Reviewed, UniProtKB/Swiss-Prot P68135 (ACTS_RABIT)

Names and origin

Protein names

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

Gene names

Name:	ACTA1
Synonyms:	ACTA

Organism

Oryctolagus cuniculus (Rabbit)

Taxonomic identifier

9986 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

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. Interacts with TTID By similarity.
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 Phosphoprotein
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	actin filament Inferred from sequence or structural similarity. Source: UniProtKB 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 protein binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Cobl	Q5NBX1	1	EBI-367540,EBI-1550138	From a different organism.
Dbnl	Q62418	1	EBI-367540,EBI-1550322	From a different organism.
Pacsin1	Q9Z0W5	1	EBI-367540,EBI-1550185	From a different organism.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Propeptide

1 – 2

2

Removed in mature form

PRO_0000000850

Chain

3 – 377

375

Actin, alpha skeletal muscle

PRO_0000000851

Amino acid modifications

Modified residue

3

1

N-acetylaspartate

Modified residue

55

1

Phosphotyrosine By similarity

Modified residue

63

1

N6-acetyllysine By similarity

Modified residue

70

1

N6-acetyllysine By similarity

Modified residue

75

1

Tele-methylhistidine

Modified residue

93

1

Phosphotyrosine By similarity

Modified residue

193

1

N6-acetyllysine By similarity

Modified residue

242

1

Phosphotyrosine By similarity

Modified residue

328

1

N6-acetyllysine By similarity

Modified residue

330

1

N6-acetyllysine By similarity

Secondary structure

1

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377

Helix Strand Turn

Details...

Beta strand

10 – 14

5

Beta strand

16 – 23

8

Beta strand

30 – 34

5

Beta strand

37 – 39

3

Helix

58 – 61

4

Beta strand

65 – 70

6

Beta strand

72 – 74

3

Helix

81 – 93

13

Helix

100 – 102

3

Beta strand

105 – 109

5

Helix

115 – 127

13

Beta strand

132 – 138

7

Helix

139 – 146

8

Beta strand

150 – 157

8

Beta strand

162 – 168

7

Helix

174 – 176

3

Beta strand

178 – 181

4

Helix

184 – 197

14

Helix

205 – 218

14

Helix

225 – 234

10

Beta strand

240 – 243

4

Beta strand

249 – 253

5

Helix

255 – 261

7

Turn

262 – 264

3

Helix

266 – 269

4

Helix

276 – 286

11

Helix

289 – 291

3

Helix

292 – 296

5

Beta strand

299 – 303

5

Helix

304 – 306

3

Helix

311 – 322

12

Turn

335 – 338

4

Helix

340 – 350

11

Helix

352 – 357

6

Beta strand

358 – 360

3

Helix

361 – 367

7

Helix

369 – 371

3

Helix

372 – 375

4

Sequences

	Sequence		Length	Mass (Da)
	P68135-1 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: DF2A3A046346A179	FASTA	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 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

V00872 mRNA. Translation: CAA24241.1.
V00873 mRNA. Translation: CAA24242.1.
V00874 mRNA. Translation: CAA24243.1.

