number: P60706
Secondary accession number(s): P02570

Q64316

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	April 1, 1988
Last modified:	May 1, 2013
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Cleaved into the following chain:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Other

Entry information

Relevant documents