Actin, alpha skeletal muscle - Gallus gallus (Chicken)

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Reviewed, UniProtKB/Swiss-Prot P68139 (ACTS_CHICK)

Last modified November 24, 2009. Version 47. History...

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

Names and origin

Protein names

Recommended name:
Actin, alpha skeletal muscle
Alternative name(s):
Alpha-actin-1

Gene names

Name:	ACTA1
Synonyms:	ACTA

Organism

Gallus gallus (Chicken)

Taxonomic identifier

Taxonomic lineage

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

Protein attributes

Sequence length	377 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
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
Molecular function	Muscle protein
PTM	Acetylation Methylation
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	muscle thin filament assembly Inferred from sequence or structural similarity. Source: UniProtKB skeletal muscle fiber development Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	stress fiber Inferred from sequence or structural similarity. Source: UniProtKB striated muscle thin filament Inferred from sequence or structural similarity. Source: UniProtKB
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

Propeptide

2

Removed in mature form

PRO_0000000854

Chain

375

Actin, alpha skeletal muscle

PRO_0000000855

Amino acid modifications

Modified residue

1

N-acetylaspartate

Modified residue

1

Tele-methylhistidine

Secondary structure

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377

Helix Strand Turn

Sequences

Sequence

Length

Mass (Da)

Tools

P68139-1 [UniParc].

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

377

42,051

        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

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

V01507 Genomic DNA. Translation: CAA24753.1.

IPI

PIR

ATCH. A93432.

RefSeq

NP_001026234.1.

UniGene

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1MDU	X-ray	2.20	B/E	1-377	[»]

ModBase

Protein-protein interaction databases

STRING

Genome annotation databases

Ensembl

ENSGALT00000016005; ENSGALP00000015988; ENSGALG00000009844; Gallus gallus. [Genome view]

GeneID

KEGG

Organism-specific databases

CTD

Phylogenomic databases

HOVERGEN

Family and domain databases

InterPro

IPR004000. Actin-like.
IPR004001. Actin_CS.
[Graphical view]

PANTHER

PTHR11937. Actin_like. 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

Entry information

Entry name

ACTS_CHICK

Accession

Primary (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:	November 24, 2009
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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