PIR

ATRB. A92182.
I46471.
I46472.
I46473.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ALM	model	-	V/W/X/Y/Z	3-374	[»]
1ATN	X-ray	2.80	A	3-374	[»]
1EQY	X-ray	2.30	A	1-377	[»]
1ESV	X-ray	2.00	A	1-377	[»]
1H1V	X-ray	3.00	A	3-377	[»]
1IJJ	X-ray	2.85	A/B	1-377	[»]
1J6Z	X-ray	1.54	A	4-377	[»]
1KXP	X-ray	2.10	A	3-377	[»]
1LCU	X-ray	3.50	A/B	7-377	[»]
1LOT	X-ray	2.50	B	3-377	[»]
1M8Q	electron microscopy	70.00	0/1/2/3/4/5/7/8/9/V/W/X/Y/Z	3-377	[»]
1MA9	X-ray	2.40	B	8-372	[»]
1MVW	electron microscopy	70.00	1/2/3/4/5/6/7/8/9/V/W/X/Y/Z	3-377	[»]
1NWK	X-ray	1.85	A	3-377	[»]
1O18	electron microscopy	70.00	1/2/3/4/5/6/7/8/9/V/W/X/Y/Z	3-377	[»]
1O19	electron microscopy	70.00	1/2/3/4/5/6/7/8/9/V/W/X/Y/Z	3-377	[»]
1O1A	electron microscopy	70.00	1/2/3/4/5/6/7/8/9/V/W/X/Y/Z	3-377	[»]
1O1B	electron microscopy	70.00	0/1/2/3/4/5/7/8/9/V/W/X/Y/Z	3-377	[»]
1O1C	electron microscopy	70.00	0/1/2/3/4/5/7/8/9/V/W/X/Y/Z	3-377	[»]
1O1D	electron microscopy	70.00	0/1/2/3/4/5/7/8/9/V/W/X/Y/Z	3-377	[»]
1O1E	electron microscopy	70.00	1/2/3/4/5/6/7/8/9/V/W/X/Y/Z	3-377	[»]
1O1F	electron microscopy	70.00	0/1/2/3/4/5/6/7/8/V/W/X/Y/Z	3-377	[»]
1O1G	electron microscopy	70.00	1/2/3/4/5/6/7/8/9/V/W/X/Y/Z	3-377	[»]
1P8Z	X-ray	2.60	A	1-377	[»]
1QZ5	X-ray	1.45	A	3-377	[»]
1QZ6	X-ray	1.60	A	3-377	[»]
1RDW	X-ray	2.30	X	3-377	[»]
1RFQ	X-ray	3.00	A/B	3-377	[»]
1RGI	X-ray	3.00	A	1-377	[»]
1S22	X-ray	1.60	A	3-375	[»]
1SQK	X-ray	2.50	A	1-377	[»]
1T44	X-ray	2.00	A	8-377	[»]
1UY5	model	-	A	3-374	[»]
1WUA	X-ray	1.45	A	3-377	[»]
1Y64	X-ray	3.05	A	3-377	[»]
1YXQ	X-ray	2.01	A/B	3-377	[»]
2A3Z	X-ray	2.08	A	3-377	[»]
2A40	X-ray	1.80	A/D	3-377	[»]
2A41	X-ray	2.60	A	3-377	[»]
2A42	X-ray	1.85	A	3-377	[»]
2A5X	X-ray	2.49	A	3-377	[»]
2ASM	X-ray	1.60	A	3-377	[»]
2ASO	X-ray	1.70	A	3-377	[»]
2ASP	X-ray	1.64	A	3-377	[»]
2D1K	X-ray	2.50	A	3-377	[»]
2FF3	X-ray	2.00	B	3-377	[»]
2FF6	X-ray	2.05	A	3-377	[»]
2FXU	X-ray	1.35	A	3-377	[»]
2GWJ	X-ray	1.90	A	7-377	[»]
2GWK	X-ray	2.00	A/B	7-377	[»]
2HMP	X-ray	1.90	A/B	3-377	[»]
2PAV	X-ray	1.80	A	3-377	[»]
2PBD	X-ray	1.50	A	1-377	[»]
2Q0R	X-ray	1.70	A	3-377	[»]
2Q0U	X-ray	1.45	A	3-377	[»]
2Q1N	X-ray	2.70	A/B	3-377	[»]
2Q31	X-ray	2.70	A/B	3-377	[»]
2Q36	X-ray	2.50	A	3-377	[»]
2Q97	X-ray	2.50	A	3-377	[»]
2V51	X-ray	2.35	B/D	1-377	[»]
2V52	X-ray	1.45	B	1-377	[»]
2VCP	X-ray	3.20	A/B	3-377	[»]
2VYP	X-ray	2.35	A/B	1-377	[»]
2ZWH	fiber diffraction	3.30	A	3-377	[»]
3B5U	electron microscopy	-	A/B/C/D/E/F/G/H/I/J/K/L/M/N	1-377	[»]
3BUZ	X-ray	2.81	B	3-377	[»]
3CJB	X-ray	3.21	A	1-377	[»]
3CJC	X-ray	3.90	A	1-377	[»]
3DAW	X-ray	2.55	A	1-377	[»]
3FFK	X-ray	3.00	B/E	1-377	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29021N.

IntAct

P68135. 4 interactions.

STRING

P68135.

Genome annotation databases

Ensembl

ENSOCUT00000004074; ENSOCUP00000003527; ENSOCUG00000004074; Oryctolagus cuniculus. [Genome view]

Phylogenomic databases

HOVERGEN

P68135.

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

Search...

Entry information

Entry name

ACTS_RABIT

Accession

Primary (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 15, 2009
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